Department of Genetics
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ClpS, a substrate modulator of the ClpAP machine.
Molecular cell Mar, 2002 | Pubmed ID: 11931773
NMR analysis of a 900K GroEL GroES complex.
Nature Jul, 2002 | Pubmed ID: 12110894
Solution NMR techniques for large molecular and supramolecular structures.
Journal of the American Chemical Society Oct, 2002 | Pubmed ID: 12371854
Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes.
The EMBO journal Jul, 2003 | Pubmed ID: 12839985
Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics.
The EMBO journal Oct, 2003 | Pubmed ID: 14517228
Chaperonin-mediated protein folding: fate of substrate polypeptide.
Quarterly reviews of biophysics May, 2003 | Pubmed ID: 14686103
Uniform and residue-specific 15N-labeling of proteins on a highly deuterated background.
Journal of biomolecular NMR Jul, 2004 | Pubmed ID: 15213427
Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states.
Journal of molecular biology Sep, 2004 | Pubmed ID: 15313620
A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation.
Nature structural & molecular biology Nov, 2004 | Pubmed ID: 15475965
Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL.
Proceedings of the National Academy of Sciences of the United States of America Oct, 2004 | Pubmed ID: 15479763
Chaperoned protein disaggregation--the ClpB ring uses its central channel.
Cell Nov, 2004 | Pubmed ID: 15550237
No evidence for a forced-unfolding mechanism during ATP/GroES binding to substrate-bound GroEL: no observable protection of metastable Rubisco intermediate or GroEL-bound Rubisco from tritium exchange.
FEBS letters Feb, 2005 | Pubmed ID: 15710410
Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation.
Cell Jul, 2005 | Pubmed ID: 15989953
Direct NMR observation of a substrate protein bound to the chaperonin GroEL.
Proceedings of the National Academy of Sciences of the United States of America Sep, 2005 | Pubmed ID: 16116078
Roles of the N-domains of the ClpA unfoldase in binding substrate proteins and in stable complex formation with the ClpP protease.
The Journal of biological chemistry Dec, 2005 | Pubmed ID: 16207718
Probing the sequence of conformationally induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopy.
The journal of physical chemistry. B Dec, 2005 | Pubmed ID: 16375456
Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes.
Nature structural & molecular biology Feb, 2006 | Pubmed ID: 16429154
GroEL-GroES-mediated protein folding.
Chemical reviews May, 2006 | Pubmed ID: 16683761
Proton-proton Overhauser NMR spectroscopy with polypeptide chains in large structures.
Proceedings of the National Academy of Sciences of the United States of America Oct, 2006 | Pubmed ID: 17032756
Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL.
Proceedings of the National Academy of Sciences of the United States of America Oct, 2006 | Pubmed ID: 17043235
Disulfide formation as a probe of folding in GroEL-GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones.
Proceedings of the National Academy of Sciences of the United States of America Feb, 2007 | Pubmed ID: 17283341
Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL.
Proceedings of the National Academy of Sciences of the United States of America Mar, 2007 | Pubmed ID: 17372195
Two families of chaperonin: physiology and mechanism.
Annual review of cell and developmental biology , 2007 | Pubmed ID: 17489689
Topologies of a substrate protein bound to the chaperonin GroEL.
Molecular cell May, 2007 | Pubmed ID: 17499047
Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution.
Proceedings of the National Academy of Sciences of the United States of America Dec, 2007 | Pubmed ID: 18093916
Multiple states of a nucleotide-bound group 2 chaperonin.
Structure (London, England : 1993) Apr, 2008 | Pubmed ID: 18400175
Chaperonin chamber accelerates protein folding through passive action of preventing aggregation.
Proceedings of the National Academy of Sciences of the United States of America Nov, 2008 | Pubmed ID: 18987317
Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active state.
Proceedings of the National Academy of Sciences of the United States of America Dec, 2008 | Pubmed ID: 19050077
A small molecule inhibitor selective for a variant ATP-binding site of the chaperonin GroEL.
Bioorganic & medicinal chemistry letters Feb, 2009 | Pubmed ID: 19110421
An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans.
PLoS genetics Jan, 2009 | Pubmed ID: 19165329
Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS.
Proceedings of the National Academy of Sciences of the United States of America Feb, 2009 | Pubmed ID: 19171884
The GroEL/GroES cis cavity as a passive anti-aggregation device.
FEBS letters Aug, 2009 | Pubmed ID: 19577567
Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding.
Quarterly reviews of biophysics May, 2009 | Pubmed ID: 19638247
GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state.
Proceedings of the National Academy of Sciences of the United States of America Dec, 2009 | Pubmed ID: 19915138
ATP-triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP7 is not the rate-limiting step of the GroEL/GroES reaction cycle.
FEBS letters Mar, 2010 | Pubmed ID: 20083109
Double mutant MBP refolds at same rate in free solution as inside the GroEL/GroES chaperonin chamber when aggregation in free solution is prevented.
FEBS letters Jun, 2011 | Pubmed ID: 21609718
Nuclear magnetic resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL.
Protein science : a publication of the Protein Society Aug, 2011 | Pubmed ID: 21633984
Hydrogen-deuterium exchange in vivo to measure turnover of an ALS-associated mutant SOD1 protein in spinal cord of mice.
Protein science : a publication of the Protein Society Oct, 2011 | Pubmed ID: 21780215
Localization of GroEL determined by in vivo incorporation of a fluorescent amino acid.
Bioorganic & medicinal chemistry letters Oct, 2011 | Pubmed ID: 21890355
Translational diffusion of macromolecular assemblies measured using transverse-relaxation-optimized pulsed field gradient NMR.
Journal of the American Chemical Society Oct, 2011 | Pubmed ID: 21919531
Protein folding in the cell: an inside story.
Nature medicine Oct, 2011 | Pubmed ID: 21989012
QnAs with Arthur L. Horwich. Interview by Prashant Nair.
Proceedings of the National Academy of Sciences of the United States of America Feb, 2012 | Pubmed ID: 22308493
ATP-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL chaperonin.
Cell Mar, 2012 | Pubmed ID: 22445172
Structure and allostery of the chaperonin GroEL.
Journal of molecular biology May, 2013 | Pubmed ID: 23183375
RNA-Seq profiling of spinal cord motor neurons from a presymptomatic SOD1 ALS mouse.
PloS one , 2013 | Pubmed ID: 23301088
Recessive loss of function of the neuronal ubiquitin hydrolase UCHL1 leads to early-onset progressive neurodegeneration.
Proceedings of the National Academy of Sciences of the United States of America Feb, 2013 | Pubmed ID: 23359680
Molecular chaperone Hsp110 rescues a vesicle transport defect produced by an ALS-associated mutant SOD1 protein in squid axoplasm.
Proceedings of the National Academy of Sciences of the United States of America Apr, 2013 | Pubmed ID: 23509252
Chaperonin-mediated protein folding.
The Journal of biological chemistry Aug, 2013 | Pubmed ID: 23803606
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