Literature DB >> 8824426

Selective, energy-dependent proteolysis in Escherichia coli.

S Gottesman1, S Wickner, Y Jubete, S K Singh, M Kessel, M Maurizi.   

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Year:  1995        PMID: 8824426     DOI: 10.1101/sqb.1995.060.01.057

Source DB:  PubMed          Journal:  Cold Spring Harb Symp Quant Biol        ISSN: 0091-7451


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  6 in total

1.  Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP.

Authors:  S K Singh; R Grimaud; J R Hoskins; S Wickner; M R Maurizi
Journal:  Proc Natl Acad Sci U S A       Date:  2000-08-01       Impact factor: 11.205

2.  Lon and Clp family proteases and chaperones share homologous substrate-recognition domains.

Authors:  C K Smith; T A Baker; R T Sauer
Journal:  Proc Natl Acad Sci U S A       Date:  1999-06-08       Impact factor: 11.205

3.  Structure of the N-terminal fragment of Escherichia coli Lon protease.

Authors:  Mi Li; Alla Gustchina; Fatima S Rasulova; Edward E Melnikov; Michael R Maurizi; Tatyana V Rotanova; Zbigniew Dauter; Alexander Wlodawer
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2010-07-09

4.  Metabolic instability of Escherichia coli cyclopropane fatty acid synthase is due to RpoH-dependent proteolysis.

Authors:  Y Y Chang; J Eichel; J E Cronan
Journal:  J Bacteriol       Date:  2000-08       Impact factor: 3.490

5.  ClpXP and ClpAP control the Escherichia coli division protein ZapC by proteolysis.

Authors:  Monika S Buczek; Andrea L Cardenas Arevalo; Anuradha Janakiraman
Journal:  Microbiology       Date:  2016-03-15       Impact factor: 2.777

6.  Limited proteolysis of E. coli ATP-dependent protease Lon - a unified view of the subunit architecture and characterization of isolated enzyme fragments.

Authors:  Edward E Melnikov; Anna G Andrianova; Andrey D Morozkin; Anton A Stepnov; Oksana V Makhovskaya; Istvan Botos; Alla Gustchina; Alexander Wlodawer; Tatyana V Rotanova
Journal:  Acta Biochim Pol       Date:  2008-05-26       Impact factor: 2.149

  6 in total

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