Structural and functional role of the β-strand insert (γ381-390) in the fibrinogen γ-module: A "pull out" hypothesis

Annals of the New York Academy of Sciences

Volumn 936, Issue , 2001, Pages 122-124

  Yakovlev, Sergei ^a   Loukinov, Dmitry ^a   Medved, Leonid ^a  

^a HOLLAND LABORATORY   (United States)

Author keywords

Fibrinogen; Pull out hypothesis; Strand insert; Module; Crosslinking

Indexed keywords

FIBRINOGEN;

CARBOXY TERMINAL SEQUENCE; CONFERENCE PAPER; HYPOTHESIS; PROTEIN ANALYSIS; PROTEIN CROSS LINKING; PROTEIN FOLDING; PROTEIN STRUCTURE;

EID: 0034973467     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2001.tb03499.x     Document Type: Conference Paper

References (6)

1. Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen
2. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin
3. 3 fragment contains non-covalently associated γ374-396 peptide
4. Domain structure and functional activity of the recombinant human fibrinogen gamma-module (gamma 148-411)
5. Determination of the topology of factor XIIIa-induced fibrin gamma-chain cross-links by electron microscopy of ligated fragments
6. The covalent structure of factor XIIIa crosslinked fibrinogen fibrils