D. Southworth

发表

Structural Analysis of E. coli hsp90 Reveals Dramatic Nucleotide-Dependent Conformational Rearrangements

David A. Agard, Andrew K. Shiau, D. Agard, 2006, Cell.

Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle.

David A Agard, Daniel R Southworth, D. Agard, 2008, Molecular cell.

Bi-paratopic and multivalent VH domains block ACE2 binding and neutralize SARS-CoV-2

N. Krogan, D. Agard, R. Stroud, 2020, Nature Chemical Biology.

Chaperone activation and client binding of a 2-cysteine peroxiredoxin

Ben A Meinen, C. Borchers, U. Jakob, 2019, Nature Communications.

Chaperone activation and client binding of a 2-cysteine peroxiredoxin

Ben A Meinen, C. Borchers, U. Jakob, 2019, Nature Communications.

Mitochondrial peroxiredoxin functions as crucial chaperone reservoir in Leishmania infantum

U. Jakob, A. Tomás, D. Southworth, 2015, Proceedings of the National Academy of Sciences.

Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis

J. Shorter, A. Thwin, D. Southworth, 2020, Nature Structural & Molecular Biology.

Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis

J. Shorter, A. Thwin, D. Southworth, 2019, Nature Structural & Molecular Biology.

BAG3 Is a Modular, Scaffolding Protein that physically Links Heat Shock Protein 70 (Hsp70) to the Small Heat Shock Proteins.

J. Gestwicki, L. Makley, D. Southworth, 2017, Journal of molecular biology.

Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms

Miguel Correa Marrero, Robyn M. Kaake, Gwendolyn M. Jang, 2020, Science.

Compromised function of the ESCRT pathway promotes endolysosomal escape of tau seeds and propagation of tau aggregation

Marco Y. Hein, L. Grinberg, M. Leonetti, 2019, The Journal of Biological Chemistry.

The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis

Christian N. Cunningham, D. Agard, K. Krukenberg, 2012, Protein science : a publication of the Protein Society.

Chaperone Activity and Dimerization Properties of Hsp90α and Hsp90β in Glucocorticoid Receptor Activation by the Multiprotein Hsp90/Hsp70-Dependent Chaperone Machinery

T. Lawrence, W. Pratt, M. Nyati, 2018, Molecular Pharmacology.

X-linked inhibitor of apoptosis protein (XIAP) is a client of heat shock protein 70 (Hsp70) and a biomarker of its inhibition

E. Zuiderweg, A. Mapp, J. Gestwicki, 2017, The Journal of Biological Chemistry.

Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide

D. Agard, Ulrike M K Böttcher, K. Krukenberg, 2009, Protein science : a publication of the Protein Society.

Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation.

J. Gestwicki, Victoria A. Assimon, D. Southworth, 2015, Biochemistry.

Polyphosphate: A Conserved Modifier of Amyloidogenic Processes.

M. Chapman, U. Jakob, D. Southworth, 2016, Molecular cell.

Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104

J. Shorter, Meredith E. Jackrel, E. Chuang, 2017, Science.

Mining Disaggregase Sequence Space to Safely Counter TDP-43, FUS, and α-Synuclein Proteotoxicity

J. Shorter, Meredith E. Jackrel, D. Southworth, 2019, Cell reports.

Mining Disaggregase Sequ ence Space to Safely Counter TDP-43 , FUS , and a-Synuclein Proteotoxicity Graphical

J. Shorter, Meredith E. Jackrel, D. Southworth, 2019 .

Architecture and Nucleotide-Dependent Conformational Changes of the Rvb1-Rvb2 AAA+ Complex Revealed by Cryoelectron Microscopy.

W. Houry, Min Su, D. Southworth, 2016, Structure.

PIKfyve inhibition blocks endolysosomal escape of α-synuclein fibrils and spread of α-synuclein aggregation

M. Leonetti, Stephanie K. See, J. Gestwicki, 2021, bioRxiv.

The Molecular Chaperone Hsp70 Activates Protein Phosphatase 5 (PP5) by Binding the Tetratricopeptide Repeat (TPR) Domain*

E. Zuiderweg, J. Gestwicki, Duxin Sun, 2013, The Journal of Biological Chemistry.

Structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client-maturation state

A. Thwin, D. Southworth, E. Tse, 2021, bioRxiv.

Mutational analysis of S12 protein and implications for the accuracy of decoding by the ribosome.

