(Q57360231)

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Exploring the chemical space of the lysine-binding pocket of the first kringle domain of hepatocyte growth factor/scatter factor (HGF/SF) yields a new class of inhibitors of HGF/SF-MET binding

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Exploring the chemical space of the lysine-binding pocket of the first kringle domain of hepatocyte growth factor/scatter factor (HGF/SF) yields a new class of inhibitors of HGF/SF-MET binding (English)

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object named as

A Winter

2

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object named as

M Fragai

4

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7

object named as

T L Blundell

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author name string

A G Sigurdardottir

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A Sobkowicz

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D Chirgadze

5

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D B Ascher

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E Gherardi

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language of work or name

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publication date

1 November 2015

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Chemical Science

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6

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11

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6147-6157

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Scatter factor is a fibroblast-derived modulator of epithelial cell mobility

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Essential role for the c-met receptor in the migration of myogenic precursor cells into the limb bud

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Protein engineered variants of hepatocyte growth factor/scatter factor promote proliferation of primary human hepatocytes and in rodent liver.

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Scatter factor/hepatocyte growth factor is essential for liver development

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c-Met is essential for wound healing in the skin

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Identification of the Hepatocyte Growth Factor Receptor As the c- met Proto-Oncogene Product

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Met, metastasis, motility and more

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Targeting MET in cancer: rationale and progress

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Germline and somatic mutations in the tyrosine kinase domain of the MET proto-oncogene in papillary renal carcinomas

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Overexpression of the Met/HGF receptor in ovarian cancer.

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Molecular evolution and domain structure of plasminogen-related growth factors (HGF/SF and HGF1/MSP)

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Molecular cloning and expression of human hepatocyte growth factor

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Hepatocyte growth factor (HGF)/NK1 is a naturally occurring HGF/scatter factor variant with partial agonist/antagonist activity

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An alternatively processed mRNA generated from human hepatocyte growth factor gene.

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NK1, a natural splice variant of hepatocyte growth factor/scatter factor, is a partial agonist in vivo

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Crystal structure of the NK1 fragment of HGF/SF suggests a novel mode for growth factor dimerization and receptor binding

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Crystal structures of NK1-heparin complexes reveal the basis for NK1 activity and enable engineering of potent agonists of the MET receptor.

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Crystal structure of the NK1 fragment of human hepatocyte growth factor at 2.0 A resolution

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A new crystal form of the NK1 splice variant of HGF/SF demonstrates extensive hinge movement and suggests that the NK1 dimer originates by domain swapping

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Multiple mutations and bypass mechanisms can contribute to development of acquired resistance to MET inhibitors

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Engineered mutants of HGF/SF with reduced binding to heparan sulphate proteoglycans, decreased clearance and enhanced activity in vivo

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Insights into the structure/function of hepatocyte growth factor/scatter factor from studies with individual domains

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Structural and functional basis of the serine protease-like hepatocyte growth factor beta-chain in Met binding and signaling

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Crystal structure of the kringle 2 domain of tissue plasminogen activator at 2.4-.ANG. resolution

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The refined structure of the epsilon-aminocaproic acid complex of human plasminogen kringle 4.

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Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation

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Development and validation of a genetic algorithm for flexible docking

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Cloning and expression of human tissue-type plasminogen activator cDNA in E. coli

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Crystal structures of the recombinant kringle 1 domain of human plasminogen in complexes with the ligands epsilon-aminocaproic acid and trans-4-(aminomethyl)cyclohexane-1-carboxylic Acid

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Structural biology and drug discovery for protein-protein interactions.

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Biophysical and computational fragment-based approaches to targeting protein-protein interactions: applications in structure-guided drug discovery

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Studies leading to potent, dual inhibitors of Bcl-2 and Bcl-xL

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Using a Fragment-Based Approach To Target Protein-Protein Interactions

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Functional map and domain structure of MET, the product of the c- met protooncogene and receptor for hepatocyte growth factor/scatter factor

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Perspectives on NMR in drug discovery: a technique comes of age

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Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

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Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system.

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Ligand-mediated dimerization of the Met receptor tyrosine kinase by the bacterial invasion protein InlB

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10.1039/C5SC02155C

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