The crystal structure of the bacterial chaperonin GroEL at 2.8 A (Q27730725)

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object named as

A L Horwich

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Andrzej Joachimiak

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object named as

A Joachimiak

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author name string

K Braig

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R Hegde

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D C Boisvert

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P B Sigler

https://api.crossref.org/works/10.1038%2F371578A0

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language of work or name

English

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publication date

13 October 1994

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published in

Nature

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volume

371

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issue

6498

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page(s)

578-86

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Protein folding in the cell

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Molecular chaperone functions of heat-shock proteins

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Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1

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

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A normal mitochondrial protein is selectively synthesized and accumulated during heat shock in Tetrahymena thermophila

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

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A cytoplasmic chaperonin that catalyzes beta-actin folding

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

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Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.

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

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

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

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Different conformations for the same polypeptide bound to chaperones DnaK and GroEL.

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

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The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state

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

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

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Folding intermediate binds to the bottom of bullet-shaped holo-chaperonin and is readily accessible to antibody.

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

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Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.

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

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Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer

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Symmetric complexes of GroE chaperonins as part of the functional cycle

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

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Residues in chaperonin GroEL required for polypeptide binding and release

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Improved Fourier coefficients for maps using phases from partial structures with errors

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Assessment of protein models with three-dimensional profiles

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The interpretation of protein structures: Estimation of static accessibility

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Surface, subunit interfaces and interior of oligomeric proteins

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The structure of interfaces between subunits of dimeric and tetrameric proteins

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

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The strongly conserved carboxyl-terminus glycine-methionine motif of the Escherichia coli GroEL chaperonin is dispensable.

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The symmetry of Escherichia coli cpn60 (GroEL) determined by X-ray crystallography.

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