(Q48297216)

10 February 2018

title

Chaperone-assisted protein folding: the path to discovery from a personal perspective (English)

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10 February 2018

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1

F Ulrich Hartl

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10 February 2018

language of work or name

English

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publication date

11 October 2011

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10 February 2018

published in

Nature Medicine

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10 February 2018

volume

17

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10 February 2018

issue

10

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10 February 2018

page(s)

1206-1210

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10 February 2018

https://scigraph.springernature.com/pub.10.1038/nm.2467

exact match

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cites work

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70K heat shock related proteins stimulate protein translocation into microsomes.

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A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides

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Speculations on the functions of the major heat shock and glucose-regulated proteins

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Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

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A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

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Proteins as molecular chaperones.

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Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

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

21 January 2018

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

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A polypeptide bound by the chaperonin groEL is localized within a central cavity

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

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Protein folding in the cell: molecular chaperones pave the way.

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

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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GroEL structure: a new chapter on assisted folding

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

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

21 January 2018

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

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

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

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A systematic survey of in vivo obligate chaperonin-dependent substrates

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Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

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Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding

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Monitoring Protein Conformation along the Pathway of Chaperonin-Assisted Folding

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Unfolding protein folding

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12 December 2020

Lord of the rings: GroES structure

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Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity

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

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Abortive bacteriophage T4 head assembly in mutants of Escherichia coli

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12 December 2020

Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductase

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12 December 2020

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

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12 December 2020

DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.

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12 December 2020

Peptide binding and release by proteins implicated as catalysts of protein assembly

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12 December 2020

Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs

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12 December 2020

Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits

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12 December 2020

Identifiers

DOI

10.1038/NM.2467

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10 February 2018

Dimensions Publication ID

1011803139

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10 February 2018