Insight from studies with recombinant fibrinogens

Annals of the New York Academy of Sciences

Volumn 936, Issue , 2001, Pages 101-116

  Lord, Susan T ^a   Gorkun, Oleg V ^a  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

Author keywords

Clot; Fibrin; Fibrinogen; Fibrinopeptide; Lateral aggregation; Polymerization; Recombinant

Indexed keywords

FIBRINOGEN; FIBRINOGEN VARIANT; FIBRINOPEPTIDE B;

ANIMAL CELL; BINDING SITE; CALCIUM BINDING; CHO CELL; CONFERENCE PAPER; FIBRIN POLYMERIZATION; MOLECULAR CLONING; NONHUMAN; PROTEIN SECRETION;

ANIMALIA;

EID: 0034974358     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2001.tb03497.x     Document Type: Conference Paper

References (32)

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3. Human fibrinogen - Structural variants and functional sites
4. Quantifying thrombin-catalyzed release of fibrinopeptides from fibrinogen using high-performance liquid chromatography
5. Steady state kinetic parameters for the thrombin-catalyzed conversion of human fibrinogen to fibrin
6. The sequence of cleavage of fibrinopeptides from fibrinogen is important for protofibril formation and enhancement of lateral aggregation in fibrin clots
7. Analysis of fibrinogen Aα-fusion proteins. Mutants which inhibit thrombin equivalently are not equally good substrates
8. Substitution of tyrosine for phenylalanine in fibrinopeptide A results in preferential thrombin cleavage of fibrinopeptide B from fibrinogen
9. Recombinant fibrinogen studies reveal that thrombin specificity dictates order of fibrinopeptide release
10. Fibrinogen Petoskey, a dysfibrinogenemia characterized by replacement of Arg-Aα 16 by a histidyl residue. Evidence for thrombin-catalyzed hydrolysis at a histidyl residue
11. The primary fibrin polymerization pocket 3-dimensional structure of a 30-Kda C-terminal γ chain fragment complexed with the peptide Gly-Pro-Arg-Pro
12. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin
13. Severely impaired polymerization of recombinant fibrinogen γ364 Asp - His, the substitution discovered in a heterozygous individual
14. Photoaffinity labeling of the primary fibrin polymerization site: Localization of the label to γ-chain Tyr-363
15. Fibrinogen Matsumoto I: A γ364 Asp→His (GAT→CAT) substitution associated with defective fibrin polymerization
16. The synthetic peptide Gly-Pro-Arg-Proamide limits the plasmic digestion of fibrinogen in the same fashion as calcium ion
17. Recombinant fibrinogen Vlissingen/Frankfurt IV. The deletion of residues 319 and 320 from the γ chain of fibrinogen alters calcium binding, fibrin polymerization, cross-linking, and platelet aggregation
18. The polymerization pocket "a" within the carboxyl-terminal region of the γ chain of human fibrinogen is adjacent to but independent from the calcium-binding site
19. Fibrinogen Baltimore III: Congenital dysfibrinogenemia with a shortened gamma-subunit
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21. Polymerization site in the β chain of fibrin: Mapping of the Bβ 1-55 sequence
22. The polymerization and thrombin-binding properties of des-(Bβ 1-42)-fibrin
23. Photo-oxidation of histidine as a probe for aminoterminal conformational changes during fibrinogen-fibrin conversion
24. Synthetic peptides modeled on fibrin polymerization sites
25. Characterization of fibrinogen New York I. A dysfunctional fibrinogen with a deletion of Bβ (9-72) corresponding exactly to exon 2 of the gene
26. The contribution of the three hypothesized integrin-binding sites in fibrinogen to platelet-mediated clot retraction
27. Decreased lateral aggregation of a variant recombinant fibrinogen provides insight into the polymerization mechanism
28. Strategy for recombinant multichain protein synthesis: Fibrinogen Bβ-chain variants as thrombin substrates
29. Analysis of Aα251 fibrinogen: The αC domain has a role in polymerization, albeit more subtle than anticipated from the analogous proteolytic fragment X.
30. Dissecting clot retraction and platelet aggregation. Clot retraction does not require an intact fibrinogen γ chain C terminus
31. Role of fibrinogen α and γ chain sites in platelet aggregation