γ371 Thr → Ile substitution in the fibrinogen γD domain causes hypofibrinogenaemia

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1550, Issue 2, 2001, Pages 183-188

  Brennan, Stephen O ^a   Wyatt, Jane M ^a   Fellowes, Andrew P ^a   Dlott, Jeffrey S ^b   Triplett, Douglas A ^b   George, Peter M ^a  

^a CANTERBURY HEALTH LABORATORIES   (New Zealand)

^b Midwest Hemostasis and Thrombosis Laboratories   (United States)

Author keywords

Hypofibrinogenemia; Mass spectrometry; Mutation; Plasma expression

Indexed keywords

FIBRINOGEN; ISOLEUCINE; THREONINE; FIBRINOGEN VARIANT; TRYPSIN;

ARTICLE; CLINICAL ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; EXON; FIBRINOGEN BLOOD LEVEL; HUMAN; HYDROGEN BOND; HYPOFIBRINOGENEMIA; INTRON; MOLECULAR WEIGHT; MUTATION; PEPTIDE MAPPING; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; ADULT; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CHEMICAL STRUCTURE; CHEMISTRY; FEMALE; GENETICS; HETEROZYGOTE; MASS SPECTROMETRY; MOLECULAR GENETICS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN CONFORMATION;

ADULT; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ELECTROPHORESIS, POLYACRYLAMIDE GEL; EXONS; FEMALE; FIBRINOGEN; FIBRINOGENS, ABNORMAL; HETEROZYGOTE; HUMAN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN CONFORMATION; SPECTRUM ANALYSIS, MASS; SUPPORT, NON-U.S. GOV'T; TRYPSIN;

EID: 0035905578     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(01)00280-1     Document Type: Article

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13. 461 AAA → Stop TAA)
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