Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. (Q54500735)

30 May 2018

title

Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. (English)

1 reference

30 May 2018

Holger Patzelt

3

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Nenad Ban

series ordinal

6

object named as

Nenad Ban

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30 May 2018

4

Bernd Bukau

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30 May 2018

5

Elke Deuerling

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30 May 2018

Lars Ferbitz

1

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30 May 2018

Timm Maier

series ordinal

2

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30 May 2018

language of work or name

English

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publication date

29 August 2004

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30 May 2018

number of pages

7

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inferred from page(s)

published in

Nature

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30 May 2018

volume

431

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30 May 2018

issue

7008

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30 May 2018

page(s)

590-596

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30 May 2018

https://scigraph.springernature.com/pub.10.1038/nature02899

exact match

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cites work

Getting newly synthesized proteins into shape.

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

Molecular chaperones in the cytosol: from nascent chain to folded protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

Ribosome structure and the mechanism of translation

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

The complete atomic structure of the large ribosomal subunit at 2.4 A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

The structural basis of ribosome activity in peptide bond synthesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

Recombination of protein domains facilitated by co-translational folding in eukaryotes.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

L23 protein functions as a chaperone docking site on the ribosome

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

Chaperone binding at the ribosomal exit tunnel

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

The Periplasmic Molecular Chaperone Protein SurA Binds a Peptide Motif That Is Characteristic of Integral Outer Membrane Proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

Interaction of trigger factor with the ribosome

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

Structure of the signal recognition particle interacting with the elongation-arrested ribosome.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

Distinct modes of signal recognition particle interaction with the ribosome

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

Automated MAD and MIR structure solution

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

Folding of a nascent peptide on the ribosome

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

7 January 2021

Co-translational folding of an alphavirus capsid protein in the cytosol of living cells

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

7 January 2021

Three-state equilibrium of Escherichia coli trigger factor

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

7 January 2021

Common principles of protein translocation across membranes

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

7 January 2021

Processing of X-ray diffraction data collected in oscillation mode

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02899

7 January 2021

Identifiers

DOI

10.1038/NATURE02899

1 reference

30 May 2018

Dimensions Publication ID

0 references

1 reference

30 May 2018