Structure of rat procathepsin B: model for inhibition of cysteine protease activity by the proregion (Q27733264)

2

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P Grochulski

3

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R Coulombe

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A C Storer

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J S Mort

Vacuolar/lysosomal proteolysis: proteases, substrates, mechanisms

6

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publication date

15 April 1996

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published in

Structure

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volume

4

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issue

4

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page(s)

405-16

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Recombinant pro-regions from papain and papaya proteinase IV-are selective high affinity inhibitors of the mature papaya enzymes.

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The proregion of cathepsin L is required for proper folding, stability, and ER exit

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Alignment/phylogeny of the papain superfamily of cysteine proteases

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Two distinct gene subfamilies within the family of cysteine protease genes

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Structural basis of the activation and action of trypsin

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Catalysis of a protein folding reaction: Mechanistic implications of the 2.0 .ANG. structure of the subtilisin-prodomain complex

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Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity

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Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme

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Crystal structure of cathepsin B inhibited with CA030 at 2.0-A resolution: A basis for the design of specific epoxysuccinyl inhibitors

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

8740363

1 reference

Consolidated OpenCitations Corpus – April 2017