James Shorter

Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115.

Sequential SNARE disassembly and GATE-16-GOS-28 complex assembly mediated by distinct NSF activities drives Golgi membrane fusion.

Golgi architecture and inheritance.

A direct role for GRASP65 as a mitotically regulated Golgi stacking factor.

Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers.

Navigating the ClpB channel to solution.

A cryptic Rab1-binding site in the p115 tethering protein.

Prions as adaptive conduits of memory and inheritance.

Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities.

Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity.

Prime time for alpha-synuclein.

Hsp104: a weapon to combat diverse neurodegenerative disorders.

Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104.

The Parkinson's disease protein alpha-synuclein disrupts cellular Rab homeostasis.

Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities.

Direct and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogs.

Escaping amyloid fate.

Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease.

A PDZ-binding motif controls basolateral targeting of syndecan-1 along the biosynthetic pathway in polarized epithelial cells.

Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.

The Mad2 partial unfolding model: regulating mitosis through Mad2 conformational switching.

Prion proteostasis: Hsp104 meets its supporting cast.

Motor mechanism for protein threading through Hsp104.

TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity.

N-terminal domains elicit formation of functional Pmel17 amyloid fibrils.

A synergistic small-molecule combination directly eradicates diverse prion strain structures.

Applying Hsp104 to protein-misfolding disorders.

Prion-like disorders: blurring the divide between transmissibility and infectivity.

Emergence and natural selection of drug-resistant prions.

Countering amyloid polymorphism and drug resistance with minimal drug cocktails.

Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS.

Shock and awe: unleashing the heat shock response to treat Huntington disease.

The elusive middle domain of Hsp104 and ClpB: Location and function.

RNA-binding proteins with prion-like domains in ALS and FTLD-U.

The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system.

A yeast functional screen predicts new candidate ALS disease genes.

The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease.

Evaluating the role of the FUS/TLS-related gene EWSR1 in amyotrophic lateral sclerosis.

Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans.

RNA-Binding Proteins in Amyotrophic Lateral Sclerosis and Neurodegeneration.

Inhibition of RNA lariat debranching enzyme suppresses TDP-43 toxicity in ALS disease models.

Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients.

Hsp104 drives "protein-only" positive selection of Sup35 prion strains encoding strong [PSI(+)].

Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS.

Stress granules as crucibles of ALS pathogenesis.

Fission yeast does not age under favorable conditions, but does so after stress.

Hsp104 suppresses polyglutamine-induced degeneration post onset in a drosophila MJD/SCA3 model.

Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation.

The metazoan protein disaggregase and amyloid depolymerase system: Hsp110, Hsp70, Hsp40, and small heat shock proteins.

Potentiated Hsp104 variants antagonize diverse proteotoxic misfolding events.

ALS-associated mutation FUS-R521C causes DNA damage and RNA splicing defects.

Reversing deleterious protein aggregation with re-engineered protein disaggregases.

The Surprising Role of Amyloid Fibrils in HIV Infection.

A cellular system that degrades misfolded proteins and protects against neurodegeneration.

Disease mutations in the prion-like domains of hnRNPA1 and hnRNPA2/B1 introduce potent steric zippers that drive excess RNP granule assembly.

Potentiated Hsp104 variants suppress toxicity of diverse neurodegenerative disease-linked proteins.

Specific aromatic foldamers potently inhibit spontaneous and seeded Aβ42 and Aβ43 fibril assembly.

Suramin inhibits hsp104 ATPase and disaggregase activity.

Counteracting Semen-mediated Enhancement of HIV Infection and Enveloped Virus Infection by a Lysine-specific Molecular Tweezer.