(Q54559605)

English

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

scientific article published in August 1997

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/9268318

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

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/9268318

Escherichia coli

0 references

author name string

Hesterkamp T

1

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/9268318

Deuerling E

2

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/9268318

Bukau B

3

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/9268318

language of work or name

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publication date

1 August 1997

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/9268318

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/9268318

272

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/9268318

35

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/9268318

21865-21871

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/9268318

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.35.21865

21 January 2018

The Escherichia coli trigger factor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.35.21865

21 January 2018

ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.35.21865

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.35.21865

21 January 2018

Trigger factor depletion or overproduction causes defective cell division but does not block protein export

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.35.21865

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.35.21865

21 January 2018

Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.35.21865

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.35.21865

21 January 2018

Prediction of protein secondary structure at better than 70% accuracy

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.35.21865

21 January 2018

Identification of the prolyl isomerase domain of Escherichia coli trigger factor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.35.21865

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.35.21865

21 January 2018

Identifiers

10.1074/JBC.272.35.21865

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/9268318

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/9268318

ResearchGate publication ID

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