about
High-speed and high-resolution UPLC separation at zero degrees CelsiusHydrogen/deuterium exchange mass spectrometry applied to IL-23 interaction characteristics: potential impact for therapeuticsCharacterization of IgG1 conformation and conformational dynamics by hydrogen/deuterium exchange mass spectrometryNovel mutant-selective EGFR kinase inhibitors against EGFR T790MTargeting Bcr–Abl by combining allosteric with ATP-binding-site inhibitorsConformational Locking upon Cooperative Assembly of Notch Transcription ComplexesGroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain FoldingAnalytical Aspects of Hydrogen Exchange Mass SpectrometryHydrogen exchange mass spectrometry: are we out of the quicksand?Hydrogen exchange mass spectrometry for the analysis of protein dynamicsAllosteric interactions between the myristate- and ATP-site of the Abl kinaseDifferential sensitivity of Src-family kinases to activation by SH3 domain displacement.Partial cooperative unfolding in proteins as observed by hydrogen exchange mass spectrometry.Enhanced SH3/linker interaction overcomes Abl kinase activation by gatekeeper and myristic acid binding pocket mutations and increases sensitivity to small molecule inhibitorsHIV-1 Nef interaction influences the ATP-binding site of the Src-family kinase, HckTyrosine phosphorylation in the SH3 domain disrupts negative regulatory interactions within the c-Abl kinase core.Ion mobility adds an additional dimension to mass spectrometric analysis of solution-phase hydrogen/deuterium exchange.Abl N-terminal cap stabilization of SH3 domain dynamicsThe Abl SH2-kinase linker naturally adopts a conformation competent for SH3 domain binding.Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri TipSrc family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity.Partial unfolding of diverse SH3 domains on a wide timescale.An examination of dynamics crosstalk between SH2 and SH3 domains by hydrogen/deuterium exchange and mass spectrometry.Activation of the Src family kinase Hck without SH3-linker release.Investigating monoclonal antibody aggregation using a combination of H/DX-MS and other biophysical measurementsInvestigating solution-phase protein structure and dynamics by hydrogen exchange mass spectrometry.Post-translational modifications differentially affect IgG1 conformation and receptor binding.Conformational analysis of membrane proteins in phospholipid bilayer nanodiscs by hydrogen exchange mass spectrometry.The utility of hydrogen/deuterium exchange mass spectrometry in biopharmaceutical comparability studiesConformational disturbance in Abl kinase upon mutation and deregulation.Conformational dynamics of the Escherichia coli DNA polymerase manager proteins UmuD and UmuD'.Molecular insight into the conformational dynamics of the Elongin BC complex and its interaction with HIV-1 Vif.Effects of HIV-1 Nef on human N-myristoyltransferase 1.Determining the site of spin trapping of the equine myoglobin radical by combined use of EPR, electrophoretic purification, and mass spectrometry.Semi-automated data processing of hydrogen exchange mass spectra using HX-Express.Conformational differences between arrestin2 and pre-activated mutants as revealed by hydrogen exchange mass spectrometry.Identification and characterization of EX1 kinetics in H/D exchange mass spectrometry by peak width analysis.Conformational transition of membrane-associated terminally acylated HIV-1 Nef.Hydrogen/deuterium exchange mass spectrometry for probing higher order structure of protein therapeutics: methodology and applications.Hydrogen exchange mass spectrometry: what is it and what can it tell us?
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P50
description
hulumtues
@sq
researcher
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wetenschapper
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հետազոտող
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name
John R Engen
@nl
John R Engen
@sl
John R. Engen
@en
John R. Engen
@es
type
label
John R Engen
@nl
John R Engen
@sl
John R. Engen
@en
John R. Engen
@es
prefLabel
John R Engen
@nl
John R Engen
@sl
John R. Engen
@en
John R. Engen
@es
P106
P1153
6602551499
P21
P31
P496
0000-0002-6918-9476