(Q57840107)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8603726%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

title

Effect of single point mutations in citrate synthase on binding to GroEL (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8603726%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

0 references

0 references

0 references

0 references

4

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8603726%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

author name string

R Zahn

series ordinal

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8603726%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

P Lindner

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8603726%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

S E Axmann

series ordinal

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8603726%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

language of work or name

English

0 references

publication date

1 February 1996

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8603726%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8603726%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

volume

380

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8603726%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

issue

1-2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8603726%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

page(s)

152-156

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8603726%20AND%20SRC:MED&resulttype=core&format=json

Protein folding in the cell

15 October 2019

cites work

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

Molecular chaperones in protein folding: the art of avoiding sticky situations

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

Electron microscopy and image analysis reveal common principles of organization in two large protein complexes: groEL-type proteins and proteasomes.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

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/10.1016%2F0014-5793%2896%2900013-0

Two-dimensional crystals of the molecular chaperone GroEL reveal structural plasticity.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

Transmission electron microscopy of GroEL, GroES, and the symmetrical GroEL/ES complex.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

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/10.1016%2F0014-5793%2896%2900013-0

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/10.1016%2F0014-5793%2896%2900013-0

Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature beta-lactamase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

Nature and consequences of GroEL-protein interactions.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

GroE prevents the accumulation of early folding intermediates of pre-beta-lactamase without changing the folding pathway.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

Destabilization of the complete protein secondary structure on binding to the chaperone GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

Citrate synthase: structure, control, and mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

Symmetric complexes of GroE chaperonins as part of the functional cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

The hydrophobic nature of GroEL-substrate binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

GroE facilitates refolding of citrate synthase by suppressing aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

Refolding of barnase in the presence of GroE

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2896%2900013-0

10.1016/0014-5793(96)00013-0

21 January 2018

Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8603726%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

1 reference