<p>The invitation to give plenary lecture was accepted by:</p>
<ul>
<li><strong>Karl Mechtler</strong> (Research Institute of Molecular Pathology, Vienna)</li>
<li><strong>Carlos Cordeiro</strong> (Universidade de Lisboa)</li>
<li><strong>Berndt Wollscheid</strong> (ETH Zurich)</li>
</ul>
<h3><strong>Program CEEPC/IPM/CMSC 2022</strong></h3>
<blockquote>
<p><a href="https://lcms.labrulez.com/labrulez-bucket-strapi-h3hsga3/abstractbook_2022_3bec805e4e/abstractbook_2022.pdf"><strong>Complete program including abstracts for download</strong></a></p>
</blockquote>
<h3><strong>Thursday September 29, 2022</strong></h3>
<h5><strong>8:30 - 10:00 Registration</strong></h5>
<h5><strong>10:00 - 10:10 Opening of the 16th CEEPC, 8th IPM and 10th CMSC</strong></h5>
<h4><strong>10:10 - 11:00 Plenary lecture I: New insights through Single-Cell Proteomics</strong> (Chairperson: Petr Novák)</h4>
<ul>
<li>Karl Mechtler</li>
</ul>
<h5><strong>11:00 - 11:20 Coffee break</strong></h5>
<h4><strong>11:20 - 13:00 Session I - Method Development</strong></h4>
<ul>
<li>Chairperson: Katarina Davalieva</li>
</ul>
<h5><strong>11:20 - 11:40 Identification of potential cell-surface targets and druggable enzymes in human pheochromocytoma and paraganglioma using classical and membrane-targeting proteomic approaches</strong></h5>
<ul>
<li>Ondřej Vít</li>
</ul>
<h5><strong>11:40 - 12:00 Global SEC-PCP-SILAC mapping reveals protein complexes mediating NF-κB activation in breast cancer</strong></h5>
<ul>
<li>Petr Lapčík</li>
</ul>
<h5><strong>12:00 - 12:20 Determination of changes in the milk proteome in production and storage of kefir using mass spectrometry-based omics approaches</strong></h5>
<ul>
<li>Haci Mehmet Kayili</li>
</ul>
<h5><strong>12:20 - 12:40 Non-Immunoaffinity Extraction of Intact Proteins from Biological Fluids and Their Analysis by Liquid Chromatography – Triple Quadrupole Mass Spectrometry</strong></h5>
<ul>
<li>Katarína Maráková</li>
</ul>
<h5><strong>12:40 - 13:00 Advancing Cyclic Ion Mobility Mass Spectrometry Methods for Studying Biomolecules: Towards the Conformational Dynamics of Mega Dalton Protein Aggregates</strong></h5>
<ul>
<li>Adam Pruška</li>
</ul>
<h5><strong>13:00 - 15:30 Lunch + Poster session I (Odd-numbered posters)</strong></h5>
<h4><strong>15:30 - 16:30 Company Workshop – Bruker Daltonics</strong></h4>
<h5><strong>The latest proteomics development at Bruker</strong></h5>
<ul>
<li>Gary Kruppa</li>
</ul>
<h5><strong>Clinical (phospho)proteomics with TIMS and PASEF</strong></h5>
<ul>
<li>Florian Meier</li>
</ul>
<h5><strong>16:30 - 16:50 Coffee break</strong></h5>
<h4><strong>16:50 - 17:30 Short Talks</strong></h4>
<ul>
<li>Chairperson: Petr Man</li>
</ul>
<h5><strong>Detection of C. difficile Toxin B by biomolecule-modified chips and mass spectrometry</strong></h5>
<ul>
<li>Josef Dvořák</li>
</ul>
<h5><strong>Optimized HDX-MS workflow for antibody structure monitoring by HDX-MS</strong></h5>
<ul>
<li>Zuzana Kalaninová</li>
</ul>
<h5><strong>RPLC-UV and HILIC-UV characterisation of on-site produced Ramucirumab-DTPA immunoconjugate</strong></h5>
<ul>
<li>Denis Naplekov</li>
</ul>
<h5><strong>Collision energy setting in proteomics and glycoproteomics: From individual species to a practical perspective</strong></h5>
<ul>
<li>Agnes Revesz</li>
</ul>
<h5><strong>Novel circulating biomarkers of biventricular heart failure</strong></h5>
<ul>
<li>Matěj Běhounek</li>
</ul>
<h5><strong>Comprehensive metabolomic and lipidomic study of tauopathy and Alzheimer&#39;s disease patients</strong></h5>
<ul>
<li>Dana Dobešová</li>
</ul>
<h5><strong>Overlooked oligomerization process in Azurin, a model metalloprotein</strong></h5>
<ul>
<li>Roman Tuzhilkin</li>
</ul>
<h4><strong>17:30 - 18:00 Josef Chmelik Award</strong></h4>
<h5><strong>18:00 - 19:30 Guided tour to the conference dinner</strong></h5>
<h4><strong>19:30 - 23:00 Conference dinner and sightseeing boat trip</strong></h4>
<blockquote>
<h3><strong>Sponsors</strong></h3>
</blockquote>
<blockquote>
<ul>
<li>Bruker Daltonics</li>
<li>Amedis</li>
<li>Merck</li>
<li>Beckman coulter</li>
<li><a href="https://lcms.cz/companies/42"><strong>Pragolab</strong></a></li>
<li><a href="https://lcms.cz/companies/50"><strong>Waters Corporation</strong></a></li>
</ul>
</blockquote>
<blockquote>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Sponsors_CEEPC_IPM_CMSC_2022_6f46a9b213/CSHS-Sponsors-CEEPC-IPM-CMSC-2022.webp" alt="ČSHS: Sponsors: CEEPC/IPM/CMSC 2022"/></p>
</blockquote>
<h3><strong>Friday September 30, 2022</strong></h3>
<h4><strong>8:50 - 9:40 Plenary lecture II: An FT-ICR-MS metabolomic journey</strong> (Chairperson: Michael Volný)</h4>
<ul>
<li>Carlos Cordeiro</li>
</ul>
<h4><strong>9:40 - 11:20 Session II - Novel Instrumentation and approaches</strong></h4>
<ul>
<li>Chairperson: Lászlo Drahos</li>
</ul>
<h5><strong>9:40 - 10:00 In a flash of light: Native mass spectrometry for single particle imaging with X ray free electron lasers</strong></h5>
<ul>
<li>Alan Kádek</li>
</ul>
<h5><strong>10:00 - 10:20 Qualitative and quantitative advancements of QTOF performance: the SCIEX ZenoTOF 7600 system</strong></h5>
<ul>
<li>Volker Kruft</li>
</ul>
<h5><strong>10:20 - 10:40 Synergistic success of proteo-genomics in profiling human tear fluid for disease biomarkers using a novel high sensitivity Immunoassay</strong></h5>
<ul>
<li>Suresh Jivan Gadher</li>
</ul>
<h5><strong>10:40 - 11:00 Back to Basics with Antibodies</strong></h5>
<ul>
<li>Stanislav Kukla</li>
</ul>
<h5><strong>11:00 - 11:20 Two-dimensional mass spectrometry for top-down analysis and structural characterization of proteins</strong></h5>
<ul>
<li>Maria van Agthoven</li>
</ul>
<h5><strong>11:20 - 11:40 Coffee break</strong></h5>
<h5><strong>11:40 - 13:00 Session Session III - MS and SW tools</strong></h5>
<ul>
<li>Chairperson: Eva Csosz</li>
</ul>
<h5><strong>11:40 - 12:00 Rapid ion mobility-resolved phosphoproteomics with dia-PASEF</strong></h5>
<ul>
<li>Florian Meier</li>
</ul>
<h5><strong>12:00 - 12:20 Prediction of Intact N-Glycopeptide Retention Time Windows in Hydrophilic Interaction Liquid Chromatography</strong></h5>
<ul>
<li>Tomáš Ječmen</li>
</ul>
<h5><strong>12:20 - 12:40 Quantification of small molecules in liquid chromatography/mass spectrometry datasets by CycloBranch</strong></h5>
<ul>
<li>Jiří Novák</li>
</ul>
<h5><strong>12:40 - 13:00 Mass spectrometric analysis of intact proteins: the dark side of deconvolution</strong></h5>
<ul>
<li>Lászlo Drahos</li>
</ul>
<h5><strong>13:00 - 15:30 Lunch + Poster session II (Even-numbered posters)</strong></h5>
<h4><strong>15:30 - 17:30 Session IV - Applications in Biomedicine 1</strong></h4>
<ul>
<li>Chairperson: Maria van Agthoven</li>
</ul>
<h5><strong>15:30 - 15:50 Identification of potential biomarkers for azoospermia by human testis proteomic analysis</strong></h5>
<ul>
<li>Katarina Davalieva</li>
</ul>
<h5><strong>15:50 - 16:10 Proteotype classification of renal cell carcinoma for prognosis and therapy response</strong></h5>
<ul>
<li>Pavel Bouchal</li>
</ul>
<h5><strong>16:10 - 16:30 Stability Study of Triacetylfusarinine C and Gliotoxin in bodily fluids</strong></h5>
<ul>
<li>Jiří Houšť</li>
</ul>
<h5><strong>16:30 - 16:50 MALDI-TOF mass spectrometry: A powerful method for blood meal identification in insect vectors</strong></h5>
<ul>
<li>Petr Halada</li>
</ul>
<h5><strong>16:50 - 17:10 Characterization of glycosphingolipids in iPSC-derived cerebral organoids and its application in neurodegenerative disorders</strong></h5>
<ul>
<li>Durga Jha</li>
</ul>
<h5><strong>17:10 - 17:30 Redox resetting by modulation of redox sensor Kelch-like ECH-associated protein 1 restores leukemic cells sensitivity to Azacytidine</strong></h5>
<ul>
<li>Kristýna Pimková</li>
</ul>
<h4><strong>17:30 - 18:10 <a href="https://lcms.cz/articles?search=zdenek+herman">Zdeněk Herman</a> Award presented by Resonance Foundation and presentation of the winning thesis</strong></h4>
<h5><strong>18:10 - 18:30 Coffee break</strong></h5>
<h4><strong>18:30 - 19:00 General assembly of the CSMS</strong></h4>
<h3><strong>Saturday October 1, 2022</strong></h3>
<h4><strong>8:50 - 10:50 Session V - Applications in Biomedicine 2</strong></h4>
<ul>
<li>Chairperson: Haci Mehmet Kayili</li>
</ul>
<h5><strong>8:50-9:10 Proteomic Analysis of Hepatitis B Virus</strong></h5>
<ul>
<li>Martin Hubálek</li>
</ul>
<h5><strong>9:10-9:30 The single amino acid substitutions in Mason-Pfizer Monkey Virus matrix protein modulate its proteolytic cleavage rate</strong></h5>
<ul>
<li>Jakub Sýs</li>
</ul>
<h5><strong>9:30-9:50 Cardiac alarmins as residual risk markers of atherosclerosis under lipid-lowering therapy</strong></h5>
<ul>
<li>Viorel-Iulian Suica</li>
</ul>
<h5><strong>9:50-10:10 Cervical mucus – a non-invasive uterine biomarker source?</strong></h5>
<ul>
<li>Tomáš Oždian</li>
</ul>
<h5><strong>10:10-10:30 High-Throughput µLC-MS/MS Lipidomics of 3D In Vitro Disease Models to Investigate Lipid Dysregulation</strong></h5>
<ul>
<li>Darshak Gadara</li>
</ul>
<h5><strong>10:30-10:50 Multi-omics network analysis in atherosclerosis reveals mechanisms driving the progression towords complicated lesion</strong></h5>
<ul>
<li>Eva Csosz</li>
</ul>
<h5><strong>10:50 - 11:10 Coffee break</strong></h5>
<h4><strong>11:10 - 12:00 Plenary lecture III: Light-mediated discovery of surfaceome nanoscale organization and inter-cellular receptor interaction networks</strong> (Chairperson: Pavel Bouchal)</h4>
<ul>
<li>Bernd Wollscheid</li>
</ul>
<h4><strong>12:00 - 12:20 Poster prize, Closing remarks</strong></h4>
<h5><strong>12:20 - 13:30 Lunch</strong></h5>


