Literature DB >> 8924199

Computational sequence analysis of matrix metalloproteinases.

Q A Sang1, D A Douglas.   

Abstract

Matrix metalloproteinases (MMP) play a cardinal role in the breakdown of extracellular matrix involved in a variety of biological and pathological processes. Research on MMPs has classified and characterized these enzymes according to their matrix substrate specificity, gene and protein domain structure, and regulation of activity and expression. However, the discovery of new MMPs has introduced a need for a more comprehensive and systematic method of classification and quantitative comparison of known and newly discovered members. This study compiles a sequence alignment, constructs a dendrogram, and calculates physical data and homology percentage assignments in order to obtain further insight into MMP structure-function relationships. Thorough analysis of MMP primary sequence domains, physical data patterns, and statistical analysis of sequence homology yields higher resolution in the similarities and differences that group MMP members.

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Year:  1996        PMID: 8924199     DOI: 10.1007/bf01887395

Source DB:  PubMed          Journal:  J Protein Chem        ISSN: 0277-8033


  84 in total

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Journal:  Proc Natl Acad Sci U S A       Date:  1988-04       Impact factor: 11.205

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Journal:  Biochem Biophys Res Commun       Date:  1974-11-27       Impact factor: 3.575

Review 4.  Matrix metalloproteinases: a review.

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Journal:  Crit Rev Oral Biol Med       Date:  1993

5.  Early expression of a collagenase-like hatching enzyme gene in the sea urchin embryo.

Authors:  T Lepage; C Gache
Journal:  EMBO J       Date:  1990-09       Impact factor: 11.598

6.  The metalloproteinase matrilysin is preferentially expressed by epithelial cells in a tissue-restricted pattern in the mouse.

Authors:  C L Wilson; K J Heppner; L A Rudolph; L M Matrisian
Journal:  Mol Biol Cell       Date:  1995-07       Impact factor: 4.138

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Authors:  D Patterton; W P Hayes; Y B Shi
Journal:  Dev Biol       Date:  1995-01       Impact factor: 3.582

8.  Proteolytic and non-proteolytic activation of human neutrophil progelatinase B.

Authors:  Q X Sang; H Birkedal-Hansen; H E Van Wart
Journal:  Biochim Biophys Acta       Date:  1995-09-06

9.  The NMR structure of the inhibited catalytic domain of human stromelysin-1.

Authors:  P R Gooley; J F O'Connell; A I Marcy; G C Cuca; S P Salowe; B L Bush; J D Hermes; C K Esser; W K Hagmann; J P Springer
Journal:  Nat Struct Biol       Date:  1994-02

10.  The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity.

Authors:  W Bode; P Reinemer; R Huber; T Kleine; S Schnierer; H Tschesche
Journal:  EMBO J       Date:  1994-03-15       Impact factor: 11.598

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  8 in total

Review 1.  Structural basis of matrix metalloproteinases and tissue inhibitors of metalloproteinases.

Authors:  Klaus Maskos; Wolfram Bode
Journal:  Mol Biotechnol       Date:  2003-11       Impact factor: 2.695

Review 2.  Computational sequence analysis of the tissue inhibitor of metalloproteinase family.

Authors:  D A Douglas; Y E Shi; Q A Sang
Journal:  J Protein Chem       Date:  1997-05

3.  Identification and characterization of a novel collagenase in Xenopus laevis: possible roles during frog development.

Authors:  M A Stolow; D D Bauzon; J Li; T Sedgwick; V C Liang; Q A Sang; Y B Shi
Journal:  Mol Biol Cell       Date:  1996-10       Impact factor: 4.138

4.  A novel mechanism of latency in matrix metalloproteinases.

Authors:  Mar López-Pelegrín; Miroslaw Ksiazek; Abdulkarim Y Karim; Tibisay Guevara; Joan L Arolas; Jan Potempa; F Xavier Gomis-Rüth
Journal:  J Biol Chem       Date:  2015-01-02       Impact factor: 5.157

5.  Anomalous pH-dependence of the activity of human matrilysin (matrix metalloproteinase-7) as revealed by nitration and amination of its tyrosine residues.

Authors:  Yuko Muta; Hiroshi Oneda; Kuniyo Inouye
Journal:  Biochem J       Date:  2005-03-01       Impact factor: 3.857

6.  Unique organization and involvement of GAGA factors in transcriptional regulation of the Xenopus stromelysin-3 gene.

Authors:  J Li; V C Liang; T Sedgwick; J Wong; Y B Shi
Journal:  Nucleic Acids Res       Date:  1998-06-15       Impact factor: 16.971

7.  Requirement for matrix metalloproteinase stromelysin-3 in cell migration and apoptosis during tissue remodeling in Xenopus laevis.

Authors:  A Ishizuya-Oka; Q Li; T Amano; S Damjanovski; S Ueda; Y B Shi
Journal:  J Cell Biol       Date:  2000-09-04       Impact factor: 10.539

8.  Thyroid hormone induces apoptosis in primary cell cultures of tadpole intestine: cell type specificity and effects of extracellular matrix.

Authors:  Y Su; Y Shi; M A Stolow; Y B Shi
Journal:  J Cell Biol       Date:  1997-12-15       Impact factor: 10.539

  8 in total

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