Changes in protein conformational mobility upon activation of extracellular regulated protein kinase-2 as detected by hydrogen exchange.
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Evolutionary clues to eukaryotic DNA clamp-loading mechanisms: analysis of the functional constraints imposed on replication factor C AAA+ ATPasesStructural insights into tail-anchored protein binding and membrane insertion by Get3Hydrogen exchange mass spectrometry: are we out of the quicksand?Hydrogen exchange and ligand binding: ligand-dependent and ligand-independent protection in the Src SH3 domain.Rapid analysis of protein structure and dynamics by hydrogen/deuterium exchange mass spectrometry.Adaptability in protein structures: structural dynamics and implications in ligand design.Human EGF-derived direct and reverse short linear motifs: conformational dynamics insight into the receptor-binding residues.Tracing glycoprotein structures: electrospray ionization tandem mass spectrometric analysis of sugar-peptide adducts.Hydrogen/deuterium exchange on yeast ATPase supramolecular protein complex analyzed at high sensitivity by MALDI mass spectrometry.Small-molecule inhibitors of the ERK signaling pathway: Towards novel anticancer therapeutics.Local conformational stability of HIV-1 gp120 in unliganded and CD4-bound states as defined by amide hydrogen/deuterium exchangePhosphorylation-dependent changes in structure and dynamics in ERK2 detected by SDSL and EPR.Dynamic protein complexes: insights from mass spectrometry.Environmentally coupled hydrogen tunneling. Linking catalysis to dynamics.Studies of biomolecular conformations and conformational dynamics by mass spectrometry.Phosphorylation in the catalytic cleft stabilizes and attracts domains of a phosphohexomutaseSolution NMR insights into docking interactions involving inactive ERK2Carboxyl-group footprinting maps the dimerization interface and phosphorylation-induced conformational changes of a membrane-associated tyrosine kinase.Rapid refinement of crystallographic protein construct definition employing enhanced hydrogen/deuterium exchange MS.The gatekeeper residue controls autoactivation of ERK2 via a pathway of intramolecular connectivity.Characterization of ATP-independent ERK inhibitors identified through in silico analysis of the active ERK2 structureDissecting interdomain communication within cAPK regulatory subunit type IIbeta using enhanced amide hydrogen/deuterium exchange mass spectrometry (DXMS)Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry.MAP kinases and the control of nuclear events.Application of hydrogen/deuterium exchange mass spectrometry to study protein tyrosine phosphatase dynamics, ligand binding, and substrate specificityPromiscuous aggregate-based inhibitors promote enzyme unfolding.Distal recognition sites in substrates are required for efficient phosphorylation by the cAMP-dependent protein kinase.Location of inhibitors bound to group IVA phospholipase A2 determined by molecular dynamics and deuterium exchange mass spectrometry.Hydrogen-exchange mass spectrometry reveals activation-induced changes in the conformational mobility of p38alpha MAP kinaseMonomeric and dimeric models of ERK2 in conjunction with studies on cellular localization, nuclear translocation, and in vitro analysis.Phosphorylation releases constraints to domain motion in ERK2.Unraveling the dynamics of protein interactions with quantitative mass spectrometry.HDX-MS takes centre stage at unravelling kinase dynamics.Extracellular-regulated kinase 2 is activated by the enhancement of hinge flexibility.Calcium binding rigidifies the C2 domain and the intradomain interaction of GIVA phospholipase A2 as revealed by hydrogen/deuterium exchange mass spectrometry.Requirements for PKC-augmented JNK activation by MKK4/7Interaction of group IA phospholipase A2 with metal ions and phospholipid vesicles probed with deuterium exchange mass spectrometry.Analysis of MAP kinases by hydrogen exchange mass spectrometry.Hydrogen-Deuterium Exchange of Lipoxygenase Uncovers a Relationship between Distal, Solvent Exposed Protein Motions and the Thermal Activation Barrier for Catalytic Proton-Coupled Electron Tunneling.PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain.
P2860
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P2860
Changes in protein conformational mobility upon activation of extracellular regulated protein kinase-2 as detected by hydrogen exchange.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Changes in protein conformatio ...... detected by hydrogen exchange.
@ast
Changes in protein conformatio ...... detected by hydrogen exchange.
@en
Changes in protein conformatio ...... detected by hydrogen exchange.
@nl
type
label
Changes in protein conformatio ...... detected by hydrogen exchange.
@ast
Changes in protein conformatio ...... detected by hydrogen exchange.
@en
Changes in protein conformatio ...... detected by hydrogen exchange.
@nl
prefLabel
Changes in protein conformatio ...... detected by hydrogen exchange.
@ast
Changes in protein conformatio ...... detected by hydrogen exchange.
@en
Changes in protein conformatio ...... detected by hydrogen exchange.
@nl
P2093
P2860
P356
P1476
Changes in protein conformatio ...... detected by hydrogen exchange.
@en
P2093
A N Hoofnagle
E J Goldsmith
K A Resing
P2860
P304
P356
10.1073/PNAS.98.3.956
P407
P577
2001-01-01T00:00:00Z