Journal ArticleDOI
Structure of human factor VIII.
Gordon A. Vehar,Bruce Keyt,Dan L. Eaton,Henry Rodriguez,Donogh P. O'Brien,F. Rotblat,Herman Oppermann,Rodney G. Keck,William I. Wood,Richard N. Harkins,Edward G. D. Tuddenham,Richard M. Lawn,Daniel J. Capon +12 more
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TLDR
Determination of the thrombin cleavage sites in plasma-derived factor VIII polypeptides allows prediction of the domains involved in the associated activation and inactivation of the protein.Abstract:
The deduced amino acid sequence of human factor VIII, obtained from the DNA sequence, predicts a mature polypeptide of 2,332 amino acids containing a triplicated domain structure. The polypeptide has 35% sequence homology with the copper-binding plasma protein, ceruloplasmin. Determination of the thrombin cleavage sites in plasma-derived factor VIII polypeptides allows prediction of the domains involved in the associated activation and inactivation of the protein.read more
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Journal ArticleDOI
The coagulation cascade: initiation, maintenance, and regulation
Journal ArticleDOI
The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signalling
Yousuke Ebina,Leland Ellis,Kurt Jarnagin,Marc Edery,László Gráf,Eric Clauser,Jing-Hsiung Ou,Frank Masiarz,Yuet Wai Kan,Ira D. Goldfine,Richard A. Roth,William J. Rutter +11 more
TL;DR: A cloned approximately 5 kb cDNA (human placenta) contains the coding sequences for the insulin receptor; the nucleotide sequence predicts a 1382 amino acid precursor and the overall structure is reminiscent of the EGF receptor.
Journal ArticleDOI
Characterization of the human factor VIII gene
Jane Gitschier,William I. Wood,Therese M. Goralka,Karen L. Wion,Ellson Y. Chen,Dennis H. Eaton,Gordon A. Vehar,Daniel J. Capon,Richard M. Lawn +8 more
TL;DR: The complete 186,000 base-pair (bp) human factor VIII gene has been isolated and consists of 26 exons ranging in size from 69 to 3,106 bp and introns as large as 32.4 kilobases as mentioned in this paper.
Journal ArticleDOI
Expression of active human factor VIII from recombinant DNA clones
William I. Wood,Daniel J. Capon,Christian C. Simonsen,Dan L. Eaton,Jane Gitschier,Bruce Keyt,Peter H. Seeburg,Douglas H. Smith,P Hollingshead,Karen L. Wion,Eric Delwart,Edward G. D. Tuddenham,Gordon A. Vehar,Richard M. Lawn +13 more
TL;DR: The recombinant protein corrects the clotting time of plasma from haemophiliacs and has many of the biochemical and immunological characteristics of serum-derived factor VIII.
Journal ArticleDOI
Targeted disruption of the mouse factor VIII gene produces a model of haemophilia A
L. Bi,Ann M. Lawler,Stylianos E. Antonarakis,Katherine A. High,John D. Gearhart,Haig H. Kazazian +5 more
TL;DR: A small animal model of Haemophilia A is desirable for studies of factor VIII function and gene therapy, and a mouse with severe factorVIII deficiency is made using gene targeting.
References
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Journal ArticleDOI
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article
Cleavage of structural proteins during the assemble of the head of bacterio-phage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Journal ArticleDOI
Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
TL;DR: It was found that treatment of gels with dithiothreitol prior to impregnation with silver nitrate results in more reproducible staining patterns that are also qualitatively similar to those obtained with Coomassie blue.
Journal ArticleDOI
A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides
TL;DR: The proposed existence of a signal peptidase recognition sequence A-X-B with the preferred cleavage site located after the sixth amino acid following the core sequence is proposed.