timsTOF Pro Bibliography


timsTOF Pro Bibliography  

The timsTOF Pro powered by PASEF® boosts the research capability of the labs having acquired it by offering an unprecedented, uncompromised combination of speed, sensitivity, selectivity and robustness. The reproducible measurement of Collisional Cross Section (CCS) values for every peptide has allowed to develop innovative 4D proteomics™/lipidomics™/metabolomics™ approaches, making the best use of the instrument’s selectivity. New acquisition modes are rolled out on a regular basis, like dia-PASEF® introduced at HUPO 2019. The peer-reviewed communications listed below is a non-exhaustive list from the work initiated on the first instruments, and many more are to come.  

Biology – timsTOF Pro - COVID-19 section

Title Authors Publication Link
Increasing the Throughput of Sensitive Proteomics by PlexDIA Derks, J.; Leduc, A. et al. Nat Biotechnol 2023, 41 (1), 50–59 https://doi.org/10.1038/s41587-022-01389-w
Deep Visual Proteomics Defines Single-Cell Identity and Heterogeneity Mund, A.; Coscia, F. et al. Biotechnol 2022, 40 (8), 1231–1240 https://doi.org/10.1038/s41587-022-01302-5
AI-Driven Deep Visual Proteomics Defines Cell Identity and Heterogeneity Mund, A.; Coscia, F. et al. preprint; Systems Biology 2021 https://doi.org/10.1101/2021.01.25.427969
Ultra-High Sensitivity Mass Spectrometry Quantifies Single-Cell Proteome Changes upon Perturbationn Brunner, A.-D.; Thielert, M. et al. preprint; Systems Biology 2020 https://doi.org/10.1101/2020.12.22.423933
Hyperinflammatory environment drives dysfunctional myeloid cell effector response to bacterial challenge in COVID-19 Mairpady  Shambat, S.; Gómez-Mejia, A. et al. PLoS Pathog 2022, 18 https://doi.org/10.1371/journal.ppat.1010176
Distinct Core Glycan and O-Glycoform Utilization of SARS-CoV-2 Omicron Variant Spike Protein RBD Revealed by Top-Down Mass Spectrometry Roberts, D.S.; Mann, M.; Ge, Y. et al. preprint; Biochemistry 2022 https://doi.org/10.1101/2022.02.09.479776
Immune response pattern across the asymptomatic, symptomatic and convalescent periods of COVID-19 Chen, Y.; Zhang, N.; Wong, C.C.L. et al. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2022, 1870 https://doi.org/10.1016/j.bbapap.2021.140736
Multi-level inhibition of coronavirus replication by chemical ER stress Shaban, M.S.; Müller, C. et al. Nat Commun 2021, 12, 5536 https://doi.org/10.1038/s41467-021-25551-1
Immunophenotyping assessment in a COVID-19 cohort (IMPACC): A prospective longitudinal study IMPACC Manuscript Writing Team†, on behalf of the IMPACC Network Steering Committee‡ Sci. Immunol. 2021, 6, eabf3733 https://doi.org/10.1126/sciimmunol.abf3733
DIA-Based Proteome Profiling of Nasopharyngeal Swabs from COVID-19 Patients Mun, D.-G.; Vanderboom, P.M. et al. J. Proteome Res. 20, 2021, 4165–4175 https://doi.org/10.1021/acs.jproteome.1c00506
Proteomic Analysis Identifies Prolonged Disturbances in Pathways Related to Cholesterol Metabolism and Myocardium Function in the COVID-19 Recovery Stage Chen, Y.; Yao, H.; Wong, C.C.L. et al. J. Proteome Res 2021 https://doi.org/10.1021/acs.jproteome.1c00054
SARS-CoV-2 infects human pancreatic ß cells and elicits ß cell impairment Wu, C.-T.; Lidsky, P.V.; Jackson, P.K. et al. Cell Metabolism 2021 https://doi.org/10.1016/j.cmet.2021.05.013
Second-Generation Antibodies Neutralize Emerging SARS-CoV-2 Variants of Concern Kovacech, B.; Fialova, L. et al. preprint; Microbiology 2021 https://doi.org/10.1101/2021.06.09.447527
A Blood Atlas of COVID-19 Defines Hallmarks of Disease Severity and Specificity; COvid-19 Multi-omics Blood ATlas (COMBAT) Consortium Ahern, D. J.; Ai, Z.; Fischer, R. et al. preprint; Infectious Diseases (except HIV/AIDS) 2021 https://doi.org/10.1101/2021.05.11.21256877
