Year |
Citation |
Score |
2024 |
Braxton JR, Shao H, Tse E, Gestwicki JE, Southworth DR. Asymmetric apical domain states of mitochondrial Hsp60 coordinate substrate engagement and chaperonin assembly. Nature Structural & Molecular Biology. PMID 38951622 DOI: 10.1038/s41594-024-01352-0 |
0.335 |
|
2023 |
Felker D, Lee K, Pospiech TH, Morishima Y, Zhang H, Lau M, Southworth D, Osawa Y. Mapping interactions of calmodulin and neuronal NO synthase by crosslinking and mass spectrometry. The Journal of Biological Chemistry. 105464. PMID 37979917 DOI: 10.1016/j.jbc.2023.105464 |
0.672 |
|
2023 |
Nadel CM, Thwin AC, Callahan M, Lee K, Connelly E, Craik CS, Southworth DR, Gestwicki JE. The E3 Ubiquitin Ligase, CHIP/STUB1, Inhibits Aggregation of Phosphorylated Proteoforms of Microtubule-associated Protein Tau (MAPT). Journal of Molecular Biology. 168026. PMID 37330289 DOI: 10.1016/j.jmb.2023.168026 |
0.668 |
|
2023 |
Braxton JR, Shao H, Tse E, Gestwicki JE, Southworth DR. Asymmetric apical domain states of mitochondrial Hsp60 coordinate substrate engagement and chaperonin assembly. Biorxiv : the Preprint Server For Biology. PMID 37293102 DOI: 10.1101/2023.05.15.540872 |
0.345 |
|
2022 |
Cupo RR, Rizo AN, Braun GA, Tse E, Chuang E, Gupta K, Southworth DR, Shorter J. Unique structural features govern the activity of a human mitochondrial AAA+ disaggregase, Skd3. Cell Reports. 40: 111408. PMID 36170828 DOI: 10.1016/j.celrep.2022.111408 |
0.37 |
|
2021 |
Seraphim TV, Nano N, Cheung YWS, Aluksanasuwan S, Colleti C, Mao YQ, Bhandari V, Young G, Höll L, Phanse S, Gordiyenko Y, Southworth DR, Robinson CV, Thongboonkerd V, Gava LM, et al. Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes. Structure (London, England : 1993). PMID 34492227 DOI: 10.1016/j.str.2021.08.002 |
0.321 |
|
2021 |
Lee K, Thwin AC, Nadel CM, Tse E, Gates SN, Gestwicki JE, Southworth DR. The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state. Molecular Cell. PMID 34380015 DOI: 10.1016/j.molcel.2021.07.023 |
0.724 |
|
2021 |
Verba K, Gupta M, Azumaya C, Moritz M, Pourmal S, Diallo A, Merz G, Jang G, Bouhaddou M, Fossati A, Brilot A, Diwanji D, Hernandez E, Herrera N, Kratochvil H, ... ... Southworth D, et al. CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes. Research Square. PMID 34031651 DOI: 10.21203/rs.3.rs-515215/v1 |
0.343 |
|
2021 |
Gupta M, Azumaya CM, Moritz M, Pourmal S, Diallo A, Merz GE, Jang G, Bouhaddou M, Fossati A, Brilot AF, Diwanji D, Hernandez E, Herrera N, Kratochvil HT, Lam VL, ... ... Southworth DR, et al. 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. PMID 34013269 DOI: 10.1101/2021.05.10.443524 |
0.343 |
|
2020 |
Lopez KE, Rizo AN, Tse E, Lin J, Scull NW, Thwin AC, Lucius AL, Shorter J, Southworth DR. Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis. Nature Structural & Molecular Biology. PMID 32313240 DOI: 10.1038/S41594-020-0409-5 |
0.419 |
|
2019 |
Chen JJ, Nathaniel DL, Raghavan P, Nelson M, Tian R, Tse E, Hong JY, See SK, Mok SA, Hein MY, Southworth DR, Grinberg LT, Gestwicki JE, Leonetti MD, Kampmann M. Compromised function of the ESCRT pathway promotes endolysosomal escape of tau seeds and propagation of tau aggregation. The Journal of Biological Chemistry. PMID 31578281 DOI: 10.1074/Jbc.Ra119.009432 |
