
Professor
M_IND (Neurodegenerative Dis)
+1 415 502-3775
Publications
Structures of Fab-stabilized CHIP reveal a conformational switch important in E3 ligase and chaperone functions.
bioRxiv : the preprint server for biology
Recombinant Antibodies Inhibit Enzymatic Activity of the E3 Ubiquitin Ligase CHIP via Multiple Mechanisms.
The Journal of biological chemistry
Design principles to tailor Hsp104 therapeutics.
Cell reports
Interactions with regulatory antibodies modulate CHIP E3 ubiquitin ligase-driven tau clearance.
Alzheimer's & Dementia
Cryo-EM structure of a novel a-synuclein filament subtype from multiple system atrophy.
FEBS letters
CRISPR screens in iPSC-derived neurons reveal principles of tau proteostasis.
bioRxiv : the preprint server for biology
Phosphorylation of tau at a single residue inhibits binding to the E3 ubiquitin ligase, CHIP.
Nature communications
Asymmetric apical domain states of mitochondrial Hsp60 coordinate substrate engagement and chaperonin assembly.
Nature structural & molecular biology
Cryo-EM structures reveal tau filaments from Down syndrome adopt Alzheimer's disease fold.
Acta neuropathologica communications
Cryo-EM Structures Reveal Tau Filaments from Down Syndrome Adopt Alzheimer's Disease Fold.
bioRxiv : the preprint server for biology
Amyloid Accelerator Polyphosphate Implicated as the Mystery Density in α-Synuclein Fibrils.
bioRxiv : the preprint server for biology
Design principles to tailor Hsp104 therapeutics.
bioRxiv : the preprint server for biology
Mapping interactions of calmodulin and neuronal NO synthase by crosslinking and mass spectrometry.
The Journal of biological chemistry
The p97/VCP adaptor UBXD1 drives AAA+ remodeling and ring opening through multi-domain tethered interactions.
Nature structural & molecular biology
Structural insights of the p97/VCP AAA+ ATPase: how adapter interactions coordinate diverse cellular functionality.
The Journal of biological chemistry
Phosphorylation of a Cleaved Tau Proteoform at a Single Residue Inhibits Binding to the E3 Ubiquitin Ligase, CHIP.
bioRxiv : the preprint server for biology
The E3 Ubiquitin Ligase, CHIP/STUB1, Inhibits Aggregation of Phosphorylated Proteoforms of Microtubule-associated Protein Tau (MAPT).
Journal of molecular biology
Stacked binding of a PET ligand to Alzheimer's tau paired helical filaments.
Nature communications
Asymmetric apical domain states of mitochondrial Hsp60 coordinate substrate engagement and chaperonin assembly.
bioRxiv : the preprint server for biology
The p97/VCP adapter UBXD1 drives AAA+ remodeling and ring opening through multi-domain tethered interactions.
bioRxiv : the preprint server for biology
Chemical Features of Polyanions Modulate Tau Aggregation and Conformational States.
Journal of the American Chemical Society
Unique structural features govern the activity of a human mitochondrial AAA+ disaggregase, Skd3.
Cell reports
Cryo-EM structures reveal dramatic remodeling of the p97 hexamer by the multi-domain adapter UBXD1.
Acta Crystallographica Section A: Foundations and advances
Structural and mechanistic studies of Skd3 (human CLPB) provide insight into disease-causing mutations and reveal unique AAA+ oligomerization.
Biophysical Journal
Structural basis for client engagement and chaperone cycling by human mitochondrial Hsp60.
Biophysical Journal
Structural basis for recognition of the Hsp90 closed, ATP state by the TPR-containing co-chaperone FKBP51.
Alzheimer's & Dementia
Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes.
Structure (London, England : 1993)
The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state.
Molecular cell
CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes.
Research square
CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes.
bioRxiv : the preprint server for biology
Practical considerations for using K3 cameras in CDS mode for high-resolution and high-throughput single particle cryo-EM.
Journal of structural biology
Conformational Plasticity of the Clpap Aaa+ Protease Couples Protein Unfolding and Proteolysis.
Biophysical Journal
Structural Basis for Recognition of the Hsp90 Closed, ATP State by the TPR-Containing Co-Chaperone FKBP51.
Biophysical Journal
Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms.
Science (New York, N.Y.)
