Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy
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Heterodimeric interaction and interfaces of S100A1 and S100PThe structure of Ca2+-loaded S100A2 at 1.3-Å resolutionThe heavy chain has its day: regulation of myosin-II assemblyThe C-terminal random coil region tunes the Ca²⁺-binding affinity of S100A4 through conformational activationSolution structure of the novel dispersin protein of enteroaggregative Escherichia coliStructure of Ca 2+ -Bound S100A4 and Its Interaction with Peptides Derived from Nonmuscle Myosin-IIA †Crystal structure of the Ca(2+)-form and Ca(2+)-binding kinetics of metastasis-associated protein, S100A4Crystal Structure of Metastasis-Associated Protein S100A4 in the Active Calcium-Bound FormAsymmetric Mode of Ca2+-S100A4 Interaction with Nonmuscle Myosin IIA Generates Nanomolar Affinity Required for Filament RemodelingS100A1: Structure, Function, and Therapeutic PotentialS100A4, a mediator of metastasisS100A4 regulates macrophage chemotaxisA biosensor of S100A4 metastasis factor activation: inhibitor screening and cellular activation dynamics.The metastasis-associated protein S100A4 exists in several charged variants suggesting the presence of posttranslational modifications.Mechanism of the Ca²+-dependent interaction between S100A4 and tail fragments of nonmuscle myosin heavy chain IIA.Intrinsically disordered and aggregation prone regions underlie β-aggregation in S100 proteins.Structure of the S100A4/myosin-IIA complex.Two functional S100A4 monomers are necessary for regulating nonmuscle myosin-IIA and HCT116 cell invasionS100P dissociates myosin IIA filaments and focal adhesion sites to reduce cell adhesion and enhance cell migration.Myosin-IIA heavy-chain phosphorylation regulates the motility of MDA-MB-231 carcinoma cells.Calcium-dependent and -independent interactions of the S100 protein family.Coupling S100A4 to Rhotekin alters Rho signaling output in breast cancer cells.Downregulation of S100A4 expression by RNA interference suppresses cell growth and invasion in human colorectal cancer cellsCalprotectin S100A9 calcium-binding loops I and II are essential for keratinocyte resistance to bacterial invasionA new role for PGRP-S (Tag7) in immune defense: lymphocyte migration is induced by a chemoattractant complex of Tag7 with Mts1.Solution structure and backbone dynamics of Calsensin, an invertebrate neuronal calcium-binding protein.Molecular mechanisms of Ca(2+) signaling in neurons induced by the S100A4 protein.The Calcium-Dependent Interaction of S100B with Its Protein Targets.KAHA Ligation at Serine.Multilevel Changes in Protein Dynamics upon Complex Formation of the Calcium-Loaded S100A4 with a Nonmuscle Myosin IIA Tail Fragment.Mutually antagonistic actions of S100A4 and S100A1 on normal and metastatic phenotypes
P2860
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P2860
Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy
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2002 nî lūn-bûn
@nan
2002 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
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2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
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name
Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy
@ast
Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy
@en
Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy
@nl
type
label
Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy
@ast
Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy
@en
Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy
@nl
prefLabel
Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy
@ast
Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy
@en
Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy
@nl
P2093
P356
P1433
P1476
Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy
@en
P2093
Anne R Bresnick
David J Weber
Karen C Ellis
Kristen M Vallely
Olga Varlamova
Richard R Rustandi
P304
P356
10.1021/BI020365R
P407
P577
2002-10-22T00:00:00Z