(Q54558765)

31 May 2018

title

Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR. (English)

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31 May 2018

3

Wüthrich K

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31 May 2018

author name string

Nieba-Axmann SE

series ordinal

1

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31 May 2018

Ottiger M

series ordinal

2

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31 May 2018

Plückthun A

series ordinal

4

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31 May 2018

language of work or name

English

0 references

publication date

1 September 1997

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31 May 2018

Journal of Molecular Biology

published in

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31 May 2018

volume

271

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31 May 2018

page(s)

803-818

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31 May 2018

issue

5

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31 May 2018

Primary structure effects on peptide group hydrogen exchange

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11 October 2022

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A thermodynamic coupling mechanism for GroEL-mediated unfolding

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beta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange

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Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling

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The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Kinetics of hydrogen bond breakage in the process of unfolding of ribonuclease A measured by pulsed hydrogen exchange

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

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

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution

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https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Relationship between equilibrium amide proton exchange behavior and the folding pathway of barnase.

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https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR.

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https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Residues in chaperonin GroEL required for polypeptide binding and release

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

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

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy

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https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

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

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

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https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Hydrogen exchange and structural dynamics of proteins and nucleic acids

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https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Conformational states bound by the molecular chaperones GroEL and secB: a hidden unfolding (annealing) activity

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

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

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

The hydrophobic nature of GroEL-substrate binding

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Processing of multi-dimensional NMR data with the new software PROSA

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Amide proton exchange in proteins by EX1 kinetics: studies of the basic pancreatic trypsin inhibitor at variable p2H and temperature.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

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

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

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

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

The NMR solution conformation of unligated human cyclophilin A

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Protein folding kinetics by combined use of rapid mixing techniques and NMR observation of individual amide protons

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Protein stability parameters measured by hydrogen exchange

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

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

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Hydrogen Exchange in Proteins

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

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

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

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

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Protein secondary structure determination by NMR. Application with recombinant human cyclophilin.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Mechanisms and uses of hydrogen exchange

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

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

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

IFLAT—A New Automatic Baseline-Correction Method for Multidimensional NMR Spectra with Strong Solvent Signals

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Protein folding in the cell

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Refolding of barnase in the presence of GroE

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Allosteric control by ATP of non-folded protein binding to GroEL

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.1997.1192

Identifiers

DOI

10.1006/JMBI.1997.1192

1 reference

31 May 2018

release_k2fbdg5h2rc27jjwzcv74vcgre

Fatcat ID

1 reference

https://api.fatcat.wiki/v0/release/k2fbdg5h2rc27jjwzcv74vcgre

Fatcat

reference URL

retrieved

24 November 2022

based on heuristic

mapped directly with Wikidata item

PubMed ID

9299328

1 reference

31 May 2018