Linked Life Data

11460485

Source:http://linkedlifedata.com/resource/pubmed/id/11460485

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2001-7-19
pubmed:abstractText
Fibrin stabilizing factor (factor XIII or FXIII) plays a critical role in the generation of a viable hemostatic plug. Following exposure to thrombin and calcium, the zymogen is activated to FXIIIa that, in turn, catalyzes the formation of N epsilon(gamma-glutamyl)lysine protein-to-protein side chain bridges within the clot network. Introduction of these covalent crosslinks greatly augments the viscoelastic storage modulus of the structure and its resistance to fibrinolytic enzymes. Analysis of the individual reaction steps and regulatory control mechanisms involved in clot stabilization enabled us to reconstruct the entire physiological process. This also serves as a guide for the differential diagnosis of the variety of molecular defects of fibrin stabilization.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0077-8923
pubmed:author
pubmed:issnType
Print
pubmed:volume
936
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
291-311
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Factor XIII: structure, activation, and interactions with fibrinogen and fibrin.
pubmed:affiliation
Department of Cell and Molecular Biology, Northwestern University Medical School, Searle 4-555, 303 E. Chicago Avenue, Chicago, IL 60611-3008, USA. l-lorand@northwestern.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review