Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules

[1]  D. Twardzik,et al.  Vaccinia virus encodes a polypeptide homologous to epidermal growth factor and transforming growth factor , 1985, Nature.

[2]  G. Schütz,et al.  Recent gene conversion involving bovine vasopressin and oxytocin precursor genes suggested by nucleotide sequence , 1984, Nature.

[3]  L. T. Hunt,et al.  Vaccinia virus 19-kilodalton protein: relationship to several mammalian proteins, including two growth factors. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[4]  Malinowski Dp,et al.  Characterization of a complementary deoxyribonucleic acid coding for human and bovine plasminogen. , 1984 .

[5]  P. Verde,et al.  Identification and primary sequence of an unspliced human urokinase poly(A)+ RNA. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[6]  E. Davie,et al.  Characterization of a cDNA coding for human protein C. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[7]  R. Campbell,et al.  Blood coagulation factor X mRNA encodes a single polypeptide chain containing a prepro leader sequence. , 1984, Nucleic acids research.

[8]  Z. Váli,et al.  Kringles: modules specialized for protein binding , 1984, FEBS letters.

[9]  K. Kurachi,et al.  Characterization of a cDNA coding for human factor VII. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[10]  D. Russell,et al.  Domain map of the LDL receptor: Sequence homology with the epidermal growth factor precursor , 1984, Cell.

[11]  D. Rees,et al.  The gene structure of human anti‐haemophilic factor IX. , 1984, The EMBO journal.

[12]  H. Neurath,et al.  Evolution of proteolytic enzymes. , 1984, Science.

[13]  R. MacGillivray,et al.  Characterization of bovine prothrombin mRNA and its translation product. , 1984, Biochemistry.

[14]  T. E. Petersen,et al.  Complete primary structure of the collagen-binding domain of bovine fibronectin. , 1984, European journal of biochemistry.

[15]  Russell F. Doolittle,et al.  Computer-based characterization of epidermal growth factor precursor , 1984, Nature.

[16]  R. Campbell,et al.  Internal homologies of the Ba fragment from human complement component Factor B, a class III MHC antigen. , 1984, The EMBO journal.

[17]  C. Blake Molecular biology: Exons — present from the beginning? , 1983, Nature.

[18]  L. Patthy,et al.  Common evolutionary origin of the fibrin‐binding structures of fibronectin and tissue‐type plasminogen activator , 1983, FEBS letters.

[19]  A. Ullrich,et al.  Nucleotide sequence of epidermal growth factor cDNA predicts a 128,000-molecular weight protein precursor , 1983, Nature.

[20]  D. Cox,et al.  Structure of mouse kallikrein gene family suggests a role in specific processing of biologically active peptides , 1983, Nature.

[21]  M. Trexler,et al.  Folding autonomy of the kringle 4 fragment of human plasminogen. , 1983, Proceedings of the National Academy of Sciences of the United States of America.

[22]  T. Miyata,et al.  Unusual evolutionary conservation and frequent DNA segment exchange in class I genes of the major histocompatibility complex. , 1983, Proceedings of the National Academy of Sciences of the United States of America.

[23]  R. MacGillivray,et al.  Characterization of the complementary deoxyribonucleic acid and gene coding for human prothrombin. , 1983, Biochemistry.

[24]  E. Simpson,et al.  The structure of a mutant H–2 gene suggests that the generation of polymorphism in H–2 genes may occur by gene conversion-like events , 1983, Nature.

[25]  P. Seeburg,et al.  Cloning and expression of human tissue-type plasminogen activator cDNA in E. coli , 1983, Nature.

[26]  K. Kurachi,et al.  Isolation and characterization of a cDNA coding for human factor IX. , 1982, Proceedings of the National Academy of Sciences of the United States of America.

[27]  P Fernlund,et al.  Amino acid sequence of the light chain of bovine protein C. , 1982, The Journal of biological chemistry.

[28]  L. Flohé,et al.  The primary structure of high molecular mass urokinase from human urine. The complete amino acid sequence of the A chain. , 1982, Hoppe-Seyler's Zeitschrift fur physiologische Chemie.

[29]  L. Flohé,et al.  The complete amino acid sequence of low molecular mass urokinase from human urine. , 1982, Hoppe-Seyler's Zeitschrift fur physiologische Chemie.

[30]  O. Lindqvist,et al.  A low resolution model of fragment 1 from bovine prothrombin , 1982 .

[31]  E. Schon,et al.  Gene conversion of two functional goat alpha-globin genes preserves only minimal flanking sequences. , 1982, The Journal of biological chemistry.

[32]  G. Scheele,et al.  Amino acid sequences of transport peptides associated with canine exocrine pancreatic proteins. , 1982, The Journal of biological chemistry.

[33]  W. Rutter,et al.  Primary structure of two distinct rat pancreatic preproelastases determined by sequence analysis of the complete cloned messenger ribonucleic acid sequences. , 1982, Biochemistry.

[34]  Z. Váli,et al.  Location of the intermediate and high affinity omega-aminocarboxylic acid-binding sites in human plasminogen. , 1982, The Journal of biological chemistry.

[35]  R. Doolittle Similar amino acid sequences: chance or common ancestry? , 1981, Science.

[36]  D. Baltimore,et al.  Multiple differences between the nucleic acid sequences of the IgG2aa and IgG2ab alleles of the mouse. , 1981, Proceedings of the National Academy of Sciences of the United States of America.

[37]  D. Hewett‐Emmett,et al.  THE EVOLUTIONARY RELATIONSHIPS OF THE ENZYMES INVOLVED IN BLOOD COAGULATION AND HEMOSTASIS * , 1981, Annals of the New York Academy of Sciences.

[38]  Y. Kan,et al.  Homology and concerted evolution at the α1 and α2 loci of human α-globin , 1981, Nature.

[39]  F. Castellino,et al.  Calorimetric evaluation of the existence of separate domains in bovine prothrombin. , 1981, Biochemistry.

[40]  B Touchstone,et al.  Covalent structure of human haptoglobin: a serine protease homolog. , 1980, Proceedings of the National Academy of Sciences of the United States of America.

[41]  M. James An X-ray crystallographic approach to enzyme structure and function. , 1980, Canadian journal of biochemistry.

[42]  K. Fujikawa,et al.  Amino acid sequence of the light chain of bovine factor X1 (Stuart factor). , 1980, Biochemistry.

[43]  K. Titani,et al.  Comparison of amino acid sequence of bovine coagulation Factor IX (Christmas Factor) with that of other vitamin K-dependent plasma proteins. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[44]  W. Gilbert Why genes in pieces? , 1978, Nature.

[45]  D. Hewett‐Emmett,et al.  Amino acid sequence of human prothrombin fragments 1 and 2. , 1977, Proceedings of the National Academy of Sciences of the United States of America.

[46]  H. Neurath,et al.  The phylogeny of trypsin-related serine proteases and their zymogens. New methods for the investigation of distant evolutionary relationships. , 1975, Journal of molecular biology.

[47]  D. Hewett‐Emmett,et al.  A partial gene duplication in the evolution of prothrombin? , 1974, Thrombosis research.

[48]  F. Castellino,et al.  Measurement of the binding of antifibrinolytic amino acids to various plasminogens. , 1972, Archives of biochemistry and biophysics.

[49]  J. Baguet,et al.  Haemostasis, blood coagulation and fibrinolysis in the Japanese quail. , 1982, Comparative biochemistry and physiology. A, Comparative physiology.

[50]  W. Gunzler The primary structure of high molecular mass urokinase from human urine , 1982 .