Suramin derivatives as inhibitors and activators of protein-tyrosine phosphatases. - Wikidata - awgldk - TriplyDB

Suramin derivatives as inhibitors and activators of protein-tyrosine phosphatases.

Suramin derivatives as inhibitors and activators of protein-tyrosine phosphatases.

http://www.wikidata.org/entity/Q41464016

about

Integrin CD11a cytoplasmic tail interacts with the CD45 membrane-proximal protein tyrosine phosphatase domain 1 Acceleration of epithelial cell syndecan-1 shedding by anthrax hemolytic virulence factors.A Second WNT for Old Drugs: Drug Repositioning against WNT-Dependent Cancers pCAP-based peptide substrates: the new tool in the box of tyrosine phosphatase assays Selective inhibitors of the protein tyrosine phosphatase SHP2 block cellular motility and growth of cancer cells in vitro and in vivo Characterization of a novel angiogenic model based on stable, fluorescently labelled endothelial cell lines amenable to scale-up for high content screening.Cell-permeable, small-molecule activators of the insulin-degrading enzyme.Investigating mammalian tyrosine phosphatase inhibitors as potential 'piggyback' leads to target Trypanosoma brucei transmission Potential Implications for Designing Drugs Against the Brown Spider Venom Phospholipase-D.Integrating virtual and biochemical screening for protein tyrosine phosphatase inhibitor discovery.Regulation of mammalian physiology, development, and disease by the sphingosine 1-phosphate and lysophosphatidic acid receptors.High-Throughput Screening (HTS) by NMR Guided Identification of Novel Agents Targeting the Protein Docking Domain of YopH.Targeting the PTPome in human disease.Essential role of protein-tyrosine phosphatase 1B in the modulation of insulin signaling by acetaminophen in hepatocytes.Suppression of cell membrane permeability by suramin: involvement of its inhibitory actions on connexin 43 hemichannels.Asperentin B, a New Inhibitor of the Protein Tyrosine Phosphatase 1B.4-((1E)-2-(5-(4-hydroxy-3-methoxystyryl-)-1-phenyl-1H-pyrazoyl-3-yl) vinyl)-2-methoxy-phenol) (CNB-001) Does Not Regulate Human Recombinant Protein-Tyrosine Phosphatase1B (PTP1B) Activity in vitro.Molecular mechanisms of Ca(2+) signaling in neurons induced by the S100A4 protein.Glycolipid-Dependent, Protease Sensitive Internalization of Pseudomonas aeruginosa Into Cultured Human Respiratory Epithelial Cells.Secreted neutral metalloproteases of Bacillus anthracis as candidate pathogenic factors.Amphiphilic suramin dissolves Matrigel, causing an 'inhibition' artefact within in vitro angiogenesis assays.Potent protein tyrosine phosphatase 1B (PTP1B) inhibiting constituents from Anoectochilus chapaensis and molecular docking studies.

P2860

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P2860

Suramin derivatives as inhibitors and activators of protein-tyrosine phosphatases.

http://www.wikidata.org/entity/Q41464016

description

2004 nî lūn-bûn

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2004年の論文

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2004年論文

@yue

2004年論文

@zh-hant

2004年論文

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2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

2004年论文

@zh

2004年论文

@zh-cn

name

Suramin derivatives as inhibitors and activators of protein-tyrosine phosphatases.

@en

type

label

Suramin derivatives as inhibitors and activators of protein-tyrosine phosphatases.

@en

prefLabel

Suramin derivatives as inhibitors and activators of protein-tyrosine phosphatases.

@en

P1433

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P1433

Journal of Biological Chemistry

P1476

Suramin derivatives as inhibitors and activators of protein-tyrosine phosphatases.

@en

P2093

Annett Kreimeyer

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

Antonio Gagliardi

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Daniel F McCain

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Delwood C Collins

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Li Wu

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

Matthias U Kassack

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

Peter Nickel

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

Zhong-Yin Zhang

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P2860

Crystal structure of the tandem phosphatase domains of RPTP LAR

Mitotic activation of protein-tyrosine phosphatase alpha and regulation of its Src-mediated transforming activity by its sites of protein kinase C phosphorylation

The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains

The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma

Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice

Dimerization of receptor protein-tyrosine phosphatase alpha in living cells

The structure of the membrane distal phosphatase domain of RPTPalpha reveals interdomain flexibility and an SH2 domain interaction region

Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization

Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: a paradigm for inhibitor design

Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A

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14713-14725

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scholarly article

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10.1074/JBC.M312488200

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15

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279

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2004-01-20T00:00:00Z

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8909725

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14734566

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