Conference CEEPC/IPM/CMSC 2022 (Program)

<h3><strong>Program CEEPC/IPM/CMSC 2022</strong></h3>
<blockquote>
<p><a href="https://lcms.labrulez.com/labrulez-bucket-strapi-h3hsga3/abstractbook_2022_3bec805e4e/abstractbook_2022.pdf"><strong>Complete program including abstracts for download</strong></a></p>
</blockquote>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Konference_CEEPC_IPM_CMSC_2022_Suresh_Jivan_Gadher_cb291006b9/CSHS-Konference-CEEPC-IPM-CMSC-2022-(Suresh-Jivan-Gadher).webp" alt="CSMS: Conference CEEPC/IPM/CMSC 2022 (Suresh Jivan Gadher)"/></p>
<h3><strong>Thursday September 29, 2022</strong></h3>
<h5><strong>8:30 - 10:00 Registration</strong></h5>
<h5><strong>10:00 - 10:10 Opening of the 16th CEEPC, 8th IPM and 10th CMSC</strong></h5>
<h4><strong>10:10 - 11:00 Plenary lecture I: New insights through Single-Cell Proteomics</strong> (Chairperson: Petr Novák)</h4>
<ul>
<li>Karl Mechtler</li>
</ul>
<p>The analysis of single cell proteomes has recently become a viable complement to transcriptomics and genomics studies. Proteins are the main driver of cellular functionality and mRNA levels are often an unreliable proxy of such. Therefore, the global analysis of the proteome is essential to study cellular identities. Both multiplexed and label-free mass spectrometry-based approaches with single cell resolution have lately attributed surprising heterogeneity to believed homogenous cell populations. Even though specialized experimental designs and instrumentation have demonstrated remarkable advances, the efficient sample preparation of single cells still lacks behind.</p>
<p>Here, we introduce the proteoCHIP, optimized for multiplexed single cell proteomics sample preparation at surprising sensitivity and throughput. Sample processing using the cellenONE® robot, allows to reduce final sample volumes to low nanoliters submerged in a hexadecane layer simultaneously eliminating error prone manual sample handling and overcoming evaporation. This results in around 1,500 protein groups per analytical run at remarkable reporter ion signal to noise while reducing or eliminating the carrier proteome. We identified close to 2,600 proteins across 170 multiplexed single cells from two highly similar human cell types. This dedicated loss-less workflow allows to distinguish in vitro co-differentiated cell types of self-organizing cardiac organoids based on indicative markers across 150 single cells. In-depth characterization revealed enhanced cellular motility of endothelial cells and acute myocardium sarcomere organization in cardiomyocytes.</p>
<p>In addition, we evolved a robust and sensitive one-pot label free single cell workflow. By working in standard 384 well plates and compatibility with both, cell sorting in the cellenONE® or using alternatives like a FACS device the need for specialized equipment is obsolete making this workflow easy to use, cheap and accessible to a broader community. By keeping the sample in a hydrated state during proteolytic digestion and addition of DMSO for storage we improved recovery of hydrophobic peptides and boosted ID numbers to more than 1000 proteins from a single cell without match between runs.<br/>In conclusion, our versatile, and semi-automated sample preparation workflows have not only proven to be easily adoptable but are also sufficiently sensitive to drive biological applications of single cell proteomics.</p>
<h5><strong>11:00 - 11:20 Coffee break</strong></h5>
<blockquote>
<h3><strong>Sponsors</strong></h3>
</blockquote>
<blockquote>
<ul>
<li>Bruker Daltonics</li>
<li>Amedis</li>
<li>Merck</li>
<li>Beckman coulter</li>
<li><a href="https://lcms.cz/companies/42"><strong>Pragolab</strong></a></li>
<li><a href="https://lcms.cz/companies/50"><strong>Waters Corporation</strong></a></li>
</ul>
</blockquote>
<blockquote>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Sponsors_CEEPC_IPM_CMSC_2022_6f46a9b213/CSHS-Sponsors-CEEPC-IPM-CMSC-2022.webp" alt="CMSC: Sponsors: CEEPC/IPM/CMSC 2022"/></p>
</blockquote>
<h4><strong>11:20 - 13:00 Session I - Method Development</strong></h4>
<ul>
<li>Chairperson: Katarina Davalieva</li>
</ul>
<h5><strong>11:20 - 11:40 Identification of potential cell-surface targets and druggable enzymes in human pheochromocytoma and paraganglioma using classical and membrane-targeting proteomic approaches</strong></h5>
<ul>
<li>Ondřej Vít</li>
</ul>
<p>Integral membrane proteins (IMPs) represent optimal drug targets but are under-represented in standard proteomic analyses due to their amphipathy, lack of trypsin cleavage sites, and low expression levels. To identify tumor-upregualted IMPs and druggable enzymes in rare neuroendocrine tumors – pheochromocytoma and paraganglioma (PPGL), we combined three approaches: 1) hpTC method, where the identification of IMPs is based on their hydrophobic alpha-helices, isolated by proteolytic shaving and re-cleaved with CNBr; 2) two glycocapture methods - lectin entrapment on ultrafilters (N-glyco-FASP), and solid-phase enrichment with hydrazide chemistry (SPEG); and 3) the classical detergent-trypsin approach.<br/>We focused mainly on the high-risk tumors belonging to the so-called cluster 1, characterized by mutations in genes related to citric acid cycle and hypoxia, such as SDHB, VHL, and EPAS1). The classical trypsin-based proteomic approach pointed us toward upregulated soluble druggable enzymes (autotaxin, SHMT2, and Arginase 2) and upregulated cell surface IMPs (including CD146 and CD171). The glycopeptide enrichment approach provided additional potential cell surface targets (CD39), and the hpTC method provided additional IMP targets (e.g., anoctamin-1).<br/>The above-mentioned IMPs and soluble enzymes have all been previously shown to be upregulated in several human cancers and to affect tumor progression directly. Their marked upregulation was confirmed by specific antibodies. Together, this makes these molecules promising candidates for drug targets and/or proteins enabling sensitive tumor imaging.</p>
<h5><strong>11:40 - 12:00 Global SEC-PCP-SILAC mapping reveals protein complexes mediating NF-κB activation in breast cancer</strong></h5>
<ul>
<li>Petr Lapčík</li>
</ul>
<p>NF-κB has essential role in immune response and is associated with lymph node metastasis of luminal A breast tumors (1). Analysis of protein interactome and its changes in response to NF-κB modulation could uncover pro-metastatic mechanisms related to NF-κB. We apply metabolic isotope labeling SILAC, size exclusion chromatography (SEC) and protein correlation profiling (PCP) (2) to construct a network of interactome rearrangement in response to NF-κB modulation in MCF-7 breast cancer cells.</p>
<p>We generated two co-fractionation datasets consisting of 80 fractions from SILAC-labeled and 80 fractions from label-free native MCF-7 lysates with inhibited or native NF-κB activity. LC-MS/MS analysis of SEC fractions using Orbitrap Lumos and Bruker Impact II mass spectrometers quantified 3308 and 5460 protein groups in SILAC and label-free datasets, respectively (FDR = 0.01). Interactome reconstruction using PrinCE (3) detected 7568 interactions among 1520 proteins. Co-elution of subunits of known complexes, such as ribosome, proteasome and MCM, was observed. Modulation of NF-κB was linked to interactome changes of proteins involved in immune response, cell cycle and DNA replication. NF-κB factor RELA interacted with proteins co-eluting with activators of NF-κB and these interactions were modulated by NF-κB inhibition.</p>
<p>Our interaction network represents a complex insight into dynamics of MCF-7 protein interactome associated with NF-κB pathway and could serve as a basis for future studies characterizing NF-κB in breast cancer.</p>
<h5><strong>12:00 - 12:20 Determination of changes in the milk proteome in production and storage of kefir using mass spectrometry-based omics approaches</strong></h5>
<ul>
<li>Haci Mehmet Kayili</li>
</ul>
