Characterization of mutations in the factor VIII gene by direct sequencing of amplified genomic DNA
References (44)
- et al.
The molecular basis of hemophilia in man
Trends Genet
(1988) - et al.
Characterization of recombinant human factor VIII
J. Biol. Chem
(1987) - et al.
The structure and evolution of the human beta-globin gene family
Cell
(1980) - et al.
An immunogenic region within residues Val1670-Glu1684 of the factor VIII light chain induces antibodies which inhibit binding of factor VIII to von Willebrand factor
J. Biol. Chem
(1988) - et al.
Mutations of factor VIII cleavage sites in hemophilia A
Blood
(1988) - et al.
Molecular defects in hemophilia A: Identification and characterization of mutations in the factor VIII gene and family analysis
Blood
(1989) - et al.
Synthesis, processing, and secretion of recombinant human factor VIII expressed in mammalian cells
J. Biol. Chem
(1988) - et al.
Molecular basis and prenatal diagnosis of β-thalassemia
Blood
(1988) - et al.
Association of the factor VIII light chain with von Willebrand factor
J. Biol. Chem
(1988) - et al.
Hemophilia A: Detection of molecular defects and of carrier by DNA analysis
N. Engl. J. Med
(1985)
DNA polymorphism haplotypes of the human apolipoprotein APOA1-APOC3-APOA4 gene cluster
Hum. Genet
Direct characterization of factor VIII in plasma: Detection of a mutation detecting a thrombin cleavage site (arginine-372 → histidine)
Nonuniform recombination within the human β-globin gene cluster
Amer. J. Hum. Genet
Patterns of polymorphisms and linkage disequilibrium suggest independent origins of the human growth hormone gene cluster
An estimate of unique DNA sequence heterozygosity in the human genome
Hum. Genet
Reactivity of cytosine and thymine in single-base-pair mismatches with hydroxylamine and osmium tetroxide and its application to the study of mutations
Proteolytic processing of human factor VIII: Correlation of specific cleavages of thrombin, factor Xa, and activated protein C with activation and inactivation of factor VIII coagulant activity
Biochemistry
Reconstitution of human factor VIII from isolated subunits
Arch. Biochem. Biophys
Characterization of the human factor VIII gene
Nature (London)
Detection and sequence of mutations in the factor VIII gene of hemophiliacs
Nature (London)
Identification of a missense mutation in the factor VIII gene of a mild hemophiliac
Science
A somatic mosaic for hemophilia A detected at the DNA level
Mol. Biol. Med
Cited by (74)
Protein modifications: Protein tyrosine sulfation
2021, Encyclopedia of Biological Chemistry: Third EditionHuman genomic variants and inherited disease: Molecular mechanisms and clinical consequences
2018, Emery and Rimoin's Principles and Practice of Medical Genetics and Genomics: FoundationsHuman Gene Mutation in Inherited Disease: Molecular Mechanisms and Clinical Consequences
2013, Emery and Rimoin's Principles and Practice of Medical GeneticsProtein tyrosine-O-sulfation in the retina
2009, Experimental Eye ResearchCitation Excerpt :However, the only published evidence showing that lack of sulfation in humans can lead to a phenotype is from cases of mild-to-moderate hemophilia A that result from missense mutations in the factor VIII gene. These mutations result in a Tyr1680Phe substitution in the von Willebrand factor binding site at the junction of the B and A3 domain (Jacquemin et al., 2000; Higuchi et al., 1990; Moore, 2003). It was later shown that optimal binding to von Willebrand factor requires sulfation of Tyr1680 in factor VIII (Leyte et al., 1991).
Post-translational modifications in proteins involved in blood coagulation
2005, Journal of Thrombosis and HaemostasisThe Biology and Enzymology of Protein Tyrosine O-Sulfation
2003, Journal of Biological ChemistryCitation Excerpt :In most cases in which a role for sulfation in the function of a protein has been defined, that function has been decreased in the absence of tyrosine O-sulfation but not absent. The only evidence that decreased tyrosine O-sulfation may have functional consequences in vivo comes from cases of mild to moderate hemophilia A that are due to missense mutations in the factor VIII gene that result in a Tyr1680 → Phe substitution in the von Willebrand factor binding site at the junction of the B and A3 domain (46). Sulfation of Tyr1680 in factor VIII is required for optimal binding to von Willebrand factor, which acts as a carrier protein for factor VIII in plasma, thereby increasing the circulating half-life of factor VIII in vivo (47).