Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Engineering the NK1 fragment of hepatocyte growth factor/scatter factor as a MET receptor antagonist.

Journal of molecular biology - 28 Mar 2008

Youles Mark, Holmes Oliver, Petoukhov Maxim V, Nessen Merel A, Stivala Simona, Svergun Dmitri I, Gherardi Ermanno

Abstract excerpt

The growth and motility factor hepatocyte growth factor/scatter factor (HGF/SF) and its receptor MET, the tyrosine kinase encoded by the c-MET proto-oncogene, exert major roles in cancer invasion and metastasis and are key targets for therapy. NK1 is an alternative spliced variant of HGF/SF that consists of the N-terminal (N) and first kringle (K1) domains and has partial agonistic activity. NK1 crystallizes as a...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alternative Splicing
Share to Cell Movement

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dimerization

Share to DNA Replication

Share to Hepatocyte Growth Factor

Share to Proto-Oncogene Mas

Share to Proto-Oncogene Proteins c-met

Source

Identifiers

PMID: 18291418
DOI: 10.1016/j.jmb.2008.01.034

Genes

MET
HGF

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Engineering the NK1 fragment of hepatocyte growth factor/scatter factor as a MET receptor antagonist.PMID 18291418Read ↗

A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist.Semantic proximity Read ↗

Dimer Interface in Natural Variant NK1 Is Dispensable for HGF-Dependent Met Receptor Activation.Semantic proximity Read ↗

Structural basis for agonism and antagonism of hepatocyte growth factor.Semantic proximity Read ↗

HGF–MET Cascade, a Key Target for Inhibiting Cancer Metastasis: The Impact of NK4 Discovery on Cancer Biology and TherapeuticsSemantic proximity Read ↗

State of the structure address on MET receptor activation by HGF.Semantic proximity Read ↗

Insights into the structure/function of hepatocyte growth factor/scatter factor from studies with individual domains.Semantic proximity Read ↗

Structures of the interleukin 11 signalling complex reveal dynamics of gp130 extracellular domains and the inhibitory mechanism of a cytokine variantSemantic proximity Read ↗

A dual role for the N-terminal domain of the IL-3 receptor in cell signalling.Semantic proximity Read ↗

Engineering and crystal structure of a monomeric FLT3 ligand variant.Semantic proximity Read ↗

The juxtamembrane region of the EGF receptor functions as an activation domain.Semantic proximity Read ↗

Antagonistic effect of NK4, a novel hepatocyte growth factor variant, on in vitro angiogenesis of human vascular endothelial cells.Semantic proximity Read ↗

Distinct amino acid residues may be involved in coactivator and ligand interactions in hepatocyte nuclear factor-4alpha.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.