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

The COOH-terminal globular domain of fibrinogen gamma chain suppresses angiogenesis and tumor growth.

Cancer research - 1 Oct 2006

Akakura Nobuaki, Hoogland Case, Takada Yoko K, Saegusa Jun, Ye Xiaojing, Liu Fu-Tong, Cheung Anthony Tze-Wai, Takada Yoshikazu

Abstract excerpt

Fibrinogen is a major plasma protein (350 kDa) that induces proliferative signals by serving as a scaffold to support the binding of growth factors and to promote the cellular responses of adhesion, proliferation, and migration during wound healing, angiogenesis, and tumor growth. Fibrin(ogen) degradation products generated during fibrinolysis are implicated in tissue injury. The fibrinogen gamma chain has a...

Read the complete abstract on PubMed

Topics

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

Share to Angiogenesis Inhibitors
Share to Colonic Neoplasms

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endothelial Cells

Share to Fibrin Fibrinogen Degradation Products

Share to Fibrinogen

Share to Integrin alphaVbeta3

Share to Mammary Neoplasms, Experimental

Share to Mice, SCID

Source

Identifiers

PMID: 17018627
DOI: 10.1158/0008-5472.CAN-06-1686

Genes

DLD

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The COOH-terminal globular domain of fibrinogen gamma chain suppresses angiogenesis and tumor growth.PMID 17018627Read ↗

A cluster of basic amino acid residues in the gamma370-381 sequence of fibrinogen comprises a binding site for platelet integrin alpha(IIb)beta3 (glycoprotein IIb/IIIa).Semantic proximity Read ↗

Interaction of fibrin(ogen) with leukocyte receptor alpha M beta 2 (Mac-1): further characterization and identification of a novel binding region within the central domain of the fibrinogen gamma-module.Semantic proximity Read ↗

The interaction of integrin αIIbβ3 with fibrin occurs through multiple binding sites in the αIIb β-propeller domain.Semantic proximity Read ↗

Fibrinogen Alpha Chain Knockout Promotes Tumor Growth and Metastasis through Integrin–AKT Signaling Pathway in Lung CancerSemantic proximity Read ↗

Fibrinogen Hillsborough: a novel gammaGly309Asp dysfibrinogen with impaired clotting.Semantic proximity Read ↗

[Assembly and secretion of mutant fibrinogens with variant gamma-chain C terminal region (gamma313-gamma345)].Semantic proximity Read ↗

Soluble Endoglin Specifically Binds Bone Morphogenetic Proteins 9 and 10 via Its Orphan Domain, Inhibits Blood Vessel Formation, and Suppresses Tumor GrowthSemantic proximity Read ↗

Endoglin: An accessory component of the TGF‐β‐binding receptor‐complex with diagnostic, prognostic, and bioimmunotherapeutic potential in human malignanciesSemantic proximity Read ↗

A new substitution, gamma 358 Ser-->Cys, in fibrinogen Milano VII causes defective fibrin polymerization.Semantic proximity Read ↗

Analysis of engineered fibrinogen variants suggests that an additional site mediates platelet aggregation and that "B-b" interactions have a role in protofibril formation.Semantic proximity Read ↗

A new functional role of the fibrinogen RGD motif as the molecular switch that selectively triggers integrin alphaIIbbeta3-dependent RhoA activation during cell spreading.Semantic proximity Read ↗

Cleavage of galectin-3 by matrix metalloproteases induces angiogenesis in breast cancer.Semantic proximity Read ↗

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