R. Green, D. Southworth, D. Sharma, 2007, Journal of molecular biology.

Cisplatin Induces Bmi1 and Enhances the Stem Cell Fraction in Head and Neck Cancer

A. Chinnaiyan, D. Beer, Guoan Chen, 2015 .

Chemical Features of Polyanions Modulate Tau Aggregation and Conformational States

J. Gestwicki, A. Thwin, D. Southworth, 2022, bioRxiv.

Allosteric Regulation of Oligomerization by a B12 Trafficking G-Protein Is Corrupted in Methylmalonic Aciduria.

R. Banerjee, G. Campanello, M. Ohi, 2019, Cell chemical biology.

Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes.

S. Phanse, M. Babu, W. Houry, 2021, Structure.

The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex.

H. Paulson, E. Zuiderweg, J. Gestwicki, 2013, Biochemistry.

Polyphosphate Stabilizes Protein Unfolding Intermediates as Soluble Amyloid-like Oligomers.

Ben A Meinen, U. Jakob, M. Gray, 2018, Journal of molecular biology.

KRAS protein stability is regulated through SMURF2: UBCH5 complex-mediated β-TrCP1 degradation.

A. Chinnaiyan, D. Beer, Guoan Chen, 2014, Neoplasia.

Glucocorticoid Receptor Function Regulated by Coordinated Action of the Hsp90 and Hsp70 Chaperone Cycles

D. Agard, P. Griffin, Devrishi Goswami, 2014, Cell.

The full-length cytochrome P450 enzyme CYP102A1 dimerizes at its reductase domains and has flexible heme domains for efficient catalysis

Min Su, P. Hollenberg, D. Southworth, 2018, The Journal of Biological Chemistry.

Single-particle cryo-electron microscopy of macromolecular complexes.

Georgios Skiniotis, Daniel R Southworth, G. Skiniotis, 2016, Microscopy.

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.

R. Green, D. Southworth, D. Sharma, 2004, RNA.

EFG-independent translocation of the mRNA:tRNA complex is promoted by modification of the ribosome with thiol-specific reagents.

R. Green, D. Southworth, J. Brunelle, 2002, Journal of molecular biology.

CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes.

Gwendolyn M. Jang, N. Krogan, D. Agard, 2021, bioRxiv.

Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase

J. Shorter, L. Castellano, D. Southworth, 2018, bioRxiv.

Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex.

D. Agard, D. Southworth, 2011, Molecular cell.

Practical considerations for using K3 cameras in CDS mode for high-resolution and high-throughput single particle cryo-EM.

D. Agard, Yifan Cheng, K. Verba, 2021, Journal of structural biology.

Mechanistic insights into the protective roles of polyphosphate against amyloid cytotoxicity

M. Ivanova, U. Jakob, D. Southworth, 2019, Life Science Alliance.

The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions.

B. Schwappach, Sheng Li, U. Jakob, 2014, Molecular cell.

Supplemental Information The Protein Targeting Factor Get 3 Functions as ATP-Independent Chaperone under Oxidative Stress Conditions

B. Schwappach, U. Jakob, I. Gostimskaya, 2014 .

Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation

J. Shorter, Meredith E. Jackrel, Min Su, 2016, Nature Structural &Molecular Biology.

Ribosomal proteins S12 and S13 function as control elements for translocation of the mRNA:tRNA complex.

Daniel R Southworth, Rachel Green, Julie L Brunelle, 2003, Molecular cell.

CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes.

Gwendolyn M. Jang, N. Krogan, D. Agard, 2021, Research square.

Compromised function of the ESCRT pathway promotes endolysosomal escape of tau seeds and propagation of tau aggregation

Marco Y. Hein, L. Grinberg, M. Leonetti, 2019, The Journal of Biological Chemistry.

Aggregation of Mod5 is affected by tRNA binding with implications for tRNA gene‐mediated silencing

D. Engelke, D. F. Read, D. Southworth, 2017, FEBS letters.

Switch I-dependent allosteric signaling in a G-protein chaperone–B12 enzyme complex

R. Banerjee, G. Campanello, D. Southworth, 2017, The Journal of Biological Chemistry.

Ribosomal translocation: sparsomycin pushes the button

Rachel Green, R. Green, D. Southworth, 2003, Current Biology.

Unique structural features govern the activity of a human mitochondrial AAA+ disaggregase, Skd3

J. Shorter, E. Chuang, D. Southworth, 2022, bioRxiv.

Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase.

J. Shorter, D. Southworth, 2019, Cold Spring Harbor perspectives in biology.

Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau

D. Agard, Miguel Betegon, J. Gestwicki, 2018, Nature Communications.

Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau

D. Agard, Miguel Betegon, J. Gestwicki, 2018, Nature Communications.

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.

