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

Roles of fibrin α- and γ-chain specific cross-linking by FXIIIa in fibrin structure and function.

Thrombosis and haemostasis - 5 May 2014

Duval Cédric, Allan Peter, Connell Simon D A, Ridger Victoria C, Philippou Helen, Ariëns Robert A S

Abstract excerpt

Factor XIII is responsible for the cross-linking of fibrin γ-chains in the early stages of clot formation, whilst α-chain cross-linking occurs at a slower rate. Although γ- and α-chain cross-linking was previously shown to contribute to clot stiffness, the role of cross-linking of both chains in determining clot structure is currently unknown. Therefore, the aim of this study was to determine the role of...

Read the complete abstract on PubMed

Topics

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

Share to Blood Coagulation
Share to Elasticity

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fibrin

Share to Fibrin Fibrinogen Degradation Products

Share to Fibrinogen

Share to Molecular Structure

Share to Peptide Fragments

Share to Protein Binding

Source

Identifiers

PMID: 24430058
DOI: 10.1160/TH13-10-0855

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

Roles of fibrin α- and γ-chain specific cross-linking by FXIIIa in fibrin structure and function.PMID 24430058Read ↗

The Non-catalytic B Subunit of Coagulation Factor XIII Accelerates Fibrin Cross-linking.Semantic proximity Read ↗

The involvement of blood coagulation factor XIII in fibrinolysis and thrombosis.Semantic proximity Read ↗

Missing regions within the molecular architecture of human fibrin clots structurally resolved by XL-MS and integrative structural modeling.Semantic proximity Read ↗

Factor XIII and Fibrin Clot Properties in Acute Venous Thromboembolism.Semantic proximity Read ↗

The plasma Factor XIII heterotetrameric complex structure: unexpected unequal pairing within a symmetric complexSemantic proximity Read ↗

Flexible regions in the molecular architecture of Human fibrin clots structurally resolved by XL-MS and integrative structural modelingSemantic proximity Read ↗

An engineered fibrinogen variant AαQ328,366P does not polymerise normally, but retains the ability to form α cross-links.Semantic proximity Read ↗

On the mechanism of αC polymer formation in fibrin.Semantic proximity Read ↗

Factor XIII, clot structure, thrombosis.Semantic proximity Read ↗

Thrombin activation of the factor XI dimer is a multistaged process for each subunit.Semantic proximity Read ↗

Factor XIII A-Subunit V34L Variant Affects Thrombus Cross-Linking in a Murine Model of Thrombosis.Semantic proximity Read ↗

Fibrin γ/γ' influences the secretion of fibrinolytic components and clot structureSemantic proximity Read ↗

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