Cysteine 81 is critical for the interaction of S100A4 and myosin-IIA - Wikidata - wikimedia - TriplyDB

Cysteine 81 is critical for the interaction of S100A4 and myosin-IIA

Cysteine 81 is critical for the interaction of S100A4 and myosin-IIA

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Crystal structure of the S100A4-nonmuscle myosin IIA tail fragment complex reveals an asymmetric target binding mechanism Asymmetric Mode of Ca2+-S100A4 Interaction with Nonmuscle Myosin IIA Generates Nanomolar Affinity Required for Filament Remodeling Structure of the S100A4/myosin-IIA complex.S100 proteins in cancer.Sulfiredoxin redox-sensitive interaction with S100A4 and non-muscle myosin IIA regulates cancer cell motility.Systemic shRNA mediated knock down of S100A4 in colorectal cancer xenografted mice reduces metastasis formation.CtBP- an emerging oncogene and novel small molecule drug target: Advances in the understanding of its oncogenic action and identification of therapeutic inhibitors.A generally applicable translational strategy identifies S100A4 as a candidate gene in allergy.Antileukaemic effect of PI3K-mTOR inhibitors in acute myeloid leukaemia-gene expression profiles reveal CDC25B expression as determinate of pharmacological effect.

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Cysteine 81 is critical for the interaction of S100A4 and myosin-IIA

http://www.wikidata.org/entity/Q33958590

description

2011 nî lūn-bûn

@nan

2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հուլիսին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Cysteine 81 is critical for the interaction of S100A4 and myosin-IIA

@ast

Cysteine 81 is critical for the interaction of S100A4 and myosin-IIA

@en

type

label

Cysteine 81 is critical for the interaction of S100A4 and myosin-IIA

@ast

Cysteine 81 is critical for the interaction of S100A4 and myosin-IIA

@en

prefLabel

Cysteine 81 is critical for the interaction of S100A4 and myosin-IIA

@ast

Cysteine 81 is critical for the interaction of S100A4 and myosin-IIA

@en

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Cysteine 81 is critical for the interaction of S100A4 and myosin-IIA

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Anne R Bresnick

http://www.w3.org/2001/XMLSchema#string

Dominic A Scudiero

http://www.w3.org/2001/XMLSchema#string

Karen M Hite

http://www.w3.org/2001/XMLSchema#string

Natalya G Dulyaninova

http://www.w3.org/2001/XMLSchema#string

Robert H Shoemaker

http://www.w3.org/2001/XMLSchema#string

Steven C Almo

http://www.w3.org/2001/XMLSchema#string

Wendy D Zencheck

http://www.w3.org/2001/XMLSchema#string

P2860

Mts1 regulates the assembly of nonmuscle myosin-IIA

Structure of the Ca2+/S100B/NDR kinase peptide complex: insights into S100 target specificity and activation of the kinase

Binding of pEL98 protein, an S100-related calcium-binding protein, to nonmuscle tropomyosin

Structure of the negative regulatory domain of p53 bound to S100B(betabeta)

Structure 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, S100A4

Crystal Structure of Metastasis-Associated Protein S100A4 in the Active Calcium-Bound Form

Phenothiazines inhibit S100A4 function by inducing protein oligomerization

The crystal structure of a complex of p11 with the annexin II N-terminal peptide

Intracellular and extracellular roles of S100 proteins

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7218-7227

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scholarly article

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10.1021/BI200853Y

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33

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2011-07-21T00:00:00Z

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