<p>Kefir is an important food source based in the Caucasus region. The beneficial effects of kefir on human health are indicated in the literature. The mechanisms underlying these critical properties of kefir have not yet been elucidated. This study aims to examine the changes in milk protein profiles during kefir production and storage by using mass spectrometry-based-omics approaches. In addition, the detection of kefir-based proteins that transfer to milk from kefir microflora was investigated within the scope of the study. First, Kefir production was carried out. During the production and storage of kefir, kefir samples were taken from the periods determined in the study, and milk proteins were extracted. Peptides were produced using Lys-C and trypsin enzymes by a classical proteomics approach. Afterward, the fractionation of the peptides was carried out. Peptide-containing samples were analyzed by nLC-QExactive-Plus mass spectrometry. The data obtained as a result of the analysis were processed with the Maxquant software, and statistical analyzes were performed. According to the results obtained, significant changes were found in the milk proteome in 3 proteins between 0-12 hours, 39 proteins between 0-24 hours, 41 proteins between 0-7 days, and finally, 42 proteins between 0-28 days. From the 24th hour, a significant change was observed in 23 proteins. In the analysis, it was determined in the study that 398 kefir-based proteins were released into the milk. It is anticipated that these results will provide valuable contributions to the literature in terms of showing the changes in the milk proteome in kefir production.</p>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Konference_CEEPC_IPM_CMSC_2022_Determination_of_changes_in_the_milk_proteome_in_production_and_storage_of_kefir_using_mass_spectrometry_based_omics_approaches_Haci_Mehmet_Kayili_866576d951/CSHS-Konference-CEEPC-IPM-CMSC-2022-Determination-of-changes-in-the-milk-proteome-in-production-and-storage-of-kefir-using-mass-spectrometry-based-omics-approaches-(Haci-Mehmet-Kayili).webp" alt="CSMS: Conference CEEPC/IPM/CMSC 2022: Determination of changes in the milk proteome in production and storage of kefir using mass spectrometry-based omics approaches (Haci Mehmet Kayili)"/></p>
<h5><strong>12:20 - 12:40 Non-Immunoaffinity Extraction of Intact Proteins from Biological Fluids and Their Analysis by Liquid Chromatography – Triple Quadrupole Mass Spectrometry</strong></h5>
<ul>
<li>Katarína Maráková</li>
</ul>
<p>One of the crucial steps in quantitation of intact proteins from complex biological matrices is, except their reliable analysis, also sample preparation to achieve sufficient specificity and sensitivity. Commonly used immunoaffinity-based methods are characterized by their superior selectivity, although this can be a drawback if simultaneous analysis of multiple different proteins from a single sample is required. In our work, we developed non-immunoaffinity sample preparation based on a generally widely affordable microelution solid phase extraction for eleven model intact proteins (5.5 – 29 kDa) with various isoelectric points (4.5 - 11.3). Extracted intact proteins were analysed by reversed-phase liquid chromatography coupled with a triple quadrupole mass spectrometer operated in a multiple reaction monitoring (MRM) mode. Reversed-phase separations were performed on the Restek wide-pore Viva C4 column, as mobile phases served water and acetonitrile acidified by 0.1% difluoroacetic acid and 0.2% formic acid. The best recoveries for most of the selected proteins were obtained by using the HLB stationary phase. 1% trifluoroacetic acid and 0.2% Triton X-100 were used as efficient pretreatment reagents to release interactions between the proteins and biological matrix. Multiple sample loading was found out to be essential to obtain recoveries &gt;65% in urine for all targeted proteins (up to 30kDa) and &gt;50% in serum/plasma for most of the proteins. Limits of quantitation in biological matrices were in the range 2 - 1200 ng/mL, corresponding to 0.23 - 97.6 nM.</p>
<h5><strong>12:40 - 13:00 Advancing Cyclic Ion Mobility Mass Spectrometry Methods for Studying Biomolecules: Towards the Conformational Dynamics of Mega Dalton Protein Aggregates</strong></h5>
<ul>
<li>Adam Pruška</li>
</ul>
<p>Native mass spectrometry is a powerful tool for the analysis of non-covalent complexes. When coupled with high-resolution ion mobility, this technique can be used to investigate the conformational changes induced in said complexes by different solution or gas-phase conditions. In this study, we describe how a new generation high-resolution ion mobility instrument equipped with a cyclic ion mobility cell can be utilized for the analysis of large biomolecular systems, including temperature-induced protein aggregates of masses greater than 1.5 MDa, as well as a 63 kDa oligonucleotide complex. The effects of and the interplay between the voltages applied to the different components of the cyclic ion mobility spectrometry system on ion transmission and arrival time distribution were demonstrated using biomolecules covering the m/z range 2 000 to 10 000. These data were used to establish a theoretical framework for achieving the best separation on the cyclic ion mobility system. Finally, the cyclic ion mobility mass spectrometer was coupled with a temperature-controlled electrospray ionization source to investigate high-mass protein aggregation. This analysis showed that it was possible to continuously monitor the change in abundance for several conformations of MDa aggregates with increasing temperature. This work significantly increases the range of biomolecules that can be analyzed by both cyclic ion mobility and temperature-controlled electrospray ionization mass spectrometry, providing new possibilities for high-resolution ion mobility analysis.</p>
<h5><strong>13:00 - 15:30 Lunch + Poster session I (Odd-numbered posters)</strong></h5>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Konference_CEEPC_IPM_CMSC_2022_Posterova_sekce_I_Postery_liche_aecf40bb37/CSHS-Konference-CEEPC-IPM-CMSC-2022-Posterova-sekce-I-(Postery-liche).webp" alt="CSMS: Conference CEEPC/IPM/CMSC 2022 Poster session I (Odd-numbered posters)"/></p>
<h4><strong>15:30 - 16:30 Company Workshop – Bruker Daltonics</strong></h4>
<h5><strong>The latest proteomics development at Bruker</strong></h5>
<ul>
<li>Gary Kruppa</li>
</ul>
<h5><strong>Clinical (phospho)proteomics with TIMS and PASEF</strong></h5>
<ul>
<li>Florian Meier</li>
</ul>
<h5><strong>16:30 - 16:50 Coffee break</strong></h5>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Konference_CEEPC_IPM_CMSC_2022_Petr_Novak_a_Michael_Volny_8288df35cd/CSHS-Konference-CEEPC-IPM-CMSC-2022-Petr-Novak-a-Michael-Volny.webp" alt="CSMS: Conference CEEPC/IPM/CMSC 2022: Petr Novák and Michael Volný"/></p>
<h4><strong>16:50 - 17:30 Short Talks</strong></h4>
<ul>
<li>Chairperson: Petr Man</li>
</ul>
<h5><strong>Detection of C. difficile Toxin B by biomolecule-modified chips and mass spectrometry</strong></h5>
<ul>
<li>Josef Dvořák</li>
</ul>
<h5><strong>Optimized HDX-MS workflow for antibody structure monitoring by HDX-MS</strong></h5>
<ul>
<li>Zuzana Kalaninová</li>
</ul>
<h5><strong>RPLC-UV and HILIC-UV characterisation of on-site produced Ramucirumab-DTPA immunoconjugate</strong></h5>
<ul>
<li>Denis Naplekov</li>
</ul>
<h5><strong>Collision energy setting in proteomics and glycoproteomics: From individual species to a practical perspective</strong></h5>
<ul>
<li>Agnes Revesz</li>
</ul>
<h5><strong>Novel circulating biomarkers of biventricular heart failure</strong></h5>
<ul>
<li>Matěj Běhounek</li>
</ul>
<h5><strong>Comprehensive metabolomic and lipidomic study of tauopathy and Alzheimer&#39;s disease patients</strong></h5>
<ul>
<li>Dana Dobešová</li>
</ul>
<h5><strong>Overlooked oligomerization process in Azurin, a model metalloprotein</strong></h5>
<ul>
<li>Roman Tuzhilkin</li>
</ul>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Konference_CEEPC_IPM_CMSC_2022_Den_1_62de462e8b/CSHS-Konference-CEEPC-IPM-CMSC-2022-Den-1.webp" alt="CSMS: Conference CEEPC/IPM/CMSC 2022 Day 1"/></p>
<h4><strong>17:30 - 18:00 Josef Chmelik Award</strong></h4>
<h5><strong>18:00 - 19:30 Guided tour to the conference dinner</strong></h5>
<h4><strong>19:30 - 23:00 Conference dinner and sightseeing boat trip</strong></h4>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Konference_CEEPC_IPM_CMSC_2022_Slavnostni_vecere_a_vylet_na_lodi_249c7c3702/CSHS-Konference-CEEPC-IPM-CMSC-2022-Slavnostni-vecere-a-vylet-na-lodi.webp" alt="CSMS: Conference CEEPC/IPM/CMSC 2022 Conference dinner and sightseeing boat trip"/></p>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Konference_CEEPC_IPM_CMSC_2022_Slavnostni_vecere_a_vylet_na_lodi_3_6452afa91a/CSHS-Konference-CEEPC-IPM-CMSC-2022-Slavnostni-vecere-a-vylet-na-lodi-3.webp" alt="CSMS: Conference CEEPC/IPM/CMSC 2022 Conference dinner and sightseeing boat trip"/></p>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Konference_CEEPC_IPM_CMSC_2022_Slavnostni_vecere_a_vylet_na_lodi_2_42bb7f554d/CSHS-Konference-CEEPC-IPM-CMSC-2022-Slavnostni-vecere-a-vylet-na-lodi-2.webp" alt="CSMS: Conference CEEPC/IPM/CMSC 2022 Conference dinner and sightseeing boat trip"/></p>


