Structural aspects of the metzincin clan of metalloendopeptidases. (Q35127317)

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3 November 2019

review article

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title

Structural aspects of the metzincin clan of metalloendopeptidases (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12746556%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

1

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3 November 2019

author name string

F Xavier Gomis-Rüth

series ordinal

1

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6 August 2017

publication date

1 June 2003

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3 November 2019

published in

Molecular Biotechnology

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3 November 2019

volume

24

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3 November 2019

issue

2

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3 November 2019

page(s)

157-202

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3 November 2019

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Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon

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Aspzincin, a family of metalloendopeptidases with a new zinc-binding motif. Identification of new zinc-binding sites (His(128), His(132), and Asp(164)) and three catalytically crucial residues (Glu(129), Asp(143), and Tyr(106)) of deuterolysin from

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Comparative specificity of microbial proteinases.

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Remarkable roles of proteolysis on and beyond the cell surface

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Native carboxypeptidase A in a new crystal environment reveals a different conformation of the important tyrosine 248

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Role of proteolytic enzymes in biological regulation (a review)

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Caenorhabditis elegans: a model genetic host to study Pseudomonas aeruginosa pathogenesis

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Implications of the three-dimensional structure of astacin for the structure and function of the astacin family of zinc-endopeptidases

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