Wayne A. Fenton

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

Chaperonin-mediated protein folding: fate of substrate polypeptide.

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

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.

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

GroEL-GroES-mediated protein folding.

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.

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

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

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.

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

Structure and allostery of the chaperonin GroEL.

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

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