Conference CEEPC/IPM/CMSC 2022 (Day 1)

Conference CEEPC/IPM/CMSC 2022 (Day 2)

<h3><strong>Program CEEPC/IPM/CMSC 2022</strong></h3>
<blockquote>
<p><a href="https://lcms.labrulez.com/labrulez-bucket-strapi-h3hsga3/abstractbook_2022_3bec805e4e/abstractbook_2022.pdf"><strong>Complete program including abstracts for download</strong></a></p>
</blockquote>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Konference_CEEPC_IPM_CMSC_2022_2_aa28bf7c17/CSHS-Konference-CEEPC-IPM-CMSC-2022-2.webp" alt="CSMS: Conference CEEPC/IPM/CMSC 2022"/></p>
<h3><strong>Saturday October 1, 2022</strong></h3>
<h4><strong>8:50 - 10:50 Session V – Applications in Biomedicine 2</strong></h4>
<ul>
<li>Chairperson: Haci Mehmet Kayili</li>
</ul>
<h5><strong>8:50-9:10 Proteomic Analysis of Hepatitis B Virus</strong></h5>
<ul>
<li>Martin Hubálek</li>
</ul>
<p>According to the World Health Organisation, an estimated 296 million people worldwide are infected with Hepatitis B virus (HBV). HBV is a small enveloped DNA virus from Hepadnaviridae family that persists in the infected hepatocytes by establishing an episomal covalently closed circular double-stranded DNA (cccDNA) genome containing four open reading frames (C, P, S and X). The ORFs largely overlap and encode multiple proteins using different in-frame start codons. The S ORF encodes three forms of surface envelope glycoproteins S-, M-, and L- HBs). The HBV preC-C gene gives rise to two different products translated from distinct mRNAs – core protein (HBc) and precore protein (HBe). Despite their high sequence similarity, these proteins exhibit different functions and subcellular localizations. The P ORF encodes viral polymerase, and the X ORF encodes regulatory HBx protein.</p>
<p>Mass Spectrometry department of IOCB has established a collaboration with the groups of Iva Pichova and Jan Weber from IOCB. This collaboration on proteomics experiments lead to the discovery of several important biological and biochemical findings including identification of interacting partners of HBc, HBx and HBe proteins or posttranslational modifications of HBc protein. The collaboration resulted in several publications. The proteomic analysis of individually expressed viral proteins has also captured out-of-frame products suggesting the possibility of frameshift or alternative internal initiation of translation. The presentation will highlight the proteomic analyses of HBV at IOCB</p>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Konference_CEEPC_IPM_CMSC_2022_Proteomic_Analysis_of_Hepatitis_B_Virus_Martin_Hubalek_a95dd6216f/CSHS-Konference-CEEPC-IPM-CMSC-2022-Proteomic-Analysis-of-Hepatitis-B-Virus-(Martin-Hubalek).webp" alt="CSMS: Conference CEEPC/IPM/CMSC 2022: Proteomic Analysis of Hepatitis B Virus (Martin Hubálek)"/></p>
<h5><strong>9:10-9:30 The single amino acid substitutions in Mason-Pfizer Monkey Virus matrix protein modulate its proteolytic cleavage rate</strong></h5>
<ul>
<li>Jakub Sýs</li>
</ul>
<p>N-terminal domain of polyprotein Gag of Mason-Pfizer Monkey Virus (M-PMV) Matrix protein (MA) is naturally myristoylated on its N-terminus. When MA is a part of polyprotein Gag, the myristate moiety is buried inside hydrophobic pocket and exposed probably upon interaction with host cell plasma membrane (PM). This mechanism called myristoyl switch does not occur in M-PMV as readily as it does in HIV-1, suggesting that it may have an important role in M-PMV maturation by regulating the MA cleavage from Gag polyprotein.</p>
<p>To address this hypothesis, we have treated the myristoylated (myrMAPPHis) and nonmyristoylated MAPPHis (nonmyrMAPPHis) M PMV construct, bearing the cleavage site for M-PMV viral protease (Pr13), on artificial liposomes mimicking PM by Pr13 for several time points. In contrast to rapidly degraded nonmyrMAPPHis even without liposomes, the myrMAPPHis, surprisingly, become cleaved more frequently only after addition of liposomes indicating the possible exposure of myristate upon interaction with PM.</p>
<p>To support our findings, we have designed and examined also four mutants of MAPPHis M PMV with single amino acid substitutions with expectation to block or, conversely, facilitate the myristoyl switch by stabilization (A79V, A79L) or destabilization (I51A, I86A) of MA M PMV hydrophobic pocket. The mutants A79V and A79L were cleaved even less effectively than myrMAPPHis as well as the degradation of mutants I51A and I86A was faster compared to nonmyrMAPPHis. The different cleavage rates of proteins were confirmed also on structural level by using method of hydrogendeuterium exchange coupled with mass spectrometric detection. It shows that the protease cleavage site has different dynamics in proteins as a result of disruption/stabilisation of hydrophobic pocket.</p>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Konference_CEEPC_IPM_CMSC_2022_The_single_amino_acid_substitutions_in_Mason_Pfizer_Monkey_Virus_matrix_protein_modulate_its_proteolytic_cleavage_rate_Jakub_Sys_e300792938/CSHS-Konference-CEEPC-IPM-CMSC-2022-The-single-amino-acid-substitutions-in-Mason-Pfizer-Monkey-Virus-matrix-protein-modulate-its-proteolytic-cleavage-rate-(Jakub-Sys).webp" alt="CSMS: Conference CEEPC/IPM/CMSC 2022: The single amino acid substitutions in Mason-Pfizer Monkey Virus matrix protein modulate its proteolytic cleavage rate (Jakub Sýs)"/></p>
<h5><strong>9:30-9:50 Cardiac alarmins as residual risk markers of atherosclerosis under lipid-lowering therapy</strong></h5>
<ul>
<li>Viorel-Iulian Suica</li>
</ul>
<p>Background: The major cause in the initiation and progression of atherosclerosis are the high levels of low-density lipoproteins. Although statin treatment can effectively lower these levels, there is still a residual risk of cardiovascular events. We hypothesize that a specific panel of alarmins, a family of stress-sensing molecules, could indicate the persistence of silent atherosclerosis residual risk. </p>
<p>Methods: New Zeeland White rabbits were divided into: the control group (C) with standard diet, a group which received a high-fat diet for 12 weeks (Au) and a treated hyperlipidemic group, with a lipid diet for 8 weeks followed by standard diet and hypolipidemic treatment (atorvastatin and PCSK9 siRNA-inhibitor) for 4 weeks (Asi). We used the LTQ Orbitrap Velos Pro mass spectrometer to analyse the left ventricle lysates. The experiments were complemented by immunologic and genomic assays to corroborate the data.</p>
<p>Results: The hyperlipidemic diet determined a general alarmin up-regulation tendency over C group. A significant spectral abundance increase was measured for specific heat shock proteins, S100 family members, HMGB1 and Annexin A1. The hypolipidemic treatment demonstrated a reversed regulation trend, with non-significant spectral alteration over the C group for some identified alarmins.</p>
<p>Conclusion: Our study highlights the discriminating potential of alarmins in hyperlipidemia or following a hypolipidemic treatment.</p>
<h5><strong>9:50-10:10 Cervical mucus – a non-invasive uterine biomarker source?</strong></h5>
<ul>
<li>Tomáš Oždian</li>
</ul>
<p>Cervical mucus (CM) is a viscous fluid produced by cervical glands located in the myometrium of the uterine cervix. Usually, CM forms a plug between vagina and uterus. During the ovulation, CM starts to be more fluidic to allow the sperm to go through. During the ovulation, there is a good window for non-invasive sampling of the CM, originating from uterine derived tissues. The main hypothesis for CM proteomic study is to develop a method for CM sampling, processing and to answer if there are enough proteins in the CM for potential biomarker search. The resulting protocol consists of mucus dissolution, multi-enzyme digestion, and LC-MS proteomic analysis. The optimized approach allows to identify more than thousand proteins from every sample tested. The bioinformatic analysis reveals that the identified proteins are both intra and extra cellular and discovers the proteins with enriched expression in the broader female reproductive tract. To our best knowledge, we provide the most extensive proteomic characterization available.</p>
<h5><strong>10:10-10:30 High-Throughput µLC-MS/MS Lipidomics of 3D In Vitro Disease Models to Investigate Lipid Dysregulation</strong></h5>
<ul>
<li>Darshak Gadara</li>
</ul>