Practical Considerations of Using the K3 Camera in CDS Mode for High-resolution and High-throughput Single Particle Cryo-EM.
Microscopy and Microanalysis
Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis.
Nature structural & molecular biology
Compromised function of the ESCRT pathway promotes endolysosomal escape of tau seeds and propagation of tau aggregation.
The Journal of biological chemistry
Mechanistic insights into the protective roles of polyphosphate against amyloid cytotoxicity.
Life science alliance
Mining Disaggregase Sequence Space to Safely Counter TDP-43, FUS, and a-Synuclein Proteotoxicity.
Cell reports
Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase.
Cold Spring Harbor perspectives in biology
Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase.
Nature communications
Allosteric Regulation of Oligomerization by a B12 Trafficking G-Protein Is Corrupted in Methylmalonic Aciduria.
Cell chemical biology
Chaperone activation and client binding of a 2-cysteine peroxiredoxin.
Nature communications
Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau.
Nature communications
Polyphosphate Stabilizes Protein Unfolding Intermediates as Soluble Amyloid-like Oligomers.
Journal of molecular biology
Chaperone Activity and Dimerization Properties of Hsp90a and Hsp90ß in Glucocorticoid Receptor Activation by the Multiprotein Hsp90/Hsp70-Dependent Chaperone Machinery.
Molecular pharmacology
The full-length cytochrome P450 enzyme CYP102A1 dimerizes at its reductase domains and has flexible heme domains for efficient catalysis.
The Journal of biological chemistry
X-linked inhibitor of apoptosis protein (XIAP) is a client of heat shock protein 70 (Hsp70) and a biomarker of its inhibition.
The Journal of biological chemistry
Switch I-dependent allosteric signaling in a G-protein chaperone-B12 enzyme complex.
The Journal of biological chemistry
Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104.
Science (New York, N.Y.)
Aggregation of Mod5 is affected by tRNA binding with implications for tRNA gene-mediated silencing.
FEBS letters
BAG3 Is a Modular, Scaffolding Protein that physically Links Heat Shock Protein 70 (Hsp70) to the Small Heat Shock Proteins.
Journal of molecular biology
Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation.
Nature structural & molecular biology
Architecture and Nucleotide-Dependent Conformational Changes of the Rvb1-Rvb2 AAA+ Complex Revealed by Cryoelectron Microscopy.
Structure (London, England : 1993)
Single-particle cryo-electron microscopy of macromolecular complexes.
Microscopy (Oxford, England)
Enhancement of dynamin polymerization and GTPase activity by Arc/Arg3.1.
Biochimica et biophysica acta
Mitochondrial peroxiredoxin functions as crucial chaperone reservoir in Leishmania infantum.
Proceedings of the National Academy of Sciences of the United States of America
The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions.
Molecular cell
Architecture of the nitric-oxide synthase holoenzyme reveals large conformational changes and a calmodulin-driven release of the FMN domain.
The Journal of biological chemistry
KRAS protein stability is regulated through SMURF2: UBCH5 complex-mediated ß-TrCP1 degradation.
Neoplasia (New York, N.Y.)
The molecular chaperone Hsp70 activates protein phosphatase 5 (PP5) by binding the tetratricopeptide repeat (TPR) domain.
The Journal of biological chemistry
The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex.
Biochemistry
The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis.
Protein science : a publication of the Protein Society
Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex.
Molecular cell
High-Q nanomechanics via destructive interference of elastic waves.
Physical review letters
Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide.
Protein science : a publication of the Protein Society
pH-dependent conformational changes in bacterial Hsp90 reveal a Grp94-like conformation at pH 6 that is highly active in suppression of citrate synthase aggregation.
Journal of molecular biology
Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle.
Molecular cell
Mutational analysis of S12 protein and implications for the accuracy of decoding by the ribosome.
Journal of molecular biology
EF-G-independent reactivity of a pre-translocation-state ribosome complex with the aminoacyl tRNA substrate puromycin supports an intermediate (hybrid) state of tRNA binding.
RNA (New York, N.Y.)
Demonstration of the role of the DnaK chaperone system in assembly of 30S ribosomal subunits using a purified in vitro system.
RNA (New York, N.Y.)
Ribosomal translocation: sparsomycin pushes the button.
Current biology : CB