Literature DB >> 10356396

Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed.

E Morgunova1, A Tuuttila, U Bergmann, M Isupov, Y Lindqvist, G Schneider, K Tryggvason.   

Abstract

Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide (cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability.

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Year:  1999        PMID： 10356396     DOI： 10.1126/science.284.5420.1667

Source DB:  PubMed          Journal:  Science        ISSN： 0036-8075            Impact factor:   47.728


  112 in total

1.  The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding.

Authors:  A R Pickford; S P Smith; D Staunton; J Boyd; I D Campbell
Journal:  EMBO J       Date:  2001-04-02       Impact factor: 11.598

2.  Origin of fibronectin type II (FN2) modules: structural analyses of distantly-related members of the kringle family idey the kringle domain of neurotrypsin as a potential link between FN2 domains and kringles.

Authors:  O A Ozhogina; M Trexler; L Bányai; M Llinás; L Patthy
Journal:  Protein Sci       Date:  2001-10       Impact factor: 6.725

3.  Substrate recognition by gelatinase A: the C-terminal domain facilitates surface diffusion.

Authors:  I E Collier; S Saffarian; B L Marmer; E L Elson; G Goldberg
Journal:  Biophys J       Date:  2001-10       Impact factor: 4.033

Review 4.  Angiogenesis in hematologic malignancies and its clinical implications.

Authors:  Renchi Yang; Zhong Chao Han
Journal:  Int J Hematol       Date:  2002-04       Impact factor: 2.490

5.  Circular trimers of gelatinase B/matrix metalloproteinase-9 constitute a distinct population of functional enzyme molecules differentially regulated by tissue inhibitor of metalloproteinases-1.

Authors:  Jennifer Vandooren; Benjamin Born; Inna Solomonov; Ewa Zajac; Radka Saldova; Michael Senske; Estefanía Ugarte-Berzal; Erik Martens; Philippe E Van den Steen; Jo Van Damme; Angeles Garcia-Pardo; Matheus Froeyen; Elena I Deryugina; James P Quigley; Søren K Moestrup; Pauline M Rudd; Irit Sagi; Ghislain Opdenakker
Journal:  Biochem J       Date:  2015-01-15       Impact factor: 3.857

6.  pH- and temperature-dependence of functional modulation in metalloproteinases. A comparison between neutrophil collagenase and gelatinases A and B.

Authors:  G F Fasciglione; S Marini; S D'Alessio; V Politi; M Coletta
Journal:  Biophys J       Date:  2000-10       Impact factor: 4.033

7.  Use of gel zymography to examine matrix metalloproteinase (gelatinase) expression in brain tissue or in primary glial cultures.

Authors:  Harald Frankowski; Yu-Huan Gu; Ji Hoe Heo; Richard Milner; Gregory J Del Zoppo
Journal:  Methods Mol Biol       Date:  2012

Review 8.  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 9.  [Anti-aging. Facts and visions].

Authors:  N Y Schürer
Journal:  Hautarzt       Date:  2003-09       Impact factor: 0.751

10.  In vivo bradykinin B2 receptor activation reduces renal fibrosis.

Authors:  Joost P Schanstra; Eric Neau; Pascale Drogoz; Miguel A Arevalo Gomez; José Miguel Lopez Novoa; Denis Calise; Christiane Pecher; Michael Bader; Jean-Pierre Girolami; Jean-Loup Bascands
Journal:  J Clin Invest       Date:  2002-08       Impact factor: 14.808
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