A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist - Test2 - elhamkhani - TriplyDB

A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist

A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist

http://www.wikidata.org/entity/Q27647900

about

MET: a critical player in tumorigenesis and therapeutic target Molecular recognition of parathyroid hormone by its G protein-coupled receptor Structural basis for agonism and antagonism of hepatocyte growth factor Engineered variants of InlB with an additional leucine-rich repeat discriminate between physiologically relevant and packing contacts in crystal structures of the InlB:MET complex The solution structure of the MANEC-type domain from hepatocyte growth factor activator inhibitor-1 reveals an unexpected PAN/apple domain-type fold Noncoding mutations of HGF are associated with nonsyndromic hearing loss, DFNB39.The angiotensin IV analog Nle-Tyr-Leu-psi-(CH2-NH2)3-4-His-Pro-Phe (norleual) can act as a hepatocyte growth factor/c-Met inhibitor.Utilizing combinatorial engineering to develop Tie2 targeting antagonistic angiopoetin-2 ligands as candidates for anti-angiogenesis therapy Engineering hepatocyte growth factor fragments with high stability and activity as Met receptor agonists and antagonists.Single-molecule photobleaching reveals increased MET receptor dimerization upon ligand binding in intact cells A role for septins in the interaction between the Listeria monocytogenes INVASION PROTEIN InlB and the Met receptor Biochemical and pharmacological characterization of human c-Met neutralizing monoclonal antibody CE-355621 Flexibility and small pockets at protein-protein interfaces: New insights into druggability.Targeting the HGF-cMET Axis in Hepatocellular Carcinoma.Current Screens Based on the AlphaScreen Technology for Deciphering Cell Signalling Pathways Pseudo-active sites of protease domains: HGF/Met and Sonic hedgehog signaling in cancer.Plexin structures are coming: opportunities for multilevel investigations of semaphorin guidance receptors, their cell signaling mechanisms, and functions.The binding properties of minimal oligosaccharides reveal a common heparan sulfate/dermatan sulfate-binding site in hepatocyte growth factor/scatter factor that can accommodate a wide variety of sulfation patterns.Structural Basis of TPR-Mediated Oligomerization and Activation of Oncogenic Fusion Kinases.Oligonucleotide-Based Mimetics of Hepatocyte Growth Factor.Allosteric peptide activators of pro-hepatocyte growth factor stimulate Met signaling.Analogs of the hepatocyte growth factor and macrophage-stimulating protein hinge regions act as Met and Ron dual inhibitors in pancreatic cancer cells.An engineered dimeric fragment of hepatocyte growth factor is a potent c-MET agonist.Structural Basis for Interactions Between Contactin Family Members and Protein-tyrosine Phosphatase Receptor Type G in Neural Tissues.Physiological Signaling and Structure of the HGF Receptor MET.

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A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist

http://www.wikidata.org/entity/Q27647900

description

2007 nî lūn-bûn

@nan

2007 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2007年の論文

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2007年論文

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2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist

@ast

A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist

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A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist

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type

label

A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist

@ast

A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist

@en

A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist

@nl

prefLabel

A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist

@ast

A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist

@en

A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist

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PNAS.0704290104

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Proceedings of the National Academy of Sciences of the United States of America

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A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist

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P2093

ChongFeng Gao

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

Cindy Miranti

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

Ermanno Gherardi

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

George Vande Woude

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

H Eric Xu

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

Jennifer Daugherty

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

Qian Xie

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

W David Tolbert

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

P2860

Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor

Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization

Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin

Crystal structure of the HGF beta-chain in complex with the Sema domain of the Met receptor

Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha

Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains

Identification of the hepatocyte growth factor receptor as the c-met proto-oncogene product

Crystal structure at 1.7 A resolution of VEGF in complex with domain 2 of the Flt-1 receptor

Neutralizing monoclonal antibodies to hepatocyte growth factor/scatter factor (HGF/SF) display antitumor activity in animal models

Improved methods for building protein models in electron density maps and the location of errors in these models

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14592-7

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scholarly article

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10.1073/PNAS.0704290104

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37

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104

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2007-09-11T00:00:00Z

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6035336

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17804794

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identical protein binding

Hepatocyte growth factor

Hepatocyte growth factor

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1965485

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