Systematic Functional Analysis of SARS-CoV-2 Proteins Uncovers Viral Innate Immune Antagonists and Remaining Vulnerabilities Hayn, M.; Hirschenberger, M. et al. Cell Reports 2021, 109126 https://doi.org/10.1016/j.celrep.2021.109126
Large Scale Discovery of Coronavirus-Host Factor Protein Interaction Motifs Reveals SARS-CoV-2 Specific Mechanisms and Vulnerabilities Kruse, T.; Benz, C.; Mann, M. et al. Biochemistry 2021 https://doi.org/10.1101/2021.04.19.440086
The COVIDome Explorer Researcher Portal Sullivan, K. D.; Galbraith, M. D. et al. Allergy and Immunology 2021 https://doi.org/10.1101/2021.03.04.21252945
Structural O-Glycoform Heterogeneity of the SARS-CoV-2 Spike Protein Receptor-Binding Domain Revealed by Native Top-Down Mass Spectrometry Roberts, D. S.; Mann, M. W.; Ge, Y. et al. preprint; Biochemistry 2021 https://doi.org/10.1101/2021.02.28.433291
Structural and Functional Characterization of SARS-CoV-2 RBD Domains Produced in Mammalian Cells Gstöttner, C.; Zhang, T.; Wuhrer, M. et al. preprint; Biochemistry 2021 https://doi.org/10.1101/2021.02.23.432424
High-Resolution Longitudinal Serum Proteome Trajectories in COVID-19 Reveal Patients-Specific Seroconversion Geyer, P. E.; Arend, F. M. et al. preprint; Infectious Diseases (except HIV/AIDS) 2021 https://doi.org/10.1101/2021.02.22.21252236
The Host Interactome of Spike Expands the Tropism of SARS-CoV-2 Bamberger, C.; Pankow, S.; Yates, J. et al. preprint; Molecular Biology 2021 https://doi.org/10.1101/2021.02.16.431318
Evidence of Structural Protein Damage and Membrane Lipid Remodeling in Red Blood Cells from COVID-19 Patients Thomas, T.; Stefanoni, D. et al. Proteome Res. 2020, 19 (11), 4455–4469 https://doi.org/10.1021/acs.jproteome.0c00606
Mass Spectrometric detection of SARS-CoV-2 virus in scrapings of the epithelium of the nasopharynx of infected patients via Nucleocapsid N protein (preprint). Nikolaev, E.; Indeykina, M.; Borchers, C. et al. Molecular Biology 2020 https://doi.org/10.1101/2020.05.24.113043
Immune Suppression in the Early Stage of COVID-19 Disease Tian, W.; Zhang, N.; Wong, C. C. L. et al. Nat Commun 2020, 11 (1), 5859 https://doi.org/10.1038/s41467-020-19706-9
SARS-CoV-2 Induced CYP19A1 Expression in the Lung Correlates with Increased Aromatization of Testosterone-to-Estradiol in Male Golden Hamsters Stanelle-Bertram, S.; Schaumburg, B. et al. preprint; In Review 2020 https://doi.org/10.21203/rs.3.rs-107474/v1
Transcriptional and Proteomic Insights into the Host Response in Fatal COVID-19 Cases Wu, M.; Chen, Y. et al. Proc Natl Acad Sci USA 2020, 117 (45), 28336–28343 https://doi.org/10.1073/pnas.2018030117
Serum Proteomics in COVID-19 Patients: Altered Coagulation and Complement Status as a Function of IL-6 Level D’Alessandro, A.; Thomas, T. et al. Proteome Res. 2020, 19 (11), 4417–4427 https://doi.org/10.1021/acs.jproteome.0c00365

Biology – timsTOF Pro  

Title Authors Publication Link
Oxonium Ion–Guided Optimization of Ion Mobility–Assisted Glycoproteomics on the timsTOF Pro Mukherjee, S.; Jankevics, A. et al. Molecular & Cellular Proteomics 2023, 22 (2), 100486 https://doi.org/10.1016/j.mcpro.2022.100486
Linkage-Specific Identification and Quantification of Sialylated Glycans by TIMS-TOF MS through Conjugation with Metal Complexes Li, Y.; Wang, H. et al. Talanta 2023, 253, 123995 https://doi.org/10.1016/j.talanta.2022.123995
Glycoproteomic Analyses of Influenza A Viruses Using TimsTOF Pro MS Wong, T. L.; Mooney, B. P. et al. Proteome Res. 2023, 22 (1), 62–77 https://doi.org/10.1021/acs.jproteome.2c00469