0.327 |
|
2019 |
Tariq A, Lin J, Jackrel ME, Hesketh CD, Carman PJ, Mack KL, Weitzman R, Gambogi C, Hernandez Murillo OA, Sweeny EA, Gurpinar E, Yokom AL, Gates SN, Yee K, Sudesh S, ... ... Southworth DR, et al. Mining Disaggregase Sequence Space to Safely Counter TDP-43, FUS, and α-Synuclein Proteotoxicity. Cell Reports. 28: 2080-2095.e6. PMID 31433984 DOI: 10.1016/J.Celrep.2019.07.069 |
0.394 |
|
2019 |
Rizo AN, Lin J, Gates SN, Tse E, Bart SM, Castellano LM, DiMaio F, Shorter J, Southworth DR. Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase. Nature Communications. 10: 2393. PMID 31160557 DOI: 10.1038/S41467-019-10150-Y |
0.456 |
|
2019 |
Ruetz M, Campanello GC, McDevitt L, Yokom AL, Yadav PK, Watkins D, Rosenblatt DS, Ohi MD, Southworth DR, Banerjee R. Allosteric Regulation of Oligomerization by a B Trafficking G-Protein Is Corrupted in Methylmalonic Aciduria. Cell Chemical Biology. PMID 31056463 DOI: 10.1016/J.Chembiol.2019.03.014 |
0.372 |
|
2019 |
Shorter J, Southworth DR. Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase. Cold Spring Harbor Perspectives in Biology. PMID 30745294 DOI: 10.1101/Cshperspect.A034033 |
0.405 |
|
2019 |
Teixeira F, Tse E, Castro H, Makepeace KAT, Meinen BA, Borchers CH, Poole LB, Bardwell JC, Tomás AM, Southworth DR, Jakob U. Chaperone activation and client binding of a 2-cysteine peroxiredoxin. Nature Communications. 10: 659. PMID 30737390 DOI: 10.2210/Pdb6E0G/Pdb |
0.466 |
|
2018 |
Freilich R, Betegon M, Tse E, Mok SA, Julien O, Agard DA, Southworth DR, Takeuchi K, Gestwicki JE. Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau. Nature Communications. 9: 4563. PMID 30385828 DOI: 10.1038/S41467-018-07012-4 |
0.431 |
|
2018 |
Yoo N, Dogra S, Meinen BA, Tse E, Haefliger J, Southworth DR, Gray MJ, Dahl JU, Jakob U. Polyphosphate Stabilizes Protein Unfolding Intermediates as Soluble Amyloid-like Oligomers. Journal of Molecular Biology. PMID 30130556 DOI: 10.1016/J.Jmb.2018.08.016 |
0.387 |
|
2018 |
Morishima Y, Mehta RK, Yoshimura M, Lau M, Southworth DR, Lawrence TS, Pratt WB, Nyati MK, Osawa Y. Chaperone Activity and Dimerization Properties of Hsp90α and Hsp90β in Glucocorticoid Receptor Activation by the Multiprotein Hsp90/Hsp70-Dependent Chaperone Machinery. Molecular Pharmacology. PMID 29941666 DOI: 10.1124/Mol.118.112516 |
0.396 |
|
2018 |
Zhang H, Yokom AL, Cheng S, Su M, Hollenberg PF, Southworth DR, Osawa Y. 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. PMID 29618513 DOI: 10.1074/Jbc.Ra117.000600 |
0.38 |
|
2017 |
Cesa LC, Shao H, Srinivasan SR, Tse E, Jain C, Zuiderweg ERP, Southworth DR, Mapp AK, Gestwicki JE. 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. PMID 29255093 DOI: 10.1074/Jbc.Ra117.000634 |
0.374 |
|
2017 |
Campanello GC, Lofgren M, Yokom AL, Southworth DR, Banerjee R. Switch I-Dependent Allosteric Signaling In A G-Protein Chaperone-B12 Enzyme Complex. The Journal of Biological Chemistry. PMID 28882898 DOI: 10.1074/Jbc.M117.786095 |
0.452 |
|
2017 |
