(Q48297212)

10 February 2018

title

Protein folding in the cell: an inside story. (English)

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10 February 2018

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1

Arthur L Horwich

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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)

1211-1216

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10 February 2018

https://scigraph.springernature.com/pub.10.1038/nm.2468

exact match

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cites work

Principles that govern the folding of protein chains

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Structure and Expression of a Complementary DNA for the Nuclear Coded Precursor of Human Mitochondrial Ornithine Transcarbamylase

21 January 2018

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Import and processing of human ornithine transcarbamoylase precursor by mitochondria from Saccharomyces cerevisiae

21 January 2018

1 reference

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

21 January 2018

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Uncoating ATPase is a member of the 70 kilodalton family of stress proteins.

21 January 2018

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Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria.

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

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Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor

21 January 2018

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Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10.

21 January 2018

1 reference

Protein synthesis in chloroplasts IX. Assembly of newly-synthesized large subunits into ribulose bishopshate carboxylase in isolated intact pea chloroplasts

21 January 2018

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

21 January 2018

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A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1.

21 January 2018

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The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes

21 January 2018

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T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol

21 January 2018

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TCP1 complex is a molecular chaperone in tubulin biogenesis

21 January 2018

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A cytoplasmic chaperonin that catalyzes beta-actin folding

21 January 2018

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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

21 January 2018

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

21 January 2018

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

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

21 January 2018

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Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

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21 January 2018

Binding of chaperonins.

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

21 January 2018

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

21 January 2018

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

21 January 2018

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Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism

21 January 2018

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GroEL-GroES-mediated protein folding

21 January 2018

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Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.

21 January 2018

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The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

21 January 2018

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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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Drifting Through the Year

21 January 2018

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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

21 January 2018

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12 December 2020

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

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12 December 2020

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

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12 December 2020

GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings

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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

Involvement of a bacterial factor in morphogenesis of bacteriophage capsid.

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12 December 2020

Role of the Host Cell in Bacteriophage Morphogenesis: Effects of a Bacterial Mutation on T4 Head Assembly

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12 December 2020

Identifiers

DOI

10.1038/NM.2468

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10 February 2018

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10 February 2018