Benchmarking Commonly Used Software Suites and Analysis Workflows for DIA Proteomics and Phosphoproteomics Lou, R.; Cao, Y. et al. Nat Commun 2023, 14 (1), 94 https://doi.org/10.1038/s41467-022-35740-1
Multi-Omics Based Anti-Inflammatory Immune Signature Characterizes Long COVID-19 Syndrome Kovarik, J. J.; Bileck, A. et al. iScience 2023, 26 (1), 105717 https://doi.org/10.1016/j.isci.2022.105717
Increasing the Throughput of Sensitive Proteomics by PlexDIA Derks, J.; Leduc, A. et al. Nat Biotechnol 2023, 41 (1), 50–59 https://doi.org/10.1038/s41587-022-01389-w
Induction of Amphotericin B Resistance in Susceptible Candida Auris by Extracellular Vesicles Chan, W.; Chow, F. W.-N. et al. Emerging Microbes & Infections 2022, 11 (1), 1900–1909. https://doi.org/10.1080/22221751.2022.2098058
Top-Down Ion Mobility Separations of Isomeric Proteoforms Berthias, F.; Thurman, H. A. et al. Anal. Chem. 2022, acs.analchem.2c02948 https://doi.org/10.1021/acs.analchem.2c02948
HIP1R and Vimentin Immunohistochemistry Predict 1p/19q Status in IDH-Mutant Glioma Felix, M.; Friedel, D. et al. Neuro-Oncology 2022, 24 (12), 2121–2132 https://doi.org/10.1093/neuonc/noac111
CPEB1 Directs Muscle Stem Cell Activation by Reprogramming the Translational Landscape Zeng, W.; Yue, L. et al. Nat Commun 2022, 13 (1), 947 https://doi.org/10.1038/s41467-022-28612-1
CEND1 Deficiency Induces Mitochondrial Dysfunction and Cognitive Impairment in Alzheimer’s Disease Xie, W.; Guo, D. et al. Cell Death Differ 2022, 29 (12), 2417–2428 https://doi.org/10.1038/s41418-022-01027-7
Proteomics Based Markers of Clinical Pain Severity in Juvenile Idiopathic Arthritis Van Der Heijden, H.; Fatou, B. et al. Pediatr Rheumatol 2022, 20 (1), 3 https://doi.org/10.1186/s12969-022-00662-1
A Novel Protein Encoded by ZCRB1-Induced CircHEATR5B Suppresses Aerobic Glycolysis of GBM through Phosphorylation of JMJD5 Song, J.; Zheng, J. et al. J Exp Clin Cancer Res 2022, 41 (1), 171 https://doi.org/10.1186/s13046-022-02374-6
Mass Spectroscopy-Based Proteomics and Metabolomics Analysis of Triple-Positive Breast Cancer Cells Treated with Tamoxifen and/or Trastuzumab Sharaf, B. M.; Giddey, A. D. et al. Cancer Chemother Pharmacol 2022, 90 (6), 467–488 https://doi.org/10.1007/s00280-022-04478-4
Hornerin Deposits in Neuronal Intranuclear Inclusion Disease: Direct Identification of Proteins with Compositionally Biased Regions in Inclusions Park, H.; Yamanaka, T. et al. acta neuropathol commun 2022, 10 (1), 28 https://doi.org/10.1186/s40478-022-01333-8
LKB1 Drives Stasis and C/EBP-Mediated Reprogramming to an Alveolar Type II Fate in Lung Cancer Murray, C. W.; Brady, J. J. et al. Nat Commun 2022, 13 (1), 1090 https://doi.org/10.1038/s41467-022-28619-8
Proximity Proteomics of C9orf72 Dipeptide Repeat Proteins Identifies Molecular Chaperones as Modifiers of Poly-GA Aggregation Liu, F.; Morderer, D. et al. acta neuropathol commun 2022, 10 (1), 22 https://doi.org/10.1186/s40478-022-01322-x
Ibrutinib Reverses IL-6-Induced Osimertinib Resistance through Inhibition of Laminin Α5/FAK Signaling Li, L.; Li, Z. et al. Commun Biol 2022, 5 (1), 155 https://doi.org/10.1038/s42003-022-03111-7
Proteomic Profiling of End-Stage COVID-19 Lung Biopsies Gindlhuber, J.; Tomin, T. et al. Clin Proteom 2022, 19 (1), 46 https://doi.org/10.1186/s12014-022-09386-6
Lima1 Mediates the Pluripotency Control of Membrane Dynamics and Cellular Metabolism Duethorn, B.; Groll, F. et al. Nat Commun 2022, 13 (1), 610 https://doi.org/10.1038/s41467-022-28139-5
Dia-PASEF Data Analysis Using FragPipe and DIA-NN for Deep Proteomics of Low Sample Amounts Demichev, V.; Szyrwiel, L. et al. Nat Commun 2022, 13 (1), 3944 https://doi.org/10.1038/s41467-022-31492-0