Gates SN, Yokom AL, Lin J, Jackrel ME, Rizo AN, Kendsersky NM, Buell CE, Sweeny EA, Mack KL, Chuang E, Torrente MP, Su M, Shorter J, Southworth DR. Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104. Science (New York, N.Y.). PMID 28619716 DOI: 10.1126/Science.Aan1052 |
0.446 |
|
2017 |
Read DF, Waller TJ, Tse E, Southworth DR, Engelke DR, Smaldino PJ. Aggregation of Mod5 is affected by tRNA binding with implications for tRNA gene-mediated silencing. Febs Letters. PMID 28303570 DOI: 10.1002/1873-3468.12627 |
0.401 |
|
2016 |
Rauch JN, Tse E, Freilich R, Mok SA, Makley LN, Southworth DR, Gestwicki JE. BAG3 is a modular, scaffolding protein that physically links heat shock protein 70 (Hsp70) to the small heat shock proteins. Journal of Molecular Biology. PMID 27884606 DOI: 10.1016/J.Jmb.2016.11.013 |
0.404 |
|
2016 |
Cremers CM, Knoefler D, Gates S, Martin N, Dahl JU, Lempart J, Xie L, Chapman MR, Galvan V, Southworth DR, Jakob U. Polyphosphate: A Conserved Modifier of Amyloidogenic Processes. Molecular Cell. PMID 27570072 DOI: 10.1016/J.Molcel.2016.07.016 |
0.308 |
|
2016 |
Yokom AL, Gates SN, Jackrel ME, Mack KL, Su M, Shorter J, Southworth DR. Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation. Nature Structural & Molecular Biology. PMID 27478928 DOI: 10.1038/Nsmb.3277 |
0.461 |
|
2016 |
Ewens CA, Su M, Zhao L, Nano N, Houry WA, Southworth DR. Architecture and Nucleotide-Dependent Conformational Changes of the Rvb1-Rvb2 AAA+ Complex Revealed by Cryoelectron Microscopy. Structure (London, England : 1993). PMID 27112599 DOI: 10.1016/J.Str.2016.03.018 |
0.434 |
|
2015 |
Assimon VA, Southworth DR, Gestwicki JE. Specific binding of tetratricopeptide repeat (TPR) proteins to heat shock protein 70 (Hsp70) and heat shock protein 90 (Hsp90) is regulated by affinity and phosphorylation. Biochemistry. PMID 26565746 DOI: 10.1021/Acs.Biochem.5B00801 |
0.456 |
|
2015 |
Rajagopal P, Tse E, Borst AJ, Delbecq SP, Shi L, Southworth DR, Klevit RE. A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis. Elife. 4. PMID 25962097 DOI: 10.7554/Elife.07304 |
0.391 |
|
2015 |
Teixeira F, Castro H, Cruz T, Tse E, Koldewey P, Southworth DR, Tomás AM, Jakob U. Mitochondrial peroxiredoxin functions as crucial chaperone reservoir in Leishmania infantum. Proceedings of the National Academy of Sciences of the United States of America. 112: E616-24. PMID 25646478 DOI: 10.1073/Pnas.1419682112 |
0.445 |
|
2014 |
Voth W, Schick M, Gates S, Li S, Vilardi F, Gostimskaya I, Southworth DR, Schwappach B, Jakob U. The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions. Molecular Cell. 56: 116-27. PMID 25242142 DOI: 10.1016/J.Molcel.2014.08.017 |
0.406 |
|
2014 |
Kirschke E, Goswami D, Southworth D, Griffin PR, Agard DA. Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles. Cell. 157: 1685-97. PMID 24949977 DOI: 10.1016/J.Cell.2014.04.038 |
0.399 |
|
2014 |
Yokom AL, Morishima Y, Lau M, Su M, Glukhova A, Osawa Y, Southworth DR. 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. 289: 16855-65. PMID 24737326 DOI: 10.1074/Jbc.M114.564005 |
0.377 |
|
2014 |
Shukla S, Allam US, Ahsan A, Chen G, Krishnamurthy PM, Marsh K, Rumschlag M, Shankar S, Whitehead C, Schipper M, Basrur V, Southworth DR, Chinnaiyan AM, Rehemtulla A, Beer DG, et al. KRAS protein stability is regulated through SMURF2: UBCH5 complex-mediated β-TrCP1 degradation. Neoplasia (New York, N.Y.). 16: 115-28. PMID 24709419 DOI: 10.1593/Neo.14184 |
