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ATP-bound states of GroEL captured by cryo-electron microscopy
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title
ATP-bound states of GroEL captured by cryo-electron microscopy
(English)
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main subject
cryogenic electron microscopy
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author
Arthur L. Horwich
series ordinal
6
object named as
A L Horwich
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author name string
N A Ranson
series ordinal
1
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G W Farr
series ordinal
2
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A M Roseman
series ordinal
3
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B Gowen
series ordinal
4
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W A Fenton
series ordinal
5
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H R Saibil
series ordinal
7
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language of work or name
English
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publication date
28 December 2001
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published in
Cell
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volume
107
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page(s)
869-79
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issue
7
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cites work
The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S
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Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
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The crystal structure of the bacterial chaperonin GroEL at 2.8 A
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The Hsp70 and Hsp60 chaperone machines
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The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle
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Release of both native and non-native proteins from a cis-only GroEL ternary complex.
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Folding of malate dehydrogenase inside the GroEL-GroES cavity
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A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL.
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Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy.
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Cryo-electron microscopy of vitrified specimens
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Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.
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Residues in chaperonin GroEL required for polypeptide binding and release
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SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields
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Cooperativity in ATP hydrolysis by GroEL is increased by GroES
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Molecular chaperones in cellular protein folding
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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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Improved methods for building protein models in electron density maps and the location of errors in these models
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Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings
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Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition
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A dynamic model for the allosteric mechanism of GroEL
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Protein folding in the central cavity of the GroEL-GroES chaperonin complex
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Chaperonins
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Docking structures of domains into maps from cryo-electron microscopy using local correlation
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The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.
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Structures of unliganded and ATP-bound states of the Escherichia coli chaperonin GroEL by cryoelectron microscopy
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Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.
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GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings
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Chaperonin function: folding by forced unfolding
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Structure and function in GroEL-mediated protein folding
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Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10
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Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding
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Energy transduction in the F1 motor of ATP synthase
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Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES.
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reference URL
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Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction
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Structural basis of allosteric changes in the GroEL mutant Arg197-->Ala
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The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
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Crossref
reference URL
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inferred from DOI database lookup
Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196-->Ala.
1 reference
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reference URL
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inferred from DOI database lookup
Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.
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inferred from DOI database lookup
Transient kinetic analysis of adenosine 5'-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL
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stated in
Crossref
reference URL
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Identifiers
DOI
10.1016/S0092-8674(01)00617-1
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
829595
OpenCitations bibliographic resource ID
829595
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
829595
PubMed ID
11779463
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
829595
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