Reconstruction and Analysis of a Large-Scale Binary Ras-Effector Signaling Network Catozzi, S.; Ternet, C. et al. Cell Commun Signal 2022, 20 (1), 24 https://doi.org/10.1186/s12964-022-00823-5
Deep Proteome Profiling Reveals Signatures of Age and Sex Differences in Paw Skin and Sciatic Nerve of Naïve Mice Xian, F.; Sondermann, J. R. et al eLife 2022, 11, e81431 https://doi.org/10.7554/eLife.81431
A de Novo MS1 Feature Detector for the Bruker TimsTOF Pro Wilding-McBride, D.; Webb, A. I. PLoS ONE 2022, 17 (11), e0277122 https://doi.org/10.1371/journal.pone.0277122
Subcellular Redox Responses Reveal Different Cu-Dependent Antioxidant Defenses between Mitochondria and Cytosol Zhang, Y.; Wen, M.-H. et al. Metallomics 2022, 14 (11), mfac087 https://doi.org/10.1093/mtomcs/mfac087
Ion Mobility‐resolved Phosphoproteomics with Dia‐PASEF and Short Gradients Oliinyk, D.; Meier, F. Proteomics 2022, 2200032 https://doi.org/10.1002/pmic.202200032
Rapid Proteomic Characterization of Bacteriocin-Producing Enterococcus Faecium Strains from Foodstuffs Quintela-Baluja, M.; Jobling, K. et al. IJMS 2022, 23 (22), 13830 https://doi.org/10.3390/ijms232213830
Phenazopyridine Promotes RPS23RG1/Rps23rg1 Transcription and Ameliorates Alzheimer-Associated Phenotypes in Mice Wang, C.; Zhang, Y. et al. Neuropsychopharmacol. 2022, 47 (12), 2042–2050 https://doi.org/10.1038/s41386-022-01373-7
Micro‐pillar Array Columns (ΜPAC): An Efficient Tool for Comparing Tissue and Cultured Cells of Glioblastoma Berg, H. E.; Halldórsson, S. et al. Journal of Chromatography Open 2022, 2, 100047 https://doi.org/10.1016/j.jcoa.2022.100047
Slice-PASEF: Fragmenting All Ions for Maximum Sensitivity in Proteomics Szyrwiel, L.; Sinn, L. et al. preprint; Biochemistry, 2022 https://doi.org/10.1101/2022.10.31.514544
A Comprehensive Study of Gradient Conditions for Deep Proteome Discovery in a Complex Protein Matrix Wei, X.; Liu, P. N. et al. IJMS 2022, 23 (19), 11714 https://doi.org/10.3390/ijms231911714
Proteome-Wide Analysis of the Hippocampus in Adolescent Male Mice with Learning and Memory Impairment Caused by Chronic Ethanol Exposure Liu, D.; Liu, S. et al. Neurobiology of Learning and Memory 2022, 194, 107661 https://doi.org/10.1016/j.nlm.2022.107661
CLE Peptides Join the Plant Longevity Club Han, H.; Zhuang, K. et al. Trends in Plant Science 2022, 27 (10), 961–963 https://doi.org/10.1016/j.tplants.2022.07.001
Proteomic Analysis Reveals Zinc-Finger CCHC-Type Containing Protein 3 as a Factor Inhibiting Virus Infection by Promoting Innate Signaling Chen, X.; Li, Z. et al. Virus Research 2022, 319, 198876 https://doi.org/10.1016/j.virusres.2022.198876
Evaluation of Quantitative Platforms for Single Target Mass Spectrometry Imaging Bowman, A. P.; Sawicki, J. et al. Pharmaceuticals 2022, 15 (10), 1180 https://doi.org/10.3390/ph15101180
Parallelization with Dual-Trap Single-Column Configuration Maximizes Throughput of Proteomic Analysis Kreimer, S.; Haghani, A. et al. Anal. Chem. 2022, 94 (36), 12452–12460 https://doi.org/10.1021/acs.analchem.2c02609
HLAII Peptide Presentation of Infliximab Increases When Complexed with TNF Casasola-LaMacchia, A.; Seward, R. J. et al. Front. Immunol. 2022, 13, 932252 https://doi.org/10.3389/fimmu.2022.932252
Metabolomic and Proteomic Responses of Phaeodactylum Tricornutum to Hypoxia Zhao, P.; Wu, Q. et al. Ocean. Limnol. 2022, 40 (5), 1963–1973 https://doi.org/10.1007/s00343-021-1232-5
Rapid and In-Depth Coverage of the (Phospho-)Proteome With Deep Libraries and Optimal Window Design for Dia-PASEF Skowronek, P.; Thielert, M. et al. Molecular & Cellular Proteomics 2022, 21 (9), 100279 https://doi.org/10.1016/j.mcpro.2022.100279