<p>Microflow liquid chromatography interfaced with mass spectrometry is increasingly applied for the high-throughput profiling of biological samples, as it demonstrated an acceptable tradeoff between sensitivity and reproducibility. However, a limited number of applications developed in lipidomics. This study introduces a robust, sensitive, and high-throughput μLC-MS/MS lipidomics workflow, applied in a differential lipidome study of APOE 3 and 4 phenotypes in iPSC-derived cerebral organoids (CO). First, we optimized the microbore column gradient conditions, injecting a mixture of 15 lipid standards on the UHPLC system coupled to a 6469 QQQ. Our μLC-MS/MS method allows quantitation of 351 lipid species from the single CO. The microflow lipidomics shows an average 3.7-fold increase in response compared to a conventional high-flow method. To benchmark the quantitative performance, 303 samples were acquired over 75 hours. The median coefficient of variation (CV) of 351 lipid species was 12.95%, only 26 lipid species show CV higher than 30%. We demonstrated that microflow separation coupled to three-stage quadruple MS substantially increases the sensitivity and allows for robust multiplexed lipid profiling (including cholesterol determination) in a single cerebral organoid. As a proof of concept, lipidomics analysis was performed for the lipid extract of APOE 3/3 and APOE 4/4 (n=10) CO samples. To our knowledge, this is the first systematic report to demonstrate the microflow LC-MS/MS allows for sensitive, high-throughput, and robust measurement of global lipidome, opening an avenue for routine application of microflow separation in the field of lipidomics.</p>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Konference_CEEPC_IPM_CMSC_2022_High_Throughput_LC_MS_MS_Lipidomics_of_3_D_In_Vitro_Disease_Models_to_Investigate_Lipid_Dysregulation_Darshak_Gadara_0935fe540d/CSHS-Konference-CEEPC-IPM-CMSC-2022-High-Throughput-LC-MS-MS-Lipidomics-of-3D-In-Vitro-Disease-Models-to-Investigate-Lipid-Dysregulation-(Darshak-Gadara).webp" alt="CSMS: Conference CEEPC/IPM/CMSC 2022: High-Throughput µLC-MS-MS Lipidomics of 3D In Vitro Disease Models to Investigate Lipid Dysregulation (Darshak Gadara)"/></p>
<h5><strong>10:30-10:50 Multi-omics network analysis in atherosclerosis reveals mechanisms driving the progression towords complicated lesion</strong></h5>
<ul>
<li>Eva Csosz</li>
</ul>
<p>From a biological point of view, it is crucial to understand the mechanisms laying behind atherosclerosis and its complicated forms. In the process of atherosclerosis, first, an atheromatous plaque builds up, which in some conditions can lead to the appearance of complicated lesions. The complicated lesion is characterized by ruptures on the atherosclerotic plaque surface and/or hemorrhage into the plaque. According to the WHO, hemorrhaged lesions, contribute to a considerable extent of deaths worldwide.</p>
<p>The main goal of our project was to perform a multi-omics study involving transcriptomics and proteomics data to get more insights into the pathophysiological processes dominating the complicated lesions.</p>
<p>Transcriptomic (RNAseq) and proteomic (label-free quantification) data were obtained by the analysis of artery samples originating from healthy arteries, atheromatous lesions, and complicated lesions. Both data types were examined separately by Ingenuity Pathway Analysis and later an overlay of the networks was achieved.</p>
<p>120 differentially expressed (DE) proteins and more than 4000 DE genes were detected. The deep analysis of the data could identify the proteins and transcripts characteristic of the complicated lesions and could reveal the pathways specific to atheroma and complicated lesions, respectively. The DE genes were arranged into 25 networks, while the DE proteins were into 12 networks. The lower number of DE proteins compared to the number of DE genes did not result in loss of information, indicating the power of the proteomics experiments. In spite of providing a lower number of DE items, the biological information achievable from proteomics experiments has equal value compared to transcriptomics data.</p>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Konference_CEEPC_IPM_CMSC_2022_Multi_omics_network_analysis_in_atherosclerosis_reveals_mechanisms_driving_the_progression_towords_complicated_lesion_Eva_Csosz_aa54a2b04f/CSHS-Konference-CEEPC-IPM-CMSC-2022-Multi-omics-network-analysis-in-atherosclerosis-reveals-mechanisms-driving-the-progression-towords-complicated-lesion-(Eva-Csosz).webp" alt="CSMS: Conference CEEPC/IPM/CMSC 2022: Multi-omics network analysis in atherosclerosis reveals mechanisms driving the progression towords complicated lesion (Eva Csosz)"/></p>
<h5><strong>10:50 - 11:10 Coffee break</strong></h5>
<h4><strong>11:10 - 12:00 Plenary lecture III:: Light-mediated discovery of surfaceome nanoscale organization and inter-cellular receptor interaction networks</strong> (Chairperson: Pavel Bouchal)</h4>
<ul>
<li>Bernd Wollscheid</li>
</ul>
<p>The molecular nanoscale organization of the surfaceome is a fundamental regulator of cellular signaling in health and disease. Technologies for mapping the spatial relationships of cell surface receptors and their extracellular signaling synapses would unlock theranostic opportunities to target protein communities and the possibility to engineer extracellular signaling. Here, we develop an optoproteomic technology termed LUX-MS that enables the targeted elucidation of acute protein interactions on and in between living cells using light-controlled singlet oxygen generators (SOG). By using SOG-coupled antibodies, small molecule drugs, biologics and intact viral particles, we demonstrate the ability of LUX-MS to decode ligand receptor interactions across organisms and to discover surfaceome receptor nanoscale organization with direct implications for drug action. Furthermore, by coupling SOG to antigens we achieved light-controlled molecular mapping of intercellular signaling within functional immune synapses between antigen-presenting cells and CD8⁺ T cells providing insights into T cell activation with spatiotemporal specificity. LUX-MS based decoding of surfaceome signaling architectures thereby provides a molecular framework for the rational development of theranostic strategies.</p>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Konference_CEEPC_IPM_CMSC_2022_Light_mediated_discovery_of_surfaceome_nanoscale_organization_and_inter_cellular_receptor_interaction_networks_Bernd_Wollscheid_019214ab5c/CSHS-Konference-CEEPC-IPM-CMSC-2022-Light-mediated-discovery-of-surfaceome-nanoscale-organization-and-inter-cellular-receptor-interaction-networks-(Bernd-Wollscheid).webp" alt="CSMS: Conference CEEPC/IPM/CMSC 2022: Light-mediated discovery of surfaceome nanoscale organization and inter-cellular receptor interaction networks (Bernd Wollscheid)"/></p>
<h4><strong>12:00 - 12:20 Poster prize, Closing remarks</strong></h4>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Predavani_oceneni_konference_CEEPC_IPM_CMSC_2022_Ales_Kvasnicka_a_Michael_Volny_4c0967dd3b/CSHS-Predavani-oceneni-konference-CEEPC-IPM-CMSC-2022-(Ales-Kvasnicka-a-Michael-Volny).webp" alt="ČSHS: Conference prize CEEPC/IPM/CMSC 2022 (Aleš Kvasnička a Michael Volný)"/></p>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Eu_PA_cestovni_granty_Nejlepsi_kratke_sdeleni_Kalaninova_Zuzana_a_Eva_Csosz_ef6a262eae/CSHS-EuPA-cestovni-granty-Nejlepsi-kratke-sdeleni-(Kalaninova-Zuzana-a-Eva-Csosz).webp" alt="ČSHS: EuPA travel grants: Short talk prize CEEPC/IPM/CMSC 2022 (Kalaninová Zuzana a Eva Csosz)"/></p>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Vyhlaseni_nejlepsiho_posteru_Konference_CEEPC_IPM_CMSC_2022_Anton_Skriba_a_Michael_Volny_0010fccaaa/CSHS-Vyhlaseni-nejlepsiho-posteru-Konference-CEEPC-IPM-CMSC-2022-(Anton-Skriba-a-Michael-Volny).webp" alt="ČSHS: Poster prize CEEPC/IPM/CMSC 2022 (Anton Škríba a Michael Volný)"/></p>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Eu_PA_cestovni_granty_Nejlepsi_poster_Jadeja_Siddharth_a_Eva_Csosz_dac2e7c761/CSHS-EuPA-cestovni-granty-Nejlepsi-poster-(Jadeja-Siddharth-a-Eva-Csosz).webp" alt="ČSHS: EuPA travel grants: Poster prize CEEPC/IPM/CMSC 2022 (Jadeja Siddharth a Eva Csosz)"/></p>
<h5><strong>12:20 - 13:30 Lunch</strong></h5>
<p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CSHS_Konference_CEEPC_IPM_CMSC_2022_Obcerstveni_44ad451fcc/CSHS-Konference-CEEPC-IPM-CMSC-2022-Obcerstveni.webp" alt="CSMS: Conference CEEPC/IPM/CMSC 2022: Coffe break"/></p>