D. Agard, K. Krukenberg, Timothy O. Street, 2009, Journal of molecular biology.

Chaperone activation and client binding of a 2-cysteine peroxiredoxin

Ben A Meinen, C. Borchers, U. Jakob, 2019, Nature Communications.

Enhancement of dynamin polymerization and GTPase activity by Arc/Arg3.1.

J. Albanesi, D. Jameson, J. A. Ross, 2015, Biochimica et biophysica acta.

A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis

R. Klevit, D. Southworth, E. Tse, 2015, eLife.

Demonstration of the role of the DnaK chaperone system in assembly of 30S ribosomal subunits using a purified in vitro system.

G. Culver, D. Southworth, J. Maki, 2003, RNA.

Stacked binding of a PET ligand to Alzheimer’s tau paired helical filaments

Nick A. Paras, S. Prusiner, W. DeGrado, 2023, Nature communications.

Stacked binding of a small molecule PET tracer to Alzheimer’s tau paired helical filaments

Nick A. Paras, S. Prusiner, W. DeGrado, 2022, bioRxiv.

The p97/VCP adapter UBXD1 drives AAA+ remodeling and ring opening through multi-domain tethered interactions

M. Arkin, A. Thwin, D. Southworth, 2023, bioRxiv.

The E3 Ubiquitin Ligase, CHIP/STUB1, Inhibits Aggregation of Phosphorylated Proteoforms of Microtubule-associated Protein Tau (MAPT).

C. Craik, J. Gestwicki, Cory M. Nadel, 2023, Journal of molecular biology.

Practical considerations for using K3 cameras in CDS mode for high-resolution and high-throughput single particle cryo-EM

D. Agard, Yifan Cheng, K. Verba, 2020, bioRxiv.

Asymmetric apical domain states of mitochondrial Hsp60 coordinate substrate engagement and chaperonin assembly

J. Gestwicki, D. Southworth, Julian R. Braxton, 2023, bioRxiv.

Architecture of the Nitric-oxide Synthase Holoenzyme Reveals Large Conformational Changes and a Calmodulin-driven Release of the FMN Domain*♦

Min Su, Alisa Glukhova, Min Su, 2014, The Journal of Biological Chemistry.

Phosphorylation of a Cleaved Tau Proteoform at a Single Residue Inhibits Binding to the E3 Ubiquitin Ligase, CHIP

C. Craik, J. Gestwicki, Daniel A. Mordes, 2023, bioRxiv.

Mitochondrial peroxiredoxin from Leishmania infantum after heat stress without unfolding client protein

Ben A Meinen, C. Borchers, U. Jakob, 2019 .

Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase

J. Shorter, L. Castellano, D. Southworth, 2018, Nature Communications.

CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes.

Gwendolyn M. Jang, N. Krogan, D. Agard, 2021, bioRxiv.

interactomics of SARS-CoV-2

Gwendolyn M. Jang, R. Stroud, T. Kortemme, 2023 .

interactomics of SARS-CoV-2

Yang, Jen, N. Krogan, 2021 .

Chaperone Activity and Dimerization Properties of Hsp90α and Hsp90β in Glucocorticoid Receptor Activation by the Multiprotein Hsp90/Hsp70-Dependent Chaperone Machinery

T. Lawrence, W. Pratt, M. Nyati, 2018, Molecular Pharmacology.

Architecture of the Nitric-oxide Synthase Holoenzyme Reveals Large Conformational Changes and a Calmodulin-

D. Southworth, A. Yokom, Yoshihiro Morishima, 2014 .

Structural insights of the p97/VCP AAA+ ATPase: How adapter interactions coordinate diverse cellular functionality

D. Southworth, Julian R. Braxton, 2023, The Journal of biological chemistry.

Single-particle cryo-electron microscopy of macromolecular complexes.

G. Skiniotis, D. Southworth, 2016, Microscopy.

Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle.

D. Agard, D. Southworth, 2008, Molecular cell.

The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis

D. Agard, K. Krukenberg, D. Southworth, 2012, Protein science : a publication of the Protein Society.

The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state.

J. Gestwicki, A. Thwin, D. Southworth, 2021, Molecular cell.

Asymmetric apical domain states of mitochondrial Hsp60 coordinate substrate engagement and chaperonin assembly.

D. Southworth, Julian R. Braxton, E. Tse, 2024, Nature structural & molecular biology.

The p97/VCP adaptor UBXD1 drives AAA+ remodeling and ring opening through multi-domain tethered interactions

M. Arkin, A. Thwin, D. Southworth, 2023, Nature structural & molecular biology.

Cryo-EM structures reveal tau filaments from Down syndrome adopt Alzheimer’s disease fold

S. Prusiner, G. Merz, Carlo Condello, 2024, bioRxiv.