Toll-Like Receptor 3 Overexpression Induces Invasion of Prostate Cancer Cells, Whereas Its Activation Triggers Apoptosis Muresan, X. M.; Slabáková, E. et al. The American Journal of Pathology 2022, 192 (9), 1321–1335 https://doi.org/10.1016/j.ajpath.2022.05.009
Discovering the Secret of Diseases by Incorporated Tear Exosomes Analysis via Rapid-Isolation System: ITEARS Hu, L.; Zhang, T. et al. ACS Nano 2022, 16 (8), 11720–11732 https://doi.org/10.1021/acsnano.2c02531
Discovery of a Potent and Selective Degrader for USP7 Pei, Y.; Fu, J. et al. Angewandte Chemie 2022, 134 (33) https://doi.org/10.1002/ange.202204395
TIMSCONVERT: A Workflow to Convert Trapped Ion Mobility Data to Open Data Formats Luu, G. T.; Freitas, M. A et al. Bioinformatics 2022, 38 (16), 4046–4047 https://doi.org/10.1093/bioinformatics/btac419
The Cluster Transfer Function of AtNEET Supports the Ferredoxin–Thioredoxin Network of Plant Cells Zandalinas, S. I.; Song, L. et al. Antioxidants 2022, 11 (8), 1533. https://doi.org/10.3390/antiox11081533
Enhancement of Proteome Coverage by Ion Mobility Fractionation Coupled to PASEF on a TIMS–QTOF Instrument Guergues, J.; Wohlfahrt, J. et al. Proteome Res. 2022, 21 (8), 2036–2044 https://doi.org/10.1021/acs.jproteome.2c00336
Engineering of Succinyl-CoA Metabolism in View of Succinylation Regulation to Improve the Erythromycin Production Ke, X.; Jiang, X. et al. Appl Microbiol Biotechnol 2022, 106 (13), 5153–5165 https://doi.org/10.1007/s00253-022-12060-4
The Succinylome of Pinctada Fucata Martensii Implicates Lysine Succinylation in the Allograft-Induced Stress Response Zhang, M.; Lu, J. Fish & Shellfish Immunology 2022, 127, 585–593 https://doi.org/10.1016/j.fsi.2022.07.009
In-Depth Profiling and Quantification of the Lysine Acetylome in Hepatocellular Carcinoma with a Trapped Ion Mobility Mass Spectrometer Xu, J.; Guan, X. et al. Molecular & Cellular Proteomics 2022, 21 (8), 100255 https://doi.org/10.1016/j.mcpro.2022.100255
Next Generation VAMS®–Trypsin Immobilization for Instant Proteolysis in Bottom-up Protein Determination Reubsaet, L.; Thiede, B. et al. Advances in Sample Preparation 2022, 3, 100027 https://doi.org/10.1016/j.sampre.2022.100027
Coral and It’s Symbionts Responses to the Typical Global Marine Pollutant BaP by 4D-Proteomics Approach Pei, Y.; Chen, S. et al. Environmental Pollution 2022, 307, 119440 https://doi.org/10.1016/j.envpol.2022.119440
Deep Visual Proteomics defines single-cell identity and heterogeneity Mund, A.; Coscia, F. et al. Nat Biotechnol 2022, 40 (8), 1231–1240 https://doi.org/10.1038/s41587-022-01302-5
Targeted Proteomics on Its Way to Discovery Mendes, M. L.; Dittmar, G. Proteomics 2022, 22 (15–16), 2100330 https://doi.org/10.1002/pmic.202100330
Molecular Mechanism of Toxin Neutralization in the HipBST Toxin-Antitoxin System of Legionella Pneumophila Zhen, X.; Wu, Y. et al. Nat Commun 2022, 13 (1), 4333 https://doi.org/10.1038/s41467-022-32049-x
Structural Analyses of Human Ryanodine Receptor Type 2 Channels Reveal the Mechanisms for Sudden Cardiac Death and Treatment Miotto, M. C.; Weninger, G. et al. Sci. Adv. 2022, 8 (29), eabo1272 https://doi.org/10.1126/sciadv.abo1272
Locality-Sensitive Hashing Enables Efficient and Scalable Signal Classification in High-Throughput Mass Spectrometry Raw Data Bob, K.; Teschner, D. et al. BMC Bioinformatics 2022, 23 (1), 287 https://doi.org/10.1186/s12859-022-04833-55
Proteomic Analysis Reveals Key Differences between Squamous Cell Carcinomas and Adenocarcinomas across Multiple Tissues Song, Q.; Yang, Y. et al. Nat Commun 2022, 13 (1), 4167 https://doi.org/10.1038/s41467-022-31719-00
Proteomic Profile of Mouse Oocytes after Vitrification: A Quantitative Analysis Based on 4D Label-Free Technique Zhuan, Q.; Du, X.et al. Theriogenology 2022, 187, 64–73 https://doi.org/10.1016/j.theriogenology.2022.04.028
