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 (Q27639093)

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English	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	scientific article

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9 November 2019

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 (English)

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9 November 2019

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9 November 2019

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9 November 2019

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Tom L Blundell

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9 November 2019

Dimitri Y Chirgadze

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Dimitri Y Chirgadze

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9 November 2019

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Keiichi Watanabe

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9 November 2019

Ermanno Gherardi

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1 May 2002

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9 November 2019

Journal of Molecular Biology

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9 November 2019

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9 November 2019

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9 November 2019

283-288

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9 November 2019

Human growth hormone and extracellular domain of its receptor: crystal structure of the complex

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Heparin-induced oligomerization of FGF molecules is responsible for FGF receptor dimerization, activation, and cell proliferation

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Structure of a heparin-linked biologically active dimer of fibroblast growth factor

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

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Molecular cloning and expression of human hepatocyte growth factor

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

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7 January 2021

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

1 reference

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7 January 2021

Heparin induces dimerization and confers proliferative activity onto the hepatocyte growth factor antagonists NK1 and NK2.

1 reference

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7 January 2021

NK1, a Natural Splice Variant of Hepatocyte Growth Factor/Scatter Factor, Is a Partial Agonist In Vivo

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Diverse tumorigenesis associated with aberrant development in mice overexpressing hepatocyte growth factor/scatter factor

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

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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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Mutational analysis and molecular modeling of the N-terminal kringle-containing domain of hepatocyte growth factor identifies amino acid side chains important for interaction with the c-Met receptor

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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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Refined structure of dimeric diphtheria toxin at 2.0 A resolution

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The crystal structure of the ternary complex of staphylococcal nuclease, Ca2+, and the inhibitor pdTp, refined at 1.65 A

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Domain swapping: entangling alliances between proteins

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7 January 2021

"Diabodies": small bivalent and bispecific antibody fragments

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One-step evolution of a dimer from a monomeric protein

1 reference

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The CCP4 suite: programs for protein crystallography

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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

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10.1016/S0022-2836(02)00199-7

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9 November 2019

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Consolidated OpenCitations Corpus – April 2017

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Europe PubMed Central

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9 November 2019

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