Year |
Citation |
Score |
2015 |
Genest O, Hoskins JR, Kravats AN, Doyle SM, Wickner S. Hsp70 and Hsp90 of E. coli Directly Interact for Collaboration in Protein Remodeling. Journal of Molecular Biology. PMID 26482100 DOI: 10.1016/j.jmb.2015.10.010 |
0.64 |
|
2015 |
Doyle SM, Shastry S, Kravats AN, Shih YH, Miot M, Hoskins JR, Stan G, Wickner S. Interplay between E. coli DnaK, ClpB and GrpE during protein disaggregation Journal of Molecular Biology. 427: 312-327. DOI: 10.1016/j.jmb.2014.10.013 |
0.64 |
|
2013 |
Doyle SM, Genest O, Wickner S. Protein rescue from aggregates by powerful molecular chaperone machines Nature Reviews Molecular Cell Biology. 14: 617-629. PMID 24061228 DOI: 10.1038/nrm3660 |
0.64 |
|
2012 |
Zhang T, Ploetz EA, Nagy M, Doyle SM, Wickner S, Smith PE, Zolkiewski M. Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency Proteins: Structure, Function and Bioinformatics. 80: 2758-2768. PMID 22890624 DOI: 10.1002/prot.24159 |
0.64 |
|
2012 |
Doyle SM, Hoskins JR, Wickner S. DnaK chaperone-dependent disaggregation by caseinolytic peptidase B (ClpB) mutants reveals functional overlap in the N-terminal domain and nucleotide-binding domain-1 pore tyrosine Journal of Biological Chemistry. 287: 28470-28479. PMID 22745126 DOI: 10.1074/jbc.M112.383091 |
0.64 |
|
2011 |
Evans ML, Schmidt JC, Ilbert M, Doyle SM, Quan S, Bardwell JC, Jakob U, Wickner S, Chapman MR. E. coli chaperones DnaK, Hsp33 and Spy inhibit bacterial functional amyloid assembly. Prion. 5: 323-34. PMID 22156728 DOI: 10.4161/pri.18555 |
0.64 |
|
2011 |
Genest O, Hoskins JR, Camberg JL, Doyle SM, Wickner S. Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling Proceedings of the National Academy of Sciences of the United States of America. 108: 8206-8211. PMID 21525416 DOI: 10.1073/pnas.1104703108 |
0.64 |
|
2011 |
Miot M, Reidy M, Doyle SM, Hoskins JR, Johnston DM, Genest O, Vitery MC, Masison DC, Wickner S. Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation Proceedings of the National Academy of Sciences of the United States of America. 108: 6915-6920. PMID 21474779 DOI: 10.1073/pnas.1102828108 |
0.64 |
|
2009 |
Hoskins JR, Doyle SM, Wickner S. Coupling ATP utilization to protein remodeling by ClpB, a hexameric AAA+ protein Proceedings of the National Academy of Sciences of the United States of America. 106: 22233-22238. PMID 19940245 DOI: 10.1073/pnas.0911937106 |
0.64 |
|
2009 |
Doyle SM, Wickner S. Hsp104 and ClpB: protein disaggregating machines Trends in Biochemical Sciences. 34: 40-48. PMID 19008106 DOI: 10.1016/j.tibs.2008.09.010 |
0.64 |
|
2007 |
Doyle SM, Hoskins JR, Wickner S. Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system Proceedings of the National Academy of Sciences of the United States of America. 104: 11138-11144. PMID 17545305 DOI: 10.1073/pnas.0703980104 |
0.64 |
|
2007 |
Doyle SM, Shorter J, Zolkiewski M, Hoskins JR, Lindquist S, Wickner S. Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity Nature Structural and Molecular Biology. 14: 114-122. PMID 17259993 DOI: 10.1038/nsmb1198 |
0.64 |
|
2005 |
Parent KN, Doyle SM, Anderson E, Teschke CM. Electrostatic interactions govern both nucleation and elongation during phage P22 procapsid assembly. Virology. 340: 33-45. PMID 16045955 DOI: 10.1016/j.virol.2005.06.018 |
0.64 |
|
2004 |
Doyle SM, Bilsel O, Teschke CM. SecA folding kinetics: a large dimeric protein rapidly forms multiple native states. Journal of Molecular Biology. 341: 199-214. PMID 15312773 DOI: 10.1016/j.jmb.2004.06.021 |
0.64 |
|
2004 |
Doyle SM, Anderson E, Parent KN, Teschke CM. A concerted mechanism for the suppression of a folding defect through interactions with chaperones. The Journal of Biological Chemistry. 279: 17473-82. PMID 14764588 DOI: 10.1074/jbc.M400467200 |
0.64 |
|
2003 |
Doyle SM, Anderson E, Zhu D, Braswell EH, Teschke CM. Rapid unfolding of a domain populates an aggregation-prone intermediate that can be recognized by GroEL. Journal of Molecular Biology. 332: 937-51. PMID 12972263 DOI: 10.1016/S0022-2836(03)00955-0 |
0.64 |
|
2000 |
de Beus MD, Doyle SM, Teschke CM. GroEL binds a late folding intermediate of phage P22 coat protein. Cell Stress & Chaperones. 5: 163-72. PMID 11005374 |
0.64 |
|
2000 |
Doyle SM, Braswell EH, Teschke CM. SecA folds via a dimeric intermediate. Biochemistry. 39: 11667-76. PMID 10995234 DOI: 10.1021/bi000299y |
0.64 |
|
1997 |
Fong DG, Doyle SM, Teschke CM. The folded conformation of phage P22 coat protein is affected by amino acid substitutions that lead to a cold-sensitive phenotype. Biochemistry. 36: 3971-80. PMID 9092827 DOI: 10.1021/bi962188y |
0.64 |
|
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