A Designer Nanoparticle Platform for Controlled Intracellular Delivery of Bioactive Macromolecules: Inhibition of Ubiquitin-Specific Protease 7 in Breast Cancer Cells McClary, W. D.; Catala, A. et al. ACS Chem. Biol. 2022, 17 (7), 1853–1865 https://doi.org/10.1021/acschembio.2c00256
On-Chip Preconcentration Microchip Capillary Electrophoresis Based CE-PRM-LIVE for High-Throughput Selectivity Profiling of Deubiquitinase Inhibitors Zhu, H.; Mellors, J. S. et al. Anal. Chem. 2022, 94 (27), 9508–9513 https://doi.org/10.1021/acs.analchem.2c01337
Ethanolamine‐phosphate on the Second Mannose Is a Preferential Bridge for Some GPI‐anchored Proteins Ishida, M.; Maki, Y.; Ninomiya, A. et al. EMBO Reports 2022, 23 (7) https://doi.org/10.15252/embr.202154352
Cyclic Immonium Ion of Lactyllysine Reveals Widespread Lactylation in the Human Proteome Wan, N.; Wang, N. et al. Nat Methods 2022, 19 (7), 854–864 https://doi.org/10.1038/s41592-022-01523-1
Zwitter-Ionic Monolith-Based Spintip Column Coupled with Evosep One Liquid Chromatography for High-Throughput Proteomic Analysis Su, Y.; Wang, X. et al. Journal of Chromatography A 2022, 1675, 463122 https://doi.org/10.1016/j.chroma.2022.463122
Super-Enhancer Hypermutation Alters Oncogene Expression in B Cell Lymphoma Bal, E.; Kumar, R. et al. Nature 2022, 607 (7920), 808–815 https://doi.org/10.1038/s41586-022-04906-8
Microanalysis of Brain Angiotensin Peptides Using Ultrasensitive Capillary Electrophoresis Trapped Ion Mobility Mass Spectrometry DeLaney, K.; Jia, D. et al. Anal. Chem. 2022, 94 (25), 9018–9025 https://doi.org/10.1021/acs.analchem.2c01062
Sucrose Nonfermenting-1-Related Protein Kinase 1 Regulates Sheath-to-Panicle Transport of Nonstructural Carbohydrates during Rice Grain Filling Hu, Y.; Liu, J. et al. Plant Physiology 2022, 189 (3), 1694–1714 https://doi.org/10.1093/plphys/kiac124
Comparative Analysis of Extracellular Vesicles (EVs) from Human and Feline Plasma Howard, J.; Wynne, K. et al. Sci Rep 2022, 12 (1), 10851 https://doi.org/10.1038/s41598-022-14211-z
Impact of in Vitro Hormone Treatments on the Bibenzyl Production of Radula Complanata Blatt-Janmaat, K.; Neumann, S. et al. Botany 2022, cjb-2022-0048 https://doi.org/10.1139/cjb-2022-0048
Human RIPK3 C-Lobe Phosphorylation Is Essential for Necroptotic Signaling Meng, Y.; Horne, C. R. et al. Cell Death Dis 2022, 13 (6), 1–12 https://doi.org/10.1038/s41419-022-05009-y
Molecular Evidence of Chemical Disguise by the Socially Parasitic Spiny Ant Polyrhachis Lamellidens (Hymenoptera: Formicidae) When Invading a Host Colony Iwai, H.; Mori, M. et al. Front. Ecol. Evol. 2022, 10, 915517 https://doi.org/10.3389/fevo.2022.915517
Targeted Protein Quantitation in Human Body Fluids by Mass Spectrometry Chen, Y.; Liao, W. et al. Mass Spectrometry Reviews 2022 https://doi.org/10.1002/mas.21788
Innate Variability in Physiological and Omics Aspects of the Beta Thalassemia Trait-Specific Donor Variation Effects Anastasiadi, A. T.; Tzounakas, V. L. et al. Front. Physiol. 2022, 13, 907444 https://doi.org/10.3389/fphys.2022.907444
Zinc Is a Master-Regulator of Sperm Function Associated with Binding, Motility, and Metabolic Modulation during Porcine Sperm Capacitation Zigo, M.; Kerns, K. et al. Commun Biol 2022, 5 (1), 1–12 https://doi.org/10.1038/s42003-022-03485-8
Different Oligomeric States of the Tumor Suppressor P53 Show Identical Binding Behavior towards the S100β Homodimer Wei, A. A. J.; Iacobucci, C. et al. ChemBioChem 2022, 23 (11) https://doi.org/10.1002/cbic.202100665