0.383 |
|
2014 |
Connarn JN, Assimon VA, Reed RA, Tse E, Southworth DR, Zuiderweg ER, Gestwicki JE, Sun D. The molecular chaperone Hsp70 activates protein phosphatase 5 (PP5) by binding the tetratricopeptide repeat (TPR) domain. The Journal of Biological Chemistry. 289: 2908-17. PMID 24327656 DOI: 10.1074/Jbc.M113.519421 |
0.46 |
|
2013 |
Smith MC, Scaglione KM, Assimon VA, Patury S, Thompson AD, Dickey CA, Southworth DR, Paulson HL, Gestwicki JE, Zuiderweg ER. The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex. Biochemistry. 52: 5354-64. PMID 23865999 DOI: 10.1021/Bi4009209 |
0.422 |
|
2012 |
Cunningham CN, Southworth DR, Krukenberg KA, Agard DA. 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. 21: 1162-71. PMID 22653663 DOI: 10.1002/Pro.2103 |
0.486 |
|
2011 |
Southworth DR, Agard DA. Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex. Molecular Cell. 42: 771-81. PMID 21700222 DOI: 10.1016/J.Molcel.2011.04.023 |
0.469 |
|
2009 |
Krukenberg KA, Böttcher UM, Southworth DR, Agard DA. 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. 18: 1815-27. PMID 19554567 DOI: 10.1002/Pro.191 |
0.438 |
|
2009 |
Krukenberg KA, Southworth DR, Street TO, Agard DA. 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. 390: 278-91. PMID 19427321 DOI: 10.1016/J.Jmb.2009.04.080 |
0.378 |
|
2008 |
Southworth DR, Agard DA. Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle. Molecular Cell. 32: 631-40. PMID 19061638 DOI: 10.1016/J.Molcel.2008.10.024 |
0.426 |
|
2007 |
Sharma D, Cukras AR, Rogers EJ, Southworth DR, Green R. Mutational analysis of S12 protein and implications for the accuracy of decoding by the ribosome. Journal of Molecular Biology. 374: 1065-76. PMID 17967466 DOI: 10.1016/J.Jmb.2007.10.003 |
0.687 |
|
2006 |
Shiau AK, Harris SF, Southworth DR, Agard DA. Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell. 127: 329-40. PMID 17055434 DOI: 10.1016/J.Cell.2006.09.027 |
0.456 |
|
2004 |
Sharma D, Southworth DR, Green R. 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.). 10: 102-13. PMID 14681589 DOI: 10.1261/Rna.5148704 |
0.628 |
|
2003 |
Maki JA, Southworth DR, Culver GM. 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.). 9: 1418-21. PMID 14623997 DOI: 10.1261/Rna.5139703 |
0.357 |
|
2003 |
Cukras AR, Southworth DR, Brunelle JL, Culver GM, Green R. Ribosomal proteins S12 and S13 function as control elements for translocation of the mRNA:tRNA complex. Molecular Cell. 12: 321-8. PMID 14536072 DOI: 10.1016/S1097-2765(03)00275-2 |
0.701 |
|
2003 |
Southworth DR, Green R. Ribosomal translocation: sparsomycin pushes the button. Current Biology : Cb. 13: R652-4. PMID 12932345 DOI: 10.1016/S0960-9822(03)00574-8 |
0.558 |
|
2002 |
Southworth DR, Brunelle JL, Green R. EFG-independent translocation of the mRNA:tRNA complex is promoted by modification of the ribosome with thiol-specific reagents. Journal of Molecular Biology. 324: 611-23. PMID 12460565 DOI: 10.1016/S0022-2836(02)01196-8 |
0.582 |
|
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