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Arthur Horwich (Amerikaans bioloog)
Arthur Horwich (US-amerikanischer Zellbiologe)
Arthur L. Horwich (American biologist)
2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S., The
Abstracts of papers presented at the 1998 meeting on molecular chaperones and the heat shock response, 1998:
Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes
ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans., An
Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space.
ATP-bound states of GroEL captured by cryo-electron microscopy.
carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K-12., A
Chaperone rings in protein folding and degradation.
Chaperoned Protein Disaggregation; The ClpB Ring Uses Its Central Channel
Chaperonin chamber accelerates protein folding through passive action of preventing aggregation
Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and nonnative forms.
Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate.
Chaperonin-mediated protein folding: fate of substrate polypeptide
Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding
Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction.
ClpA mediates directional translocation of substrate proteins into the ClpP protease.
ClpS, a substrate modulator of the ClpAP machine.
Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL.
crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex., The
crystal structure of the asymmetric GroEL-GroES-ADP7 chaperonin complex., The
crystal structure of the bacterial chaperonin GroEL at 2.8 A., The
Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains.
Deadly conformations - Protein misfolding in prion disease
Direct NMR observation of a substrate protein bound to the chaperonin GroEL.
Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.
Disulfide formation as a probe of folding in GroEL-GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones
Exploring the Structural Dynamics of the E.coli Chaperonin GroEL Using Translation-libration-screw Crystallographic Refinement of Intermediate States
Fenton et al Residues in chaperonin GroEL required for polypeptide binding and release
Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins
Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.
Folding of malate dehydrogenase inside the GroEL-GroES cavity
Folding trajectories of human dihydrofolate reductase inside the GroEL-GroES chaperonin cavity and free in solution
Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes
From the cradle to the grave: Ring complexes in the life of a protein
Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL
Global unfolding of a substrate protein by the Hsp100 chaperone ClpA
GroEL/GroES cis cavity as a passive anti-aggregation device., The
GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings.
GroEL/GroES-mediated folding of a protein too large to be encapsulated.
GroEL-GroES-Mediated Protein Folding
GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms.
Heat shock proteins and molecular chaperones: Mediators of protein conformation and turnover in the cell
Hepadnavirus envelope proteins regulate covalently closed circular DNA amplification.
High-resolution gold labeling
Hsp70 and Hsp60 chaperone machines, The
Inaugural Article by a Recently Elected Academy Member: Inaugural Article: Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL
Inherited hepatic enzyme defects as candidates for liver-directed gene therapy.
Isolation and characterisation of a new leukaemia virus mutant
Kinesis of polypeptide during GroEL-mediated folding.
Loops in the Central Channel of ClpA Chaperone Mediate Protein Binding, Unfolding, and Translocation
Mechanism of action of the Hsp100 chaperone, ClpA
Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under GroES
mitochondrial chaperonin hsp60 is required for its own assembly., The
Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria.
Mitochondrial protein import.
molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1., A
Molecular chaperones in biology and medicine at Obernai.
Multiple states of a nucleotide-bound group 2 chaperonin.
Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.
mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation, A
Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL
NMR analysis of a 900 kDa GroEL/GroES chaperonin complex
NMR analysis of a 900K GroEL--GroES complex
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.
Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL
polypeptide bound by the chaperonin groEL is localized within a central cavity., A
Precarious Balance of Nitrogen Metabolism in Women with a Urea-Cycle Defect
Prevention of protein denaturation under heat stress by the chaperonin Hsp60.
Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS
Protein aggregation in disease : a role for folding intermediates forming specific multimeric interactions
Protein aggregation in disease: A role of folding intermediates forming specific multimeric interactions
Protein-catalysed protein folding.
Protein folding causes an arrest of preprotein translocation into mitochondria in vivo.
Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis.
Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1.
Protein folding taking shape. Workshop on molecular chaperones.
Protein import into mitochondria and peroxisomes.
Proton-proton Overhauser NMR spectroscopy with polypeptide chains in large structures.
Putting a lid on protein folding: structure and function of the co-chaperonin, GroES.
Release of both native and non-native proteins from a cis-only GroEL ternary complex.
Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active state.
Residues in chaperonin GroEL required for polypeptide binding and release
Role of the [gamma]-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics
Roles of the N-domains of the ClpA Unfoldase in Binding Substrate Proteins and in Stable Complex Formation with the ClpP Protease.
Short-term response to dietary therapy in molybdenum cofactor deficiency.
small molecule inhibitor selective for a variant ATP-binding site of the chaperonin GroEL, A
Solution NMR techniques for large molecular and supramolecular structures.
Sorting pathways of mitochondrial inner membrane proteins.
Structure and function in GroEL-mediated protein folding.
Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL.
Synthesis of hepadnavirus particles that contain replication-defective duck hepatitis B virus genomes in cultured HuH7 cells.
TCP1 complex is a molecular chaperone in tubulin biogenesis.
thermosome: chaperonin with a built-in lid., The
Topologies of a substrate protein bound to the chaperonin GroEL.
Two families of chaperonin: physiology and mechanism.
Two related genes encoding extremely hydrophobic proteins suppress a lethal mutation in the yeast mitochondrial processing enhancing protein.
Uniform and residue-specific 15N-labeling of proteins on a highly deuterated background.
Unliganded GroEL at 2.8 A: structure and functional implications.
Weissman et al Mechanism of GroEL action: Productive release of poly- peptide from a sequestered position under GroES
Working with Paul Sigler
Contributed to or performed:
JOURNAL OF CLINICAL INVESTIGATION
NATURE STRUCTURAL BIOLOGY