Cryo-EM Structures of Gid12-Bound GID E3 Reveal Steric Blockade as a Mechanism Inhibiting Substrate Ubiquitylation Qiao, S.; Lee, C.-W. et al. Nat Commun 2022, 13 (1), 3041 https://doi.org/10.1038/s41467-022-30803-9
Multimodal Imaging Mass Spectrometry of Murine Gastrointestinal Tract with Retained Luminal Content Guiberson, E. R.; Good, C. J. et al. J. Am. Soc. Mass Spectrom. 2022, 33 (6), 1073–1076 https://doi.org/10.1021/jasms.1c00360
Using Plasma Proteomics to Investigate Viral Infections of the Central Nervous System Including Patients with HIV-Associated Neurocognitive Disorders Ahmed, S.; Viode, A. et al. J. Neurovirol. 2022, 28 (3), 341–354 https://doi.org/10.1007/s13365-022-01077-0
Integrated Insights into the Mechanisms Underlying Sepsis-Induced Myocardial Depression Using a Quantitative Global Proteomic Analysis Yang, N.; Wang, W. et al. Journal of Proteomics 2022, 262, 104599 https://doi.org/10.1016/j.jprot.2022.104599
Human Umbilical Cord Mesenchymal Stem Cell-Derived Treatment of Severe Pulmonary Arterial Hypertension Hansmann, G.; Chouvarine, P. et al. Nat Cardiovasc Res 2022, 1 (6), 568–576 https://doi.org/10.1038/s44161-022-00083-z
Lockd Promotes Myoblast Proliferation and Muscle Regeneration via Binding with DHX36 to Facilitate 5′ UTR RG4 Unwinding and Anp32e Translation Chen, X.; Xue, G. et al. Cell Reports 2022, 39 (10), 110927 https://doi.org/10.1016/j.celrep.2022.110927
Complex Effects of Mg-Biomaterials on the Osteoblast Cell Machinery: A Proteomic Study Cerqueira, A.; García-Arnáez, I. et al. Biomaterials Advances 2022, 137, 212826 https://doi.org/10.1016/j.bioadv.2022.212826
Extracellular Vesicles from Thyroid Cancer Harbor a Functional Machinery Involved in Extracellular Matrix Remodeling Bravo-Miana, R. del C.; Soler, M. F. et al. European Journal of Cell Biology 2022, 101 (3), 151254 https://doi.org/10.1016/j.ejcb.2022.151254
Systematic Identification of the Lysine Lactylation in the Protozoan Parasite Toxoplasma Gondii Zhao, W.; Yu, H. et al. Parasites & Vectors 2022, 15 (1), 180 https://doi.org/10.1186/s13071-022-05315-6
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Crystal Structure of Bacterial Cytotoxic Necrotizing Factor CNF Y Reveals Molecular Building Blocks for Intoxication Chaoprasid, P.; Lukat, P. et al. EMBO J 2021, 40 (4) https://doi.org/10.15252/embj.2020105202
Water-Soluble Alkaloids Extracted from Aconiti Radix Lateralis Praeparata Protect against Chronic Heart Failure in Rats via a Calcium Signaling Pathway Xu, X.; Xie, X. et al. Biomedicine & Pharmacotherapy 2021, 135, 111184 https://doi.org/10.1016/j.biopha.2020.111184
Ultra-High Sensitivity Mass Spectrometry Quantifies Single-Cell Proteome Changes upon Perturbation Brunner, A.-D.; Thielert, M. et al. preprint; Systems Biology, 2020 https://doi.org/10.1101/2020.12.22.423933
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Divergent Molecular Signatures of Regeneration and Fibrosis during Wound Repair Mascharak, S.; desJardins-Park, H. E. et al. preprint; Cell Biology, 2020 https://doi.org/10.1101/2020.12.17.423181
DiaPASEF: Parallel Accumulation–Serial Fragmentation Combined with Data-Independent Acquisition Meier, F.; Brunner, A.-D. et al. Nat Methods 2020, 17 (12), 1229–1236 https://doi.org/10.1038/s41592-020-00998-0
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In-Depth Proteomic Analysis of Plasmodium Berghei Sporozoites Using Trapped Ion Mobility Spectrometry with Parallel Accumulation-Serial Fragmentation Hamada, S.; Pionneau, C. et al. preprint; Microbiology, 2020 https://doi.org/10.1101/2020.11.26.400192
Licorice Ameliorates Cisplatin-Induced Hepatotoxicity Through Antiapoptosis, Antioxidative Stress, Anti-Inflammation, and Acceleration of Metabolism Man, Q.; Deng, Y. et al. Front. Pharmacol. 2020, 11, 563750 https://doi.org/10.3389/fphar.2020.563750
