Substrate mutations that bypass a specific Cpn10 chaperonin requirement for protein folding (Q77677831)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9852065%20AND%20SRC:MED&resulttype=core&format=json

7 December 2019

title

Substrate mutations that bypass a specific Cpn10 chaperonin requirement for protein folding (English)

1 reference

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7 December 2019

author name string

J D Andreadis

series ordinal

1

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7 December 2019

L W Black

series ordinal

2

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7 December 2019

language of work or name

English

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publication date

1 December 1998

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Journal of Biological Chemistry

7 December 2019

published in

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7 December 2019

volume

273

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7 December 2019

issue

51

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7 December 2019

page(s)

34075-34086

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

7 December 2019

cites work

1 reference

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Molecular chaperone functions of heat-shock proteins

21 January 2018

1 reference

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The universally conserved GroE (Hsp60) chaperonins

21 January 2018

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The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

21 January 2018

1 reference

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

21 January 2018

1 reference

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A polypeptide bound by the chaperonin groEL is localized within a central cavity

21 January 2018

1 reference

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

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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21 January 2018

Binding of chaperonins.

1 reference

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Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

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

21 January 2018

1 reference

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Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

1 reference

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The lid that shapes the pot: structure and function of the chaperonin GroES.

21 January 2018

1 reference

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Refolding of barnase in the presence of GroE

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

GroEL-mediated folding of structurally homologous dihydrofolate reductases.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Complexes between chaperonin GroEL and the capsid protein of bacteriophage HK97

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Assembly of membrane-containing bacteriophage PRD1 is dependent on GroEL and GroES.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Abortive bacteriophage T4 head assembly in mutants of Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Drifting Through the Year

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Developments in the Physics of Elementary Particles

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Protein folding within the cell is influenced by controlled rates of polypeptide elongation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Ribosome-mediated translational pause and protein domain organization

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Expression of synthetic suppressor tRNA genes under the control of a synthetic promoter.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Use of T7 RNA polymerase to direct expression of cloned genes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Monomer-heptamer equilibrium of the Escherichia coli chaperonin GroES.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Site-directed mutagenesis by overlap extension using the polymerase chain reaction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Assembly of bacteriophage T4 head-related structures assembly of polyheads in Vitro

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Synonymous codon preferences in bacteriophage T4: A distinctive use of transfer RNAs from T4 and from its host Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

The efficiency of folding of some proteins is increased by controlled rates of translation in vivo. A hypothesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Bacterial mutation affecting T4 phage DNA synthesis and tail production

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Interplay of structure and disorder in cochaperonin mobile loops

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Characterization of a functionally important mobile domain of GroES.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Assembly Core of Bacteriophage T4: an Intermediate in Head Formation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Mutations that eliminate the requirement for the vertex protein in bacteriophage T4 capsid assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Modulation of bacteriophage T4 capsid size

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Protein folding. Secrets of a double-doughnut.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

The maturation-dependent conformational change of phage T4 capsid involves the translocation of specific epitopes between the inner and the outer capsid surfaces

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

Form-determining function of the genes required for the assembly of the head of bacteriophage T4

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.51.34075

21 January 2018

Identifiers

DOI

10.1074/JBC.273.51.34075

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9852065%20AND%20SRC:MED&resulttype=core&format=json

7 December 2019

1 reference