Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding. (Q54635587)

1 June 2018

title

Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding. (English)

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1 June 2018

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van der Vies SM

1

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1 June 2018

Gatenby AA

series ordinal

2

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1 June 2018

Georgopoulos C

series ordinal

3

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1 June 2018

language of work or name

English

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publication date

1 April 1994

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1 June 2018

published in

Nature

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1 June 2018

volume

368

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1 June 2018

issue

6472

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1 June 2018

page(s)

654-656

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1 June 2018

https://scigraph.springernature.com/pub.10.1038/368654a0

exact match

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cites work

The universally conserved GroE (Hsp60) chaperonins

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7 January 2021

A factor preventing the major head protein of bacteriophage T4 from random aggregation

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7 January 2021

Role of the Host Cell in Bacteriophage Morphogenesis: Effects of a Bacterial Mutation on T4 Head Assembly

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7 January 2021

Mutational analysis of the phage T4 morphogenetic 31 gene, whose product interacts with the Escherichia coli GroEL protein

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7 January 2021

Cloning, sequence, and expression of the temperature-dependent phage T4 capsid assembly gene 31.

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7 January 2021

Characterization of a functionally important mobile domain of GroES.

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7 January 2021

Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes

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7 January 2021

Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins

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7 January 2021

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

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7 January 2021

GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.

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7 January 2021

Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent

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7 January 2021

Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

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7 January 2021

Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.

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7 January 2021

Properties of a mutant of Escherichia coli defective in bacteriophage lambda head formation (groE). I. Initial characterization

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7 January 2021

Assembly in E. coli of a functional multi-subunit ribulose bisphosphate carboxylase from a blue-green alga

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7 January 2021

D-Ribulose-1,5-bisphosphate carboxylase-oxygenase. Improved methods for the activation and assay of catalytic activities

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7 January 2021

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

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7 January 2021

Identifiers

DOI

10.1038/368654A0

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1 June 2018

Dimensions Publication ID

1030608079

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Fatcat ID

release_g24nicvoozgz5incdi2afdjuhm

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Fatcat

https://api.fatcat.wiki/v0/release/g24nicvoozgz5incdi2afdjuhm

24 November 2022

mapped directly with Wikidata item

PubMed ID

7908418

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1 June 2018