Arthur L. Horwich

ClpS, a substrate modulator of the ClpAP machine.

NMR analysis of a 900K GroEL GroES complex.

Solution NMR techniques for large molecular and supramolecular structures.

Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes.

Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics.

Chaperonin-mediated protein folding: fate of substrate polypeptide.

Uniform and residue-specific 15N-labeling of proteins on a highly deuterated background.

Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states.

A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation.

Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL.

Chaperoned protein disaggregation--the ClpB ring uses its central channel.

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.

Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation.

Direct NMR observation of a substrate protein bound to the chaperonin GroEL.

Roles of the N-domains of the ClpA unfoldase in binding substrate proteins and in stable complex formation with the ClpP protease.

Probing the sequence of conformationally induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopy.

Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes.

GroEL-GroES-mediated protein folding.

Proton-proton Overhauser NMR spectroscopy with polypeptide chains in large structures.

Global aggregation of newly translated proteins in an Escherichia coli strain deficient 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.

Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL.

Two families of chaperonin: physiology and mechanism.

Topologies of a substrate protein bound to the chaperonin GroEL.

Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution.

Multiple states of a nucleotide-bound group 2 chaperonin.

Chaperonin chamber accelerates protein folding through passive action of preventing aggregation.

Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active state.

A small molecule inhibitor selective for a variant ATP-binding site of the chaperonin GroEL.

An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans.

Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS.

The GroEL/GroES cis cavity as a passive anti-aggregation device.

Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding.

GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state.

ATP-triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP7 is not the rate-limiting step of the GroEL/GroES reaction cycle.

Double mutant MBP refolds at same rate in free solution as inside the GroEL/GroES chaperonin chamber when aggregation in free solution is prevented.

Nuclear magnetic resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL.

Hydrogen-deuterium exchange in vivo to measure turnover of an ALS-associated mutant SOD1 protein in spinal cord of mice.

Localization of GroEL determined by in vivo incorporation of a fluorescent amino acid.

Translational diffusion of macromolecular assemblies measured using transverse-relaxation-optimized pulsed field gradient NMR.

Protein folding in the cell: an inside story.

QnAs with Arthur L. Horwich. Interview by Prashant Nair.

ATP-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL chaperonin.

Structure and allostery of the chaperonin GroEL.

RNA-Seq profiling of spinal cord motor neurons from a presymptomatic SOD1 ALS mouse.

Recessive loss of function of the neuronal ubiquitin hydrolase UCHL1 leads to early-onset progressive neurodegeneration.

Molecular chaperone Hsp110 rescues a vesicle transport defect produced by an ALS-associated mutant SOD1 protein in squid axoplasm.

Chaperonin-mediated protein folding.