2 Å X-ray structure of adamalysin II complexed with a peptide phosphonate inhibitor adopting a retro-binding mode-Reference-Cited by-同舟云学术

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2 Å X-ray structure of adamalysin II complexed with a peptide phosphonate inhibitor adopting a retro-binding mode

Published:1997-12-01 Issue:3 Volume:418 Page:319-322
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Cirilli M.,Gallina C.,Gavuzzo E.,Giordano C.,Gomis-Rüth F.X.,Gorini B.,Kress L.F.,Mazza F.,Paglialunga Paradisi M.,Pochetti G.,Politi V.

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(97)01401-4/fullpdf

Reference38 articles.

1. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the ‘metzincins’

2. The Family of Matrix Metalloproteinases

3. Families of metalloendopeptidases and their relationships

4. The metzincins - Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc-peptidases

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2. Natural Inhibitors of Snake Venom Metalloproteinases;Australian Journal of Chemistry;2020

3. Targeting ADAM17 Sheddase Activity in Cancer;Current Drug Targets;2016-11-08

4. Metalloproteases Affecting Blood Coagulation, Fibrinolysis and Platelet Aggregation from Snake Venoms: Definition and Nomenclature of Interaction Sites;Toxins;2016-09-29

5. A novel synthetic quinolinone inhibitor presents proteolytic and hemorrhagic inhibitory activities against snake venom metalloproteases;Biochimie;2016-02

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