Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules (Q28306342)

The gene structure of human anti-haemophilic factor IX.

Europe PubMed Central

title

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

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author name string

L Patthy

series ordinal

1

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language of work or name

English

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publication date

July 1985

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published in

Cell

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volume

41

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issue

3

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page(s)

657-63

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cites work

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Haemostasis, blood coagulation and fibrinolysis in the japanese quail

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Exons--present from the beginning?

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Measurement of the binding of antifibrinolytic amino acids to various plasminogens.

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Vaccinia virus encodes a polypeptide homologous to epidermal growth factor and transforming growth factor

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Characterization of the complementary deoxyribonucleic acid and gene coding for human prothrombin

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The phylogeny of trypsin-related serine proteases and their zymogens. New methods for the investigation of distant evolutionary relationships

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Computer-based characterization of epidermal growth factor precursor

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Amino acid sequence of the light chain of bovine factor X1 (Stuart factor)

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Blood coagulation factor X mRNA encodes a single polypeptide chain containing a prepro leader sequence

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Nucleotide sequence of epidermal growth factor cDNA predicts a 128,000-molecular weight protein precursor

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The primary structure of high molecular mass urokinase from human urine. The complete amino acid sequence of the A chain

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A partial gene duplication in the evolution of prothrombin?

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The evolutionary relationship of the enzymes involved in blood coagulation and hemostasis

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Sequence homologies among E. coli ribosomal proteins: evidence for evolutionarily related groupings and internal duplications

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Homology and concerted evolution at the alpha 1 and alpha 2 loci of human alpha-globin

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Primary structure of two distinct rat pancreatic preproelastases determined by sequence analysis of the complete cloned messenger ribonucleic acid sequences

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Structure of mouse kallikrein gene family suggests a role in specific processing of biologically active peptides

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Evolution of Proteolytic Enzymes

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Kringles: modules specialized for protein binding. Homology of the gelatin-binding region of fibronectin with the kringle structures of proteases

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Calorimetric evaluation of the existence of separate domains in bovine prothrombin

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Recent gene conversion involving bovine vasopressin and oxytocin precursor genes suggested by nucleotide sequence

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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

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

3891096

1 reference

Consolidated OpenCitations Corpus – April 2017