Conference CEEPC/IPM/CMSC 2022 (Day 3)

11th Conference of the Czech Society for Mass Spectrometry (Day 1)

11th Conference of the Czech Society for Mass Spectrometry (Day 2)

11th Conference of the Czech Society for Mass Spectrometry (Day 3)

<p><strong>Thirteenth annual Conference of the Czech Society for Mass Spectrometry will take place together with the eleventh Informal Proteomic Meeting from November 19 – November 21, 2025 in České Budějovice.</strong></p><h3><strong>Registration</strong></h3><blockquote><ul><li><strong>Free on-line registration:</strong> Saturday, <strong>March 22 </strong>till Monday, <strong>November 3, 2025</strong></li><li><strong>On-site registration will be available for CZK 2500.</strong></li></ul></blockquote><h3><strong>Program</strong></h3><h4><strong>Wednesday November 19, 2025</strong></h4><h5><strong>10:00 - 18:00 Registration</strong></h5><h5><strong>12:45 - 13:45 &nbsp;</strong>Lunch – Canteen, Biology Centre CAS</h5><h5><strong>13:45 - 14:00 Conference Opening</strong></h5><h5><strong>14:00 - 15:00 Plenary Lecture I: Prof. Alexander Makarov (Thermo Fisher Scientific)&nbsp;</strong></h5><h5><strong>15:00 - 16:00 Session I&nbsp;</strong></h5><h5><strong>15:00 - 15:20 </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=8123077"><strong>WeO-01</strong></a><strong>: Towards MS-guided Precision Environmental Health: the Czech node of the European Research Infrastructure for Human Exposome Research</strong></h5><ul><li>Elliott James Price</li></ul><h5><strong>15:20 - 15:40 </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=3900926"><strong>WeO-02</strong></a><strong>: Optimization of microflow LC-MS method by design of experiments and its application to proteomics analysis</strong></h5><ul><li>Urban Jiří</li></ul><h5><strong>15:40 - 16:00 </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=5590880"><strong>WeO-03</strong></a><strong>: Simultaneous mapping of peptides and released N-glycans by HILIC-FLD-MS for quality control of protein biopharmaceuticals</strong></h5><ul><li>Starovoit Mykyta</li></ul><h5><strong>16:00 - 16:30 Coffee Break</strong></h5><h5><strong>16:30 - 16:50 Sponsor Lecture – </strong><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/companies/51"><strong>Phenomenex</strong></a></h5><h5><strong>16:50 - 18:10 Session II</strong></h5><h5><strong>16:50 - 17:10 </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=7077801"><strong>WeO-04</strong></a><strong>: G-quadruplex – ligand interaction biophysics explored by native mass spectrometry and trapped ion mobility spectrometry</strong></h5><ul><li>Melikov Aleksandr</li></ul><h5><strong>16:50 - 17:10 </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=4284116"><strong>WeO-05</strong></a><strong>: Insights into CyRepA2 primase-helicase-DNA interactions using structural mass spectrometry</strong></h5><ul><li>Smrčka Tomáš</li></ul><h5><strong>16:50 - 17:10 </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=6642100"><strong>WeO-06</strong></a><strong>: Breaking the Unbreakable: Structural Elucidation of the Hypermodified RiPP Nostatin A by IRMPD Mass Spectrometry</strong></h5><ul><li>Hájek Jan</li></ul><h5><strong>16:50 - 17:10 </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=4468653"><strong>WeO-07</strong></a><strong>: Unraveling Oligomerization-Mediated Inhibition in GGPPS by Structural Mass Spectrometry</strong></h5><ul><li>Portašiková Jasmína</li></ul><h5><strong>18:10 - 18:30 Sponsor Lecture – Genetica</strong></h5><h5><strong>18:30 - 19:00 Flash Talks I</strong></h5><h5><strong>Quantification of Oxoacids of the Human Metabolome using Liquid Chromatography-Mass Spectrometry </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=4124815"><strong>(WeS-01)</strong></a></h5><ul><li>Hebesberger Philipp</li></ul><h5><strong>Analyses of human scent samples </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=9840543"><strong>(WeS-02)</strong></a></h5><ul><li>Škeříková Veronika</li></ul><h5><strong>rDUVLAESCI-MS/MSI: a novel approach for direct analysis of biological surfaces </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=5983681"><strong>(WeS-03)</strong></a></h5><ul><li>Grepl Jakub</li></ul><h5><strong>Investigation of phenolic compounds in grape pomace through UHPLC-ESI-MS/MS </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=8595826"><strong>(WeS-04)</strong></a></h5><ul><li>Jágr Michal</li></ul><h5><strong>Mass Spectral Library Network (MERLIN) To Streamline The Generation Of Public Spectral Libraries </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=7046316"><strong>(WeS-05)</strong></a></h5><ul><li>Brigante Federico</li></ul><h5><strong>A Comprehensive timsTOF MS/MS Spectral Library for Improving Metabolite Annotation in Non-Targeted Metabolomics </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=5455392"><strong>(WeS-06)</strong></a></h5><ul><li>Mazumdar Aninda</li></ul><h5><strong>19:00 - 22:0 </strong>Welcome Reception &amp; Dinner (Canteen, live music from 19:30)</h5><h4><strong>Thursday November 20, 2025</strong></h4><h5><strong>09:00 - 09:40 Workshop </strong><a target="_blank" rel="noopener noreferrer" href="https://lcms.cz/companies/42"><strong>Pragolab</strong></a></h5><h5><strong>09:40 - 10:40 Session III</strong></h5><h5><strong>09:40 - 10:00 </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=5116751"><strong>ThO-08</strong></a><strong>: Low-input proteomics using the Orbitrap Astral</strong></h5><ul><li>Talacko Pavel</li></ul><h5><strong>10:00 - 10:20 </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=6944556"><strong>ThO-09</strong></a><strong>: Integrated multiomics classification of triple negative breast cancer</strong></h5><ul><li>Bouchal Pavel</li></ul><h5><strong>10:20 - 10:40 </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=5588120"><strong>ThO-10</strong></a><strong>: Proteomics of human breast milk</strong></h5><ul><li>Konik Peter</li></ul><h5><strong>10:40 - 11:00 Sponsor Lecture – Amedis</strong></h5><h5><strong>11:00 - 11:30 </strong>Coffee Break</h5><h5><strong>11:30 - 12:10 Workshop Genetica</strong></h5><h5><strong>12:10 - 13:10 Session IV</strong></h5><h5><strong>12:10 - 12:30 </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=5278447"><strong>ThO-11</strong></a><strong>: Development-dependent molecular strategies of stress adaptation in plants</strong></h5><ul><li>Černý Martin</li></ul><h5><strong>12:30 - 12:50 </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=4462363"><strong>ThO-12</strong></a><strong>: Deciphering adaptive shifts in the redox proteome of wheat seedlings under drought</strong></h5><ul><li>Danchenko Maksym</li></ul><h5><strong>12:50 - 13:10 </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=7250720"><strong>ThO-13</strong></a><strong>: No Mark, No Problem: Alternative Epigenetic Silencing in Algae</strong></h5><ul><li>Lochmanová Gabriela</li></ul><h5><strong>13:10 - 14:00 </strong>Lunch</h5><h5><strong>14:00 - 14:50 Plenary Lecture II: Prof. Bernhard Kuster (Technical University of Munich)&nbsp;</strong></h5><h5><strong>14:50 - 15:40 Flash Talks II</strong></h5><h5><strong>Propionic acid boosts sensitivity in high-flow RPLC-MS proteomics compared to formic and acetic acid </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=3643222"><strong>(ThS-07)</strong></a></h5><ul><li>Lenčo Juraj</li></ul><h5><strong>Towards Biomarker Discovery: Multiomics analysis of Endometriosis </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=8104565"><strong>(ThS-08)</strong></a></h5><ul><li>Oždian Tomáš</li></ul><h5><strong>Integrated proteogenomic analysis identifies synuclein gamma as a key target of the mesenchymal stem-like subtype of triple negative breast cancer </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=6375703"><strong>(ThS-09)</strong></a></h5><ul><li>Šimoník Jan</li></ul><h5><strong>Human IMPs: A tool for comparing outputs of different tools for transmembrane segment predictions in the human proteome </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=5382082"><strong>(ThS-10)</strong></a></h5><ul><li>Vít Ondřej</li></ul><h5><strong>LC-MS/MS-based terminomics unravels role of carboxypeptidase B1 in luminal A breast cancer </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=6248138"><strong>(ThS-11)</strong></a></h5><ul><li>Lapčík Petr</li></ul><h5><strong>Mass spectometry in hands of experimental biology: Impaired nucleotide salvage affects de novo synthesis in Drosophila melanogaster </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=9618906"><strong>(ThS-12)</strong></a></h5><ul><li>Sysel Jakub</li></ul><h5><strong>Bioaccumulation of pharmaceuticals in herbivorous fish: The role of aquatic plants as a dietary source </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=5574795"><strong>(ThS-13)</strong></a></h5><ul><li>Hinterholzová Helena</li></ul><h5><strong>LC-HRMS for large-scale chemical exposure studies </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=8545306"><strong>(ThS-14)</strong></a></h5><ul><li>Koudelka Štěpán</li></ul><h5><strong>15:40 - 17:00 </strong>Poster session + Coffee Break</h5><h5><strong>17:00 - 17:40 Workshop Bruker</strong></h5><h5><strong>17:40 - 18:00 Award Lecture – Prof. Josef Chmelík Prize Laureate&nbsp;</strong></h5><h5><strong>18:00 - 18:20 General Assembly of the Czech Society for Mass Spectrometry (in Czech, lecture room)</strong></h5><h5><strong>18:00 - 18:20 Informal meeting of Proteomic section of CSBMB (in Czech or English, poster room)</strong></h5><h5><strong>19:00 - 22:00 </strong>Gala Dinner – Restaurace Solnice</h5><h5><strong>21:00 Optional guided Walk-through historic center of České Budějovice – meet near the Samson's fountain at the main square</strong></h5><h4><strong>Friday November 21, 2025</strong></h4><h5><strong>09:00 - 09:50 Plenary Lecture III: Prof. Jana Roithová (Radboud University)</strong></h5><h5><strong>09:50 - 10:50 Session V</strong></h5><h5><strong>09:50 - 10:10 </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=2187982"><strong>FrO-15:</strong></a><strong> Per- and polyfluorinated compounds (PFAS) in wild common bream</strong></h5><ul><li>Grabicová Kateřina</li></ul><h5><strong>10:10 - 10:30 </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=8460763"><strong>FrO-16:</strong></a><strong> Spatial mapping of 15N-labeled ammonia with MALDI-FTICR imaging in regenerating liver tissue: Re-directing of toxic byproduct into anabolic pathways</strong></h5><ul><li>Kučera Lukáš</li></ul><h5><strong>10:30 - 10:50 </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=5845173"><strong>FrO-17</strong></a><strong>: LC-ICP-MS analysis of anti-obesity peptides and their metabolites labeled with lanthanide mass-tag</strong></h5><ul><li>Čechová Aneta</li></ul><h5><strong>10:50 - 11:00 Sponsor Lecture – Shimadzu</strong></h5><h5><strong>11:00 - 11:20 </strong>Coffee break</h5><h5><strong>11:20 - 11:40 Sponsor Lecture – Bruker</strong></h5><h5><strong>11:40 - 13:00 Session VI</strong></h5><h5><strong>11:40 - 12:00 </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=3584762"><strong>FrO-18</strong></a><strong>: Advancing Gut Microbiome Metabolomics: A Derivatization-Based Approach</strong></h5><ul><li>Stefani Tommaso</li></ul><h5><strong>12:00 - 12:20 </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=1987314"><strong>FrO-19</strong></a><strong>: Mass Spectrometry in Drug Development: From Screening to Stability and Pharmacokinetics</strong></h5><ul><li>Chalupský Karel</li></ul><h5><strong>12:20 - 12:40</strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=7700719"><strong> FrO-20</strong></a><strong>: Mass spectrometry of human body odor: Signatures of psychophysiological states</strong></h5><ul><li>Kyjakova Pavlina</li></ul><h5><strong>12:40 - 13:00 </strong><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=7256314"><strong>FrO-21:</strong></a><strong> Population-scale human chemical exposomics by automated liquid-liquid extraction coupled to gas chromatography – Orbitrap mass spectrometry</strong></h5><ul><li>Coufalíková Kateřina</li></ul><h5><strong>13:00 - 13:10 Closing Remarks and Awards</strong></h5><h5><strong>13:10 - 14:00 </strong>Lunch</h5><h5><strong>14:00 - 17:40 Guided Tour – Samson Brewery / Temelín Nuclear Power Plant</strong></h5>

