The Catalytic Domain of Escherichia coli Lon Protease Has a Unique Fold and a Ser-Lys Dyad in the Active Site-Reference-Cited by-同舟云学术

The Catalytic Domain of Escherichia coli Lon Protease Has a Unique Fold and a Ser-Lys Dyad in the Active Site

Published:2004-02 Issue:9 Volume:279 Page:8140-8148
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Botos Istvan,Melnikov Edward E.,Cherry Scott,Tropea Joseph E.,Khalatova Anna G.,Rasulova Fatima,Dauter Zbigniew,Maurizi Michael R.,Rotanova Tatyana V.,Wlodawer Alexander,Gustchina Alla

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference70 articles.

1. Posttranslational Quality Control: Folding, Refolding, and Degrading Proteins

2. Protein quality control: triage by chaperones and proteases.

3. The mechanism and functions of ATP-dependent proteases in bacterial and animal cells

4. Regulation by proteolysis: energy-dependent proteases and their targets

5. E. coli contains eight soluble proteolytic activities, one being ATP dependent

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