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Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosisQuantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readersNoncovalent interaction between Ubc9 and SUMO promotes SUMO chain formationInvestigation of protein-tyrosine phosphatase 1B function by quantitative proteomicsRecent findings and technological advances in phosphoproteomics for cells and tissuesStatus of large-scale analysis of post-translational modifications by mass spectrometryUbc9 sumoylation regulates SUMO target discriminationStructures of Down Syndrome Kinases, DYRKs, Reveal Mechanisms of Kinase Activation and Substrate RecognitionLysine acetylation targets protein complexes and co-regulates major cellular functionsGlobal, in vivo, and site-specific phosphorylation dynamics in signaling networks.Ctk1 function is necessary for full translation initiation activity in Saccharomyces cerevisiae.Signaling initiated by overexpression of the fibroblast growth factor receptor-1 investigated by mass spectrometryα4βδ GABA(A) receptors are high-affinity targets for γ-hydroxybutyric acid (GHB)Recalibrating Equus evolution using the genome sequence of an early Middle Pleistocene horsePhosphorylation of the yeast γ-tubulin Tub4 regulates microtubule functionIntegrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondriaProtein sequences bound to mineral surfaces persist into deep timeDirect evidence of milk consumption from ancient human dental calculusGenetic association study of QT interval highlights role for calcium signaling pathways in myocardial repolarizationSpecies identification of archaeological skin objects from Danish bogs: comparison between mass spectrometry-based peptide sequencing and microscopy-based methodsPathogens and host immunity in the ancient human oral cavitymiR-625-3p regulates oxaliplatin resistance by targeting MAP2K6-p38 signalling in human colorectal adenocarcinoma cellsAncient proteins resolve the evolutionary history of Darwin’s South American ungulatesIn-gel digestion for mass spectrometric characterization of proteins and proteomesAndromeda: a peptide search engine integrated into the MaxQuant environmentPredicting Kinase Activity in Angiotensin Receptor Phosphoproteomes Based on Sequence-Motifs and InteractionsTemporal proteomics of NGF-TrkA signaling identifies an inhibitory role for the E3 ligase Cbl-b in neuroblastoma cell differentiationPre-Clovis Mastodon Hunting 13,800 Years Ago at the Manis Site, WashingtonTIMP-1 Increases Expression and Phosphorylation of Proteins Associated with Drug Resistance in Breast Cancer CellsProteomic Analysis of a Pleistocene Mammoth Femur Reveals More than One Hundred Ancient Bone ProteinsFrom Phosphosites to KinasesDisulfide Linkage Characterization of Disulfide Bond-Containing Proteins and Peptides by Reducing Electrochemistry and Mass Spectrometry.Phosphorylation variation during the cell cycle scales with structural propensities of proteins.De novo sequencing of antimicrobial peptides isolated from the venom glands of the wolf spider Lycosa singoriensis.Systems Analysis for Interpretation of Phosphoproteomics Data.The human urinary proteome contains more than 1500 proteins, including a large proportion of membrane proteins.The low molecular weight proteome of Halobacterium salinarum.Comprehensive identification of SUMO2/3 targets and their dynamics during mitosis.52 Genetic Loci Influencing Myocardial Mass.Effective representation and storage of mass spectrometry-based proteomic data sets for the scientific community.
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P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Jesper V Olsen
@nl
Jesper V Olsen
@sl
Jesper V. Olsen
@en
Jesper V. Olsen
@es
type
label
Jesper V Olsen
@nl
Jesper V Olsen
@sl
Jesper V. Olsen
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Jesper V. Olsen
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altLabel
Jesper Olsen
@en
Jesper V Olsen
@en
Jesper V. Olsen
@en
Jesper Velgaard Olsen
@en
prefLabel
Jesper V Olsen
@nl
Jesper V Olsen
@sl
Jesper V. Olsen
@en
Jesper V. Olsen
@es
P106
P1153
7403259606
P21
P31
P496
0000-0002-4747-4938