(Q43690558)

25 November 2017

title

Metal ions modulate the plastic nature of Mycobacterium tuberculosis chaperonin-10. (English)

1 reference

Mycobacterium tuberculosis

25 November 2017

main subject

0 references

author name string

Taneja B

series ordinal

1

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25 November 2017

Mande SC

series ordinal

2

1 reference

25 November 2017

publication date

1 June 2001

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Protein Engineering Design and Selection

25 November 2017

published in

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25 November 2017

volume

14

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25 November 2017

issue

6

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25 November 2017

page(s)

391-395

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The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999.

25 November 2017

cites work

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.6.391

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

21 January 2018

1 reference

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

1 reference

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GroEL-substrate interactions: molding the fold, or folding the mold?

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.6.391

Mycobacterium tuberculosis chaperonin 10 forms stable tetrameric and heptameric structures. Implications for its diverse biological activities.

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.6.391

Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.6.391

Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.

21 January 2018

1 reference

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.6.391

Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae

21 January 2018

1 reference

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Raster3D Version 2.0. A program for photorealistic molecular graphics

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.6.391

Chaperonin function: folding by forced unfolding

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.6.391

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.6.391

The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.6.391

The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F14.6.391

21 January 2018

Identifiers

DOI

10.1093/PROTEIN/14.6.391

1 reference

25 November 2017

1 reference