Program of the 13th Conference of Czech Mass Spectrometry together with 11th Informal proteomic meeting

<p><strong>Thirteenth annual Conference of the Czech Society for Mass Spectrometry will take place together with the eleventh Informal Proteomic Meeting from November 19 – November 21, 2025 in České Budějovice.</strong></p><h3><strong>Registration</strong></h3><blockquote><ul><li><strong>Registration is only possible on site.&nbsp;</strong></li><li><strong>Registration fee: CZK 2500.</strong></li></ul></blockquote><h3><strong>Program</strong></h3><blockquote><p><strong>The complete program, including links to lecture abstracts, can be found HERE:</strong></p><ul><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/article/6384"><strong>Program of the 13th Conference of Czech Mass Spectrometry together with 11th Informal proteomic meeting</strong></a></li></ul></blockquote><h3><strong>List of posters (including links to their abstracts):</strong></h3><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=4124815"><strong>WeS-01:</strong></a><strong> Quantification of Oxoacids of the Human Metabolome using Liquid Chromatography-Mass Spectrometry</strong></p><ul><li>Philipp Hebesberger</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=9840543"><strong>WeS-02</strong></a><strong>: Analyses of human scent samples</strong></p><ul><li>Veronika Škeříková</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=5983681"><strong>WeS-03</strong></a><strong>: rDUVLAESCI-MS/MSI: a novel approach for direct analysis of biological surfaces</strong></p><ul><li>Jakub Grepl</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=8595826"><strong>WeS-04</strong></a><strong>: Investigation of phenolic compounds in grape pomace through UHPLC-ESI-MS/MS</strong></p><ul><li>Michal Jágr</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=7046316"><strong>WeS-05</strong></a><strong>: Mass Spectral Library Network (MERLIN) to streamline the generation of public spectral libraries</strong></p><ul><li>Federico Brigante</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=5455392"><strong>WeS-06</strong></a><strong>: A comprehensive timsTOF MS/MS spectral library for improving metabolite annotation in non-targeted metabolomics</strong></p><ul><li>Aninda Mazumdar</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=3643222"><strong>ThS-07</strong></a><strong>: Propionic acid boosts sensitivity in high-flow RPLC-MS proteomics compared to formic and acetic acid</strong></p><ul><li>Juraj Lenčo</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=8104565"><strong>ThS-08</strong></a><strong>: Towards biomarker discovery: Multiomics analysis of endometriosis</strong></p><ul><li>Tomáš Oždian</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=6375703"><strong>ThS-09</strong></a><strong>: Integrated proteogenomic analysis identifies synuclein gamma as a key target of the mesenchymal stem-like subtype of triple negative breast cancer</strong></p><ul><li>Jan Šimoník</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=5382082"><strong>ThS-10</strong></a><strong>: Human IMPs: A tool for comparing outputs of different tools for transmembrane segment predictions in the human proteome</strong></p><ul><li>Ondřej Vít</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=6248138"><strong>ThS-11</strong></a><strong>: LC-MS/MS-based terminomics unravels role of carboxypeptidase B1 in luminal A breast cancer</strong></p><ul><li>Petr Lapcik</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=9618906"><strong>ThS-12</strong></a><strong>: Mass spectrometry in hands of experimental biology: Impaired nucleotide salvage affects de novo synthesis in Drosophila melanogaster</strong></p><ul><li>Jakub Sysel</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=5574795"><strong>ThS-13</strong></a><strong>: Bioaccumulation of pharmaceuticals in herbivorous fish: The role of aquatic plants as a dietary source</strong></p><ul><li>Helena Hinterholzová</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=8545306"><strong>ThS-14</strong></a><strong>: LC-HRMS for large-scale chemical exposure studies</strong></p><ul><li>Štěpán Koudelka</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=7597199"><strong>ThP-01</strong></a><strong>: Complexome profiling workflow elucidates mitochondrial cytochrome c oxidase biogenesis</strong></p><ul><li>Marek Vrbacky</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=2382300"><strong>ThP-02</strong></a><strong>: Amino acid profiling across diverse biological matrices using the MetAmino® LC-MS Kit: Applications in free and peptide-bound amino acid analysis</strong></p><ul><li>Stanislav Opekar</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=8863587"><strong>ThP-03</strong></a><strong>: Ambient MS for rapid screening of pharmaceutically active compounds: Off-the-shelf and lab-made ion sources</strong></p><ul><li>Alžběta Němeškalová</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=3765372"><strong>ThP-04</strong></a><strong>: Adaptive proteome underpins drought tolerance in bread wheat during flowering</strong></p><ul><li>Olha Lakhneko</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=1069383"><strong>ThP-05</strong></a><strong>: Transition from natural dyestuffs to synthetic colorants depicted by ion mobility-aided mass spectrometry</strong></p><ul><li>Volodymyr Pauk</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=3752972"><strong>ThP-06</strong></a><strong>: Off-line GC–GC×GC-MS focusing on scent samples</strong></p><ul><li>Ulrika Malá</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=7593891"><strong>ThP-07</strong></a><strong>: Ambient soft landing voltammetry: Tool for electrode modification and molecular redox characterization</strong></p><ul><li>Adam Neuman</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=7978669"><strong>ThP-08</strong></a><strong>: Translational research aimed at improving heatstroke diagnosis</strong></p><ul><li>Andrej Kovac</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=2838864"><strong>ThP-09</strong></a><strong>: Tracing the Gravettian stone paths</strong></p><ul><li>Filip Gregar</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=4304936"><strong>ThP-10</strong></a><strong>: Leaf discs as a suitable alternative for cell cultures in plant omics analyses</strong></p><ul><li>Petr Čičmanec</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=4353606"><strong>ThP-11</strong></a><strong>: Characterization of nanoparticles in mixtures by Taylor dispersion analysis hyphenated to inductively coupled plasma mass spectrometry</strong></p><ul><li>Tomáš Pluháček</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=6271919"><strong>ThP-12</strong></a><strong>: Sub-cellular interacting partners of the tick-borne encephalitis virus capsid protein</strong></p><ul><li>Kateřina Kubátová</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=7486753"><strong>ThP-13</strong></a><strong>: Mass spectrometry-based proteomic profiling of Sugiyamaella lignohabitans adaptation to xylose as carbon source</strong></p><ul><li>Jana Bellová</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=3044553"><strong>ThP-14</strong></a><strong>: Proteomic analysis of acetylsalicylic acid-induced changes in the cellular, secreted, and extracellular vesicle proteome of malignant melanocytes</strong></p><ul><li>Jakub