Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli (Q34384407)

1 August 2017

title

Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli (English)

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1 August 2017

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Yoo SJ

1

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Seol JH

2

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Shin DH

3

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Rohrwild M

4

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Kang MS

5

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Tanaka K

6

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Goldberg AL

7

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Chung CH

8

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language of work or name

English

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publication date

1 June 1996

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Journal of Biological Chemistry

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published in

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volume

271

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issue

24

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1 August 2017

page(s)

14035-14040

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

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cites work

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Escherichia coli contains a soluble ATP-dependent protease (Ti) distinct from protease La.

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Addiction protein Phd of plasmid prophage P1 is a substrate of the ClpXP serine protease of Escherichia coli

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Characterization of twenty-six new heat shock genes of Escherichia coli

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Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli.

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Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Distinctive roles of the two ATP-binding sites in ClpA, the ATPase component of protease Ti in Escherichia coli

21 January 2018

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Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome

21 January 2018

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Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules

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21 January 2018

Identifiers

DOI

10.1074/JBC.271.24.14035

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1 August 2017

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