Literature DB >> 2672446

Proteolytic processing and physiological regulation.

H Neurath.   

Abstract

Proteolytic processing is a common and effective mechanism of physiological regulation. The basic principle is a conformational change induced in the protein precursor by the post-translational proteolytic cleavage of a specific peptide bond. The extension of earlier studies of model zymogens to more complex systems of physiological regulation, using methods of both protein chemistry and molecular biology, has enormously extended knowledge of the repertoire of proteolytic processing reactions and has contributed significantly to current studies of the structure, domain organization and evolution of proteins.

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Year:  1989        PMID: 2672446     DOI: 10.1016/0968-0004(89)90061-3

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN: 0968-0004            Impact factor:   13.807


  42 in total

Review 1.  Caspase activation: the induced-proximity model.

Authors:  G S Salvesen; V M Dixit
Journal:  Proc Natl Acad Sci U S A       Date:  1999-09-28       Impact factor: 11.205

2.  Autoproteolysis and feedback in a protease cascade directing Drosophila dorsal-ventral cell fate.

Authors:  M Dissing; H Giordano; R DeLotto
Journal:  EMBO J       Date:  2001-05-15       Impact factor: 11.598

3.  Identification of a nucleotide exchange-promoting activity for p21ras.

Authors:  J Downward; R Riehl; L Wu; R A Weinberg
Journal:  Proc Natl Acad Sci U S A       Date:  1990-08       Impact factor: 11.205

4.  Endoproteolysis in health and diseases--implications of proprotein convertases (PCs).

Authors:  Michel Chrétien
Journal:  J Mol Med (Berl)       Date:  2005-09-08       Impact factor: 4.599

5.  Analysis of a cDNA encoding arginine decarboxylase from oat reveals similarity to the Escherichia coli arginine decarboxylase and evidence of protein processing.

Authors:  E Bell; R L Malmberg
Journal:  Mol Gen Genet       Date:  1990-12

6.  Crystallization, data collection and processing of the chymotrypsin-BTCI-trypsin ternary complex.

Authors:  Gisele Ferreira Esteves; Rozeni Chagas Lima Teles; Nayara Silva Cavalcante; David Neves; Manuel Mateus Ventura; João Alexandre Ribeiro Gonçalves Barbosa; Sonia Maria de Freitas
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2007-11-30

7.  Defective posttranslational processing activates the tyrosine kinase encoded by the MET proto-oncogene (hepatocyte growth factor receptor).

Authors:  A Mondino; S Giordano; P M Comoglio
Journal:  Mol Cell Biol       Date:  1991-12       Impact factor: 4.272

8.  An unusual active site identified in a family of zinc metalloendopeptidases.

Authors:  A B Becker; R A Roth
Journal:  Proc Natl Acad Sci U S A       Date:  1992-05-01       Impact factor: 11.205

9.  Origins of the specificity of tissue-type plasminogen activator.

Authors:  L Ding; G S Coombs; L Strandberg; M Navre; D R Corey; E L Madison
Journal:  Proc Natl Acad Sci U S A       Date:  1995-08-15       Impact factor: 11.205

10.  On hypervariability at the reactive center of proteolytic enzymes and their inhibitors.

Authors:  T Ohta
Journal:  J Mol Evol       Date:  1994-12       Impact factor: 2.395

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