Compensatory changes in GroEL/Gp31 affinity as a mechanism for allele-specific genetic interaction (Q56896714)

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scientific article published in Journal of Biological Chemistry

Compensatory Changes in GroEL/Gp31 Affinity as a Mechanism for Allele-specific Genetic Interaction

Language	Label	Description	Also known as
English	Compensatory changes in GroEL/Gp31 affinity as a mechanism for allele-specific genetic interaction	scientific article published in Journal of Biological Chemistry	Compensatory Changes in GroEL/Gp31 Affinity as a Mechanism for Allele-specific Genetic Interaction

Statements

scholarly article

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Compensatory changes in GroEL/Gp31 affinity as a mechanism for allele-specific genetic interaction (English)

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Compensatory Changes in GroEL/Gp31 Affinity as a Mechanism for Allele-specific Genetic Interaction (English)

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author name string

A Richardson

1

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S M van der Vies

2

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F Keppel

3

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A Taher

4

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S J Landry

5

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C Georgopoulos

6

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Alexandra Richardson

1

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Saskia M. van der Vies

2

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France Keppel

3

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Abida Taher

4

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Samuel J. Landry

5

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Costa Georgopoulos

6

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language of work or name

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publication date

1 January 1999

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Journal of Biological Chemistry

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274

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1

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52-8

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52-58

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Molecular chaperones in cellular protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

In vivo observation of polypeptide flux through the bacterial chaperonin system.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Purification and properties of groE, a host protein involved in bacteriophage assembly

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

The Hsp70 and Hsp60 chaperone machines

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

GroEL-mediated protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

The ins and outs of a molecular chaperone machine.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Drifting Through the Year

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

The emergence of the chaperone machines

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Conserved sequence motifs in bacterial and bacteriophage chaperonins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Characterization of a functionally important mobile domain of GroES.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Interplay of structure and disorder in cochaperonin mobile loops

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Two classes of extragenic suppressor mutations identify functionally distinct regions of the GroEL chaperone of Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Sequence analysis and phenotypic characterization of groEL mutations that block lambda and T4 bacteriophage growth

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

A new set of useful cloning and expression vectors derived from pBlueScript.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Renaturation of citrate synthase: influence of denaturant and folding assistants

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Interaction of the cheC and cheZ gene products is required for chemotactic behavior in Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Conformation of beta hairpins in protein structures: classification and diversity in homologous structures.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Context is a major determinant of β-sheet propensity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

The structure of an actin-crosslinking domain from human fimbrin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

A chemotactic signaling surface on CheY defined by suppressors of flagellar switch mutations

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Molecular analysis of the flagellar switch protein FliM of Salmonella typhimurium

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Deciphering the message in protein sequences: tolerance to amino acid substitutions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.1.52

21 January 2018

Identifiers

10.1074/JBC.274.1.52

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