(Q44298013)

1 December 2017

title

Interaction of trigger factor with the ribosome (English)

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1 December 2017

Raimund Maier

1

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1 December 2017

Barbara Eckert

2

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1 December 2017

Christian Scholz

3

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1 December 2017

Hauke Lilie

4

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1 December 2017

Franz-Xaver Schmid

5

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1 December 2017

language of work or name

English

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publication date

1 February 2003

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Journal of Molecular Biology

1 December 2017

published in

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1 December 2017

volume

326

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1 December 2017

issue

2

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1 December 2017

page(s)

585-592

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Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form

1 December 2017

cites work

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https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor

7 January 2021

1 reference

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Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

Identification of the prolyl isomerase domain of Escherichia coli trigger factor

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

Modular structure of the trigger factor required for high activity in protein folding.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

Trigger factor, one of the Escherichia coli chaperone proteins, is an original member of the FKBP family

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl-prolyl cis/trans isomerase activity.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

Dynamic association of trigger factor with protein substrates

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

Binding specificity of Escherichia coli trigger factor

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

Recognition of protein substrates by the prolyl isomerase trigger factor is independent of proline residues

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

Trigger factor and DnaK cooperate in folding of newly synthesized proteins.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains

7 January 2021

1 reference

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The Hsp70 and Hsp60 chaperone machines

7 January 2021

1 reference

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Getting newly synthesized proteins into shape.

7 January 2021

1 reference

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The second step of ATP binding to DnaK induces peptide release.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

Catapult mechanism renders the chaperone action of Hsp70 unidirectional

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding

7 January 2021

1 reference

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Kinetics of peptide binding to the bovine 70 kDa heat shock cognate protein, a molecular chaperone

7 January 2021

1 reference

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ATP lowers the activation enthalpy barriers to DnaK-peptide complex formation and dissociation

7 January 2021

1 reference

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The functional cycle and regulation of the Thermus thermophilus DnaK chaperone system

7 January 2021

1 reference

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The "trigger factor cycle" includes ribosomes, presecretory proteins, and the plasma membrane

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

L23 protein functions as a chaperone docking site on the ribosome

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

Prolyl isomerases in a minimal cell. Catalysis of protein folding by trigger factor from Mycoplasma genitalium.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

Polypeptide elongation and tRNA cycling in Escherichia coli: a dynamic approach

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

Cyclophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

Trigger factor associates with GroEL in vivo and promotes its binding to certain polypeptides

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

Intact disulfide bonds decelerate the folding of ribonuclease T1

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

Calculation of protein extinction coefficients from amino acid sequence data

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

Evaluation of human immunodeficiency virus type 1 reverse transcriptase primer tRNA binding by fluorescence spectroscopy: specificity and comparison to primer/template binding

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2901427-4

10.1016/S0022-2836(02)01427-4

7 January 2021

Identifiers

DOI

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1 December 2017

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