1952
DOI: 10.1016/0006-3002(52)90213-8
|View full text |Cite
|
Sign up to set email alerts
|

The products of the action of thrombin on fibrinogen

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

3
51
0
3

Year Published

1953
1953
2010
2010

Publication Types

Select...
4
4

Relationship

0
8

Authors

Journals

citations
Cited by 165 publications
(57 citation statements)
references
References 5 publications
3
51
0
3
Order By: Relevance
“…This process is initiated by the activated serine protease thrombin, which specifically cleaves 4 N-terminal arginyl-glycine motifs on the 2 adjacent A␣ and B␤ chains of fibrinogen, releasing 2 sets of fibrinopeptides A and B (FpA and FpB) and exposing cryptic fibrin polymerization knobs "A" and "B," respectively. [1][2][3][4][5] The newly exposed fibrin knobs noncovalently interact with complementary "holes"' within the 2 distal C-terminal regions of the ␥ and ␤ chains (complementary holes "a" and "b," respectively) to initiate fibrin protofibril assembly. Understanding the fundamentals of this dynamic and noncovalent knob:hole interaction will lead to both a more thorough understanding of fibrin assembly mechanisms and the establishment of design criteria for superior anticoagulants with high polymerization hole affinity to inhibit fibrin assembly.…”
Section: Introductionmentioning
confidence: 99%
“…This process is initiated by the activated serine protease thrombin, which specifically cleaves 4 N-terminal arginyl-glycine motifs on the 2 adjacent A␣ and B␤ chains of fibrinogen, releasing 2 sets of fibrinopeptides A and B (FpA and FpB) and exposing cryptic fibrin polymerization knobs "A" and "B," respectively. [1][2][3][4][5] The newly exposed fibrin knobs noncovalently interact with complementary "holes"' within the 2 distal C-terminal regions of the ␥ and ␤ chains (complementary holes "a" and "b," respectively) to initiate fibrin protofibril assembly. Understanding the fundamentals of this dynamic and noncovalent knob:hole interaction will lead to both a more thorough understanding of fibrin assembly mechanisms and the establishment of design criteria for superior anticoagulants with high polymerization hole affinity to inhibit fibrin assembly.…”
Section: Introductionmentioning
confidence: 99%
“…The dramatic conversion of fibrinogen to fibrin is caused by the proteolytic action of thrombin with the release of N-terminal fibrinopeptide moieties [5][6][7][8] (Figure 2a). These "caps" have to be removed from the protein for unmasking the self-assembly potential that was built into the parent fibrinogen molecule by evolution.…”
Section: The Urea-soluble Clotmentioning
confidence: 99%
“…(estomae (135,78.159) gene (29) (29) (pancreas de (pancrbaa P.M. 25.000 P.M. 15.000 P.M. 34.500 P.M. 14.700 Pepsine (29) Lysoryme boeuf) de boeuf) de boeuf) (oeuf de poule) …”
Section: Chymotrypsinoribonurleaseunclassified
“…Au lieu de faire apparaitre, comme celle du chymotrypoinoghe, de nouvelles chahes ouvertes, elle provoque vraisemblablement le depart d'au moins un peptide N-terminal (188a).La coagulation du fibrinoghne (thrombine) fait apparaftre de l'azote non-prot6ique(143,143a). Quatre peptides prennent vraisemblablement naissance(15). Deux possedent l'acide glutamique N-terminal perdu par le fibrinoghne.…”
unclassified