Sort by
Items per page

Send to

Choose Destination

Links from Gene

Items: 1 to 20 of 51


Lifespan Control by Redox-Dependent Recruitment of Chaperones to Misfolded Proteins.

Hanzén S, Vielfort K, Yang J, Roger F, Andersson V, Zamarbide-Forés S, Andersson R, Malm L, Palais G, Biteau B, Liu B, Toledano MB, Molin M, Nyström T.

Cell. 2016 Jun 30;166(1):140-51. doi: 10.1016/j.cell.2016.05.006.


Kinetics of Formation and Asymmetrical Distribution of Hsp104-Bound Protein Aggregates in Yeast.

Paoletti C, Quintin S, Matifas A, Charvin G.

Biophys J. 2016 Apr 12;110(7):1605-14. doi: 10.1016/j.bpj.2016.02.034.


Mechanistic Insights into Hsp104 Potentiation.

Torrente MP, Chuang E, Noll MM, Jackrel ME, Go MS, Shorter J.

J Biol Chem. 2016 Mar 4;291(10):5101-15. doi: 10.1074/jbc.M115.707976.


Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.

O'Driscoll J, Clare D, Saibil H.

J Cell Biol. 2015 Oct 12;211(1):145-58. doi: 10.1083/jcb.201505104.


Cytosolic chaperones mediate quality control of higher-order septin assembly in budding yeast.

Johnson CR, Weems AD, Brewer JM, Thorner J, McMurray MA.

Mol Biol Cell. 2015 Apr 1;26(7):1323-44. doi: 10.1091/mbc.E14-11-1531.


Single-molecule analyses of the dynamics of heat shock protein 104 (Hsp104) and protein aggregates.

Okuda M, Niwa T, Taguchi H.

J Biol Chem. 2015 Mar 20;290(12):7833-40. doi: 10.1074/jbc.M114.620427.


The Hsp104 N-terminal domain enables disaggregase plasticity and potentiation.

Sweeny EA, Jackrel ME, Go MS, Sochor MA, Razzo BM, DeSantis ME, Gupta K, Shorter J.

Mol Cell. 2015 Mar 5;57(5):836-49. doi: 10.1016/j.molcel.2014.12.021.


Dicer and Hsp104 function in a negative feedback loop to confer robustness to environmental stress.

Oberti D, Biasini A, Kirschmann MA, Genoud C, Stunnenberg R, Shimada Y, Bühler M.

Cell Rep. 2015 Jan 6;10(1):47-61. doi: 10.1016/j.celrep.2014.12.006.


Suramin inhibits Hsp104 ATPase and disaggregase activity.

Torrente MP, Castellano LM, Shorter J.

PLoS One. 2014 Oct 9;9(10):e110115. doi: 10.1371/journal.pone.0110115.


Effect of endogenous Hsp104 chaperone in yeast models of sporadic and familial Parkinson's disease.

Gade VR, Kardani J, Roy I.

Int J Biochem Cell Biol. 2014 Oct;55:87-92. doi: 10.1016/j.biocel.2014.08.013.


Hsp104 overexpression cures Saccharomyces cerevisiae [PSI+] by causing dissolution of the prion seeds.

Park YN, Zhao X, Yim YI, Todor H, Ellerbrock R, Reidy M, Eisenberg E, Masison DC, Greene LE.

Eukaryot Cell. 2014 May;13(5):635-47. doi: 10.1128/EC.00300-13.


Regulation of the Hsp104 middle domain activity is critical for yeast prion propagation.

Dulle JE, Stein KC, True HL.

PLoS One. 2014 Jan 23;9(1):e87521. doi: 10.1371/journal.pone.0087521.


Roles of Hsp104 and trehalose in solubilisation of mutant huntingtin in heat shocked Saccharomyces cerevisiae cells.

Saleh AA, Gune US, Chaudhary RK, Turakhiya AP, Roy I.

Biochim Biophys Acta. 2014 Apr;1843(4):746-57. doi: 10.1016/j.bbamcr.2014.01.004.


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

Desantis ME, Sweeny EA, Snead D, Leung EH, Go MS, Gupta K, Wendler P, Shorter J.

J Biol Chem. 2014 Jan 10;289(2):848-67. doi: 10.1074/jbc.M113.520759.


Deciphering the roles of trehalose and Hsp104 in the inhibition of aggregation of mutant huntingtin in a yeast model of Huntington's disease.

Chaudhary RK, Kardani J, Singh K, Banerjee R, Roy I.

Neuromolecular Med. 2014 Jun;16(2):280-91. doi: 10.1007/s12017-013-8275-5.


The interaction of Hsp104 with yeast prion Sup35 as analyzed by fluorescence cross-correlation spectroscopy.

Ohta S, Kawai-Noma S, Kitamura A, Pack CG, Kinjo M, Taguchi H.

Biochem Biophys Res Commun. 2013 Dec 6;442(1-2):28-32. doi: 10.1016/j.bbrc.2013.10.147.


Soluble oligomers are sufficient for transmission of a yeast prion but do not confer phenotype.

Dulle JE, Bouttenot RE, Underwood LA, True HL.

J Cell Biol. 2013 Oct 28;203(2):197-204. doi: 10.1083/jcb.201307040.


Low activity of select Hsp104 mutants is sufficient to propagate unstable prion variants.

Dulle JE, True HL.

Prion. 2013 Sep-Oct;7(5):394-403. doi: 10.4161/pri.26547.


Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor.

Lee J, Kim JH, Biter AB, Sielaff B, Lee S, Tsai FT.

Proc Natl Acad Sci U S A. 2013 May 21;110(21):8513-8. doi: 10.1073/pnas.1217988110.


Characterization and Hsp104-induced artificial clearance of familial ALS-related SOD1 aggregates.

Kim Y, Park JH, Jang JY, Rhim H, Kang S.

Biochem Biophys Res Commun. 2013 May 10;434(3):521-6. doi: 10.1016/j.bbrc.2013.03.107.


Supplemental Content

Support Center