Structure of fibrin: impact on clot stability.

Structure of fibrin: impact on clot stability. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Structure of fibrin: impact on clot stability. Abstract Text:

J W Weisel,

Information on the structural origins of clot stability is necessary for understanding the functions and pathology of fibrin clots and thrombi, but is also important for interpreting correctly the results of a variety of clinical diagnostic systems and technologies used daily to assess the hemostatic potential in patients. Fibrin polymerizes to make clots with a great diversity of structural, biological, physical and chemical properties, depending on the conditions of formation, and correlations have been established between these clot properties and many pathophysiological conditions. Clot stability refers to both viscoelastic properties, which are important because the clot essentially fulfills mechanical functions, and fibrinolytic properties, because the clot must be efficiently dissolved in a timely manner. The structure of the fibrin clot, which can be characterized in terms of a branched network, directly affects the clot's fibrinolytic and viscoelastic properties, which are remarkable and unique among polymers. Basic mechanisms underlying both the mechanical and fibrinolytic characteristics of fibrin are described. Some of the known correlations between clot structure and mechanical and fibrinolytic properties are summarized.

Structure of fibrin: impact on clot stability. Publishing Authors By Initials

JW Weisel,

For similar cardiovascular diseases: vascular diseases: embolism and thrombosis: thrombosis research abstracts see: cardiovascular diseases: vascular diseases: embolism and thrombosis: thrombosis research

PUBMED ID PMID:

MEDLINE DATE:

Structure of fibrin: impact on clot stability. Journal Published:

PUBLICATION TYPE: Review

Journal: Journal of thrombosis and haemostasis : JTH

VOLUME: 5 Suppl 1

Page Numbers: 116-24

Journal Abbreviation: J. Thromb. Haemost.

ISSN: 1538-7933

DAY: 3

MONTH: Jul

YEAR: 2007

Structure of fibrin: impact on clot stability. Information

Number of References: 38

LANGUAGE: eng

NlmUniqueID: 101170508

Structure of fibrin: impact on clot stability. Keywords Mesh Terms:

KEYWORDS: Thrombosis

MESH TERMS: chemistry

Chemical & Substance for Abstract: Structure of fibrin: impact on clot stability. Information

Substance Name: Fibrin

Registry Number: 9001-31-4

Grant and Affiliation Information for Structure of fibrin: impact on clot stability.

AFFILIATION: Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6058, USA. weisel@mail.med.upenn.edu

Country: England

AGENCY: United States NHLBI

GRANT: HL30954

ACRONYM: HL

MEDLINETA: J Thromb Haemost

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Structure of fibrin: impact on clot stability Related Publications

• Biophysics. Enigmas of blood clot elasticity.
• Calcium channel blockers in myocardial and cerebral ischemia: a clinician's review from bench to bedside.
• Cell transplantation: back to the bench: introduction.
• Choroidal detachment in the surgical treatment of retinal separation.
• Direct evidence for specific interactions of the fibrinogen alphaC-domains with the central E region and with each other.
• Dynamic imaging of fibrin network formation correlated with other measures of polymerization.
• Fibrinogen Guarenas, an abnormal fibrinogen with an Aalpha-chain truncation due to a nonsense mutation at Aalpha 467 Glu (GAA)-->stop (TAA).
• Forced Unfolding of Coiled-Coils in Fibrinogen by Single-Molecule AFM.
• Future directions of vitamin E and its analogues in minimizing myocardial ischemia-reperfusion injury.
• Glycaemic control improves fibrin network characteristics in type 2 diabetes - A purified fibrinogen model.
• Haemostatic changes related to fibrin formation and fibrinolysis during the first trimester in normal pregnancy and in recurrent miscarriage.
• Homophenotypic Aalpha R16H fibrinogen (Kingsport): uniquely altered polymerization associated with slower fibrinopeptide A than fibrinopeptide B release.
• Interactions mediated by the N-terminus of fibrinogen's Bbeta chain.
• Passive dosimeters for nitrogen dioxide in personal/indoor air sampling: a review.
• Polymerization of fibrin: Direct observation and quantification of individual B:b knob-hole interactions.
• Relation of salinity to the activity of the spermatozoa of Gillichthys, a marine teleost.
• Sodium-Hydrogen Exchange Inhibition by Cariporide to Reduce the Risk of Ischemic Cardiac Events in Patients Undergoing Coronary Artery Bypass Grafting: Results of the EXPEDITION Study.
• Structure of fibrin: impact on clot stability.
• Which knobs fit into which holes in fibrin polymerization?