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Nuclear Receptor NHR-49 Promotes Peroxisome Proliferation to Compensate for Aldehyde Dehydrogenase Deficiency in C. Elegans Zeng, L.; Li, X. et al. preprint; Cell Biology, 2020 https://doi.org/10.1101/2020.12.04.411637
O-Acetylated Chemical Reporters of Glycosylation Can Display Metabolism-Dependent Background Labeling of Proteins but Are Generally Reliable Tools for the Identification of Glycoproteins Darabedian, N.; Yang, B. et al. Front. Chem. 2020, 8, 318 https://doi.org/10.3389/fchem.2020.00318
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The MPK 8‐ TCP 14 Pathway Promotes Seed Germination in Arabidopsis Zhang, W.; Cochet, F. et al. Plant J 2019, 100 (4), 677–692 https://doi.org/10.1111/tpj.14461
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Fast quantitative analysis of timsTOF PASEF data with MSFragger and IonQuant (preprint) Yu, F., Haynes, S.E. et al. Bioinformatics, 2020 https://doi.org/10.1101/2020.03.19.999334
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c-Src Promotes Tumorigenesis and Tumor Progression by Activating PFKFB3 Ma, H., Zhang, J. et al. Cell Reports 2020, 30, 4235-4249.e6 https://doi.org/10.1016/j.celrep.2020.03.005
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Quantitatively profiling acetylome of DNA repair proteins in early DNA damage (preprint) Li, S., Zhou, L. et al. In Review, 2020 https://doi.org/10.21203/rs.3.rs-44043/v1
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Spatial Metabolomics of the Human Kidney using MALDI Trapped Ion Mobility Imaging Neumann, E.K., Migas, L.G. et al. Mass Spectrometry n.d., 9
Extending the Separation Space with Trapped Ion Mobility Spectrometry Improves the Accuracy of Isobaric Tag-based Quantitation in Proteomic LC/MS/MS Ogata, K., Ishihama, Y. Anal. Chem. 2020 https://doi.org/10.1021/acs.analchem.0c01695
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Exploration of human cerebrospinal fluid: A large proteome dataset revealed by trapped ion mobility time-of-flight mass spectrometry Macron, C., Lavigne, R. et al. Data in Brief 2020, 31, 105704 https://doi.org/10.1016/j.dib.2020.105704
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Quantitative Proteomic Analysis of Chikungunya Virus-Infected Aedes aegypti Reveals Proteome Modulations Indicative of Persistent Infection Cui, Y., Liu, P. et al. J. Proteome Res. 2020 https://doi.org/10.1021/acs.jproteome.0c00173
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Chemistry (timsTOF Pro / timsTOF)

Title Authors Publication Link
Development of Approach for Flavonoid Profiling of Biotechnological Raw Materials IRIS SIBIRICA L. by HPLC with High‐resolution Tandem Mass Spectrometry Karpitskiy, D. A.; Bessonova, E. A. et al. Phytochemical Analysis 2022, 33 (6), 869–878 https://doi.org/10.1002/pca.3135
Ordered Micropattern Arrays Fabricated by Lung-Derived DECM Hydrogels for Chemotherapeutic Drug Screening Zhu, X.; Li, Y. et al. Materials Today Bio 2022, 15, 100274 https://doi.org/10.1016/j.mtbio.2022.100274
Dual-Resolving of Positional and Geometric Isomers of C=C Bonds via Bifunctional Photocycloaddition-Photoisomerization Reaction System Feng, G.; Gao, M.; et al. Nat Commun 2022, 13 (1), 2652 https://doi.org/10.1038/s41467-022-30249-z
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Isoindolines and phthalides from the rhizomes of Ligusticum chuanxiong and their relaxant effects on the uterine smooth muscle Liu, J., Feng, R. et al. Phytochemistry 2022, 198, 113159 https://doi.org/10.1016/j.phytochem.2022.113159
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