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

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

Rinsho byori. The Japanese journal of clinical pathology - 1 Aug 2010

Terasawa Fumiko, Kamijyo Yuka, Fujihara Noriko, Okumura Nobuo

Abstract excerpt

BACKGROUND: It has been reported that the structure of the fibrinogen gamma-chain C terminal (D) region (140-411 residues) has important functions in fibrinogen assembly and/or secretion. Variant fibrinogens, gamma313S>N, gamma336M>I, gamma341A>D, and gamma345N>D have been reported as hypofibrino...

Read the complete abstract on PubMed

Topics

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

Share to Cells, Cultured
Share to CHO Cells
Share to Cricetinae

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cricetulus

Share to Enzyme-Linked Immunosorbent Assay

Share to Fibrinogens, Abnormal

Share to Immunoblotting

Share to Plasmids

Source

Identifiers

PMID: 20860169

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20860169-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

[Assembly and secretion of mutant fibrinogens with variant gamma-chain C terminal region (gamma313-gamma345)].PMID 20860169Read ↗

Recombinant variant fibrinogens substituted at residues gamma326Cys and gamma339Cys demonstrated markedly impaired secretion of assembled fibrinogen.Semantic proximity Read ↗

[Comparison of fibrinogen synthesis and secretion between novel variant fibrinogen, nagakute (gamma305Thr --> Ala), and other variants located in gamma305-308 residues].Semantic proximity Read ↗

[Role of fibrinogen Bbeta-chain D-region 454-458 residues for assembly and secretion of intact fibrinogen].Semantic proximity Read ↗

Recombinant γY278H Fibrinogen Showed Normal Secretion from CHO Cells, but a Corresponding Heterozygous Patient Showed Hypofibrinogenemia.Semantic proximity Read ↗

A C-terminal amino acid substitution in the gamma-chain caused by a novel heterozygous frameshift mutation (Fibrinogen Matsumoto VII) results in hypofibrinogenaemia.Semantic proximity Read ↗

Recombinant γY278H Fibrinogen Showed Normal Secretion from CHO Cells, but a Corresponding Heterozygous Patient Showed HypofibrinogenemiaSemantic proximity Read ↗

Analysis of fibrinogen variants at gamma387Ile shows that the side chain of gamma387 and the tertiary structure of the gammaC-terminal tail are important not only for assembly and secretion of fibrinogen but also for lateral aggregation of protofibrils and XIIIa-catalyzed gamma-gamma dimer formation.Semantic proximity Read ↗

A Novel Mutation in the Fibrinogen Bβ Chain (c.490G>A; End of Exon 3) Causes a Splicing Abnormality and Ultimately Leads to Congenital Hypofibrinogenemia.Semantic proximity Read ↗

Novel variant fibrinogen γp.C352R produced hypodysfibrinogenemia leading to a bleeding episode and failure of infertility treatment.Semantic proximity Read ↗

Molecular mechanisms accounting for fibrinogen deficiency: from large deletions to intracellular retention of misfolded proteins.Semantic proximity Read ↗

Congenital fibrinogen disorder with a compound heterozygote possessing two novel FGB mutations, one qualitative and the other quantitative.Semantic proximity Read ↗

Expression of four mutant fibrinogen gammaC domains in Pichia pastoris confirms them as causes of hypofibrinogenaemia.Semantic proximity Read ↗

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