Protein isoaspartate methyltransferase is a multicopy suppressor of protein aggregation in Escherichia coli (Q33211413)

24 July 2017

title

Protein isoaspartate methyltransferase is a multicopy suppressor of protein aggregation in Escherichia coli (English)

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24 July 2017

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Renée Kern

1

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24 July 2017

Abderrahim Malki

2

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24 July 2017

Jad Abdallah

3

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24 July 2017

Jean-Claude Liebart

4

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24 July 2017

Catherine Dubucs

5

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24 July 2017

Myeong Hee Yu

6

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24 July 2017

Gilbert Richarme

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24 July 2017

language of work or name

English

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publication date

1 February 2005

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24 July 2017

published in

Journal of Bacteriology

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24 July 2017

volume

187

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24 July 2017

issue

4

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24 July 2017

page(s)

1377-1383

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Three-dimensional solution structure of an archaeal FKBP with a dual function of peptidyl prolyl cis-trans isomerase and chaperone-like activities

24 July 2017

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21 June 2018

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21 June 2018

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21 June 2018

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21 June 2018

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21 June 2018

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21 June 2018

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21 June 2018

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The L-isoaspartyl protein repair methyltransferase enhances survival of aging Escherichia coli subjected to secondary environmental stresses

21 June 2018

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21 June 2018

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The nlpD gene is located in an operon with rpoS on the Escherichia coli chromosome and encodes a novel lipoprotein with a potential function in cell wall formation

21 June 2018

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21 June 2018

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21 June 2018

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21 June 2018

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21 June 2018

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21 June 2018

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21 June 2018

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21 June 2018

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Structural elements affecting the recognition of L-isoaspartyl residues by the L-isoaspartyl/D-aspartyl protein methyltransferase. Implications for the repair hypothesis

21 June 2018

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21 June 2018

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21 June 2018

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Overexpression of l-Isoaspartate O-Methyltransferase in Escherichia coli Increases Heat Shock Survival by a Mechanism Independent of Methyltransferase Activity

21 June 2018

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31 October 2018

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31 October 2018

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31 October 2018

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12 December 2020

Purification and properties of the Escherichia coli heat shock protein, HtpG

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12 December 2020

Defect in export and synthesis of the periplasmic galactose receptor MglB in dnaK mutants of Escherichia coli, and decreased stability of the mglB mRNA

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Protein Disulfide Isomerase Acts as a Redox-Dependent Chaperone to Unfold Cholera Toxin

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10.1128/JB.187.4.1377-1383.2005

Identifiers

DOI

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24 July 2017

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24 July 2017

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