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  The HtrA family of proteases: Implications for protein composition and cell fate

Clausen, T., Southan, C., & Ehrmann, M. (2002). The HtrA family of proteases: Implications for protein composition and cell fate. Molecular Cell, 10(3), 443-455.

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Genre: Journal Article
Alternative Title : Mol. Cell

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 Creators:
Clausen, T.1, Author              
Southan, C., Author
Ehrmann, M., Author
Affiliations:
1Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              

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 Abstract: Cells precisely monitor the concentration and functionality of each protein for optimal performance. Protein quality control involves molecular chaperones, folding catalysts, and proteases that are often heat shock proteins. One quality control factor is HtrA, one of a new class of oligomeric serine proteases. The defining feature of the HtrA family is the combination of a catalytic domain with at least one C-terminal PDZ domain. Here, we discuss the properties and roles of this ATP-independent protease chaperone system in protein metabolism and cell fate.

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Language(s): eng - English
 Dates: 2002-09
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 39011
ISI: 000178330900005
 Degree: -

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Title: Molecular Cell
  Alternative Title : Mol. Cell
Source Genre: Journal
 Creator(s):
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Publ. Info: -
Pages: - Volume / Issue: 10 (3) Sequence Number: - Start / End Page: 443 - 455 Identifier: ISSN: 1097-2765