Červenka</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=1444237"><strong>ThP-15</strong></a><strong>: Apparatus for protein footprinting by singlet oxygen</strong></p><ul><li>Lada Fialová</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=7301517"><strong>ThP-16</strong></a><strong>: Insight into hemoglobin digestion pathways of Sphaerospora molnari by functional proteomics</strong></p><ul><li>Filip Dyčka</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=4960125"><strong>ThP-17</strong></a><strong>: High-flow HESI interface with point-focusing and enhanced desolvation</strong></p><ul><li>Jana Knytlová</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=6499455"><strong>ThP-18</strong></a><strong>: Proteomics identifies the landmark protein expression difference among mutation-based clusters of human pheochromocytoma and paraganglioma</strong></p><ul><li>Tereza Hrdinová</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=3701074"><strong>ThP-19</strong></a><strong>: Application of LC–MS/MS and fluorescence-based assays in the evaluation of novel carbonic anhydrase inhibitors</strong></p><ul><li>Mária Dobšovičová</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=4121623"><strong>ThP-20</strong></a><strong>: Production of sialylated glycoproteins in Ixodes ricinus ticks and tick cell lines</strong></p><ul><li>Jarmila Štěrbová</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=7502272"><strong>ThP-21</strong></a><strong>: Application of LC–MS-based “polaromics” in biochemistry, pharmacology, and biomedicine</strong></p><ul><li>Jaroslav Galba</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=2719813"><strong>ThP-22</strong></a><strong>: Development of software for LC-MS data processing of oligonucleotides</strong></p><ul><li>Evgeniya Biryukova</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=7174479"><strong>ThP-23</strong></a><strong>: Enhanced bottom-up proteomics for histone peptidoform profiling</strong></p><ul><li>Palina Ryzhaya</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=2072360"><strong>ThP-24</strong></a><strong>: Detection of deoxynivalenol in grain products by LC-MS</strong></p><ul><li>Daniel Smíšek</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=7139436"><strong>ThP-25</strong></a><strong>: FAmOS versus Percoll: Advancing organelle isolation efficiency and proteomic compatibility in plant research</strong></p><ul><li>Ivo Chamrád</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=6175084"><strong>ThP-26</strong></a><strong>: Quantification of monoclonal antibodies by middle-up capillary electrophoresis coupled to mass spectrometry</strong></p><ul><li>Jana Havlíková</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=7843229"><strong>ThP-27</strong></a><strong>: Integrative proteomic and hormonomic analysis of barley chloroplast mutant chlorina f2f2</strong></p><ul><li>Natálie Zemánková</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=9933055"><strong>ThP-28</strong></a><strong>: Microplastics and the blood–brain barrier: Mechanisms of transport and endothelial response</strong></p><ul><li>Petra Majerová</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=1637886"><strong>ThP-29</strong></a><strong>: Reactivity of singlet oxygen toward amino acid side chains</strong></p><ul><li>Marta Cruz</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=5725330"><strong>ThP-30</strong></a><strong>: Applied and residual: Assessment of pesticide residues and transformation products in irrigated Czech agricultural fields</strong></p><ul><li>Alina Sadchenko</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=5136513"><strong>ThP-31</strong></a><strong>: Expanding the FFAP protocol for structural characterization of membrane proteins</strong></p><ul><li>Michael Karpíšek</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=1961961"><strong>ThP-32</strong></a><strong>: DigDig: Streamlining digestion analysis for proteomics and HDX-MS</strong></p><ul><li>Zuzana Kalaninová</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=5856285"><strong>ThP-33</strong></a><strong>: Illuminating proteins: Dual UV/IR photodissociation in a custom FT-ICR system</strong></p><ul><li>Ezgi Gurler</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=9770654"><strong>ThP-34</strong></a><strong>: Decoding therapy-induced protein subcellular relocalization in leukemia</strong></p><ul><li>Michaela Myšáková</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=5337771"><strong>ThP-35</strong></a><strong>: Advancing AI/ML-based post-translational modification assignment using a verified FPOP dataset</strong></p><ul><li>Dmitry Loginov</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=2599017"><strong>ThP-36</strong></a><strong>: Analysis of glycerophospholipids using the method of direct infusion into a tribrid mass spectrometer with high mass resolution</strong></p><ul><li>Petr Zacek</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=1028179"><strong>ThP-37</strong></a><strong>: In situ comparison of hormonomics changes in different biotic stresses using mass spectrometry imaging</strong></p><ul><li>Chao Zhang</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=6619097"><strong>ThP-38</strong></a><strong>: Large-scale metabolomics screening of understudied plant lineages</strong></p><ul><li>Kateřina Kučerová</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=9282171"><strong>ThP-39</strong></a><strong>: Quantitative and redox proteomics identify signaling networks shaping leukemia survival and resistance</strong></p><ul><li>Dušan Nemes</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=6336342"><strong>ThP-40</strong></a><strong>: Deciphering phlebotomine sand fly taxonomy using MALDI-TOF MS protein profiling</strong></p><ul><li>Petr Halada</li></ul><p><a target="_blank" rel="noopener noreferrer" href="https://www.czechms.org/cz/events/cmsc/abstract.php?code=7924365"><strong>ThP-41</strong></a><strong>: Metabolomics analysis of type 1 diabetes mellitus among Qatari children using LC-MS</strong></p><ul><li>Haya Alsulaiti</li></ul>

Poster section of the 13th Conference of Czech Mass Spectrometry together with 11th Informal proteomic meeting

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The relatively new tradition of the Czech mass spectrometry conferences was established only in 2011, the very first event took place in Hradec Králové. Since then, the conference was organized every year except for 2020, the year of the pandemic.

Poster section of the 13th Conference of Czech Mass Spectrometry together with 11th Informal proteomic meeting

Program of the 13th Conference of Czech Mass Spectrometry together with 11th Informal proteomic meeting

11th Conference of the Czech Society for Mass Spectrometry (Day 3)

11th Conference of the Czech Society for Mass Spectrometry (Day 2)

11th Conference of the Czech Society for Mass Spectrometry (Day 1)

Conference CEEPC/IPM/CMSC 2022 (Day 3)

Conference CEEPC/IPM/CMSC 2022 (Day 2)

Conference CEEPC/IPM/CMSC 2022 (Day 1)

Conference CEEPC/IPM/CMSC 2022 (Program)

Upcoming events

Understanding quantification algorithms

36th MassSpec Forum Vienna 2026

Analytical Strategies for Peptide & Protein Therapeutics

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High-throughput stability screening strategies for antibody formulation

Big Scale, Big Wins: Prep Chromatography Explained

PFAS in Food & Food Contact Material