(Q77985253)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10400632%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

title

Analysis of GroE-assisted folding under nonpermissive conditions (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10400632%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

author name string

H Grallert

series ordinal

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10400632%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

J Buchner

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10400632%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

language of work or name

English

0 references

publication date

1 July 1999

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10400632%20AND%20SRC:MED&resulttype=core&format=json

Journal of Biological Chemistry

10 December 2019

published in

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10400632%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

volume

274

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10400632%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

issue

29

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10400632%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

page(s)

20171-20177

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10400632%20AND%20SRC:MED&resulttype=core&format=json

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

10 December 2019

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

Prevention of protein denaturation under heat stress by the chaperonin Hsp60

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

GroES binding regulates GroEL chaperonin activity under heat shock

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

Dynamics of the GroEL-protein complex: effects of nucleotides and folding mutants.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. I. GroEL recognizes the signal sequences of beta-lactamase precursor.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

Interaction of GroEL with conformational states of horse cytochrome c

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

ATP induces large quaternary rearrangements in a cage-like chaperonin structure

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

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.274.29.20171

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

Catalysis of protein folding by symmetric chaperone complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

The influence of chaperonins on protein folding. A mechanism for increasing the yield of the native form

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

Protein folding in the central cavity of the GroEL-GroES chaperonin complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

GroEL traps dimeric and monomeric unfolding intermediates of citrate synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

Calculation of protein extinction coefficients from amino acid sequence data

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

Fluorescence of Proteins in 6-M Guanidine Hydrochloride. A Method for the Quantitative Determination of Tryptophan

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

Biochemical methods for analysis of histone deacetylases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

GroE modulates kinetic partitioning of folding intermediates between alternative states to maximize the yield of biologically active protein.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

Chaperonin function: folding by forced unfolding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

Protein folding Folding with a two-stroke motor

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

A structural model for GroEL-polypeptide recognition

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.29.20171

21 January 2018

Identifiers

DOI

10.1074/JBC.274.29.20171

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10400632%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

1 reference