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Article

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

Proceedings of the National Academy of Sciences of the United States of America - 28 Jan 2020

Klykov Oleg, van der Zwaan Carmen, Heck Albert J R, Meijer Alexander B, Scheltema Richard A

Abstract excerpt

Upon activation, fibrinogen forms large fibrin biopolymers that coalesce into clots which assist in wound healing. Limited insights into their molecular architecture, due to the sheer size and the insoluble character of fibrin clots, have restricted our ability to develop novel treatments for clotting diseases. The, so far resolved, disparate structural details have provided insights into linear elongation;...

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Identifiers

PMID: 31924745
DOI: 10.1073/pnas.1911785117
PMCID: PMC6995014

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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.

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