U.S. Department of Health and Human Services
Daniel Masison

 Contact Info

Tel: 301-594-1316
Email: danielmas@helix.nih.gov

 Select Experience

  • Ph.D.University of Massachusetts Medical Center1993
  • B.S.University of Massachusetts1983

 Related Links

  • Molecular Biology/Biochemistry


A selection of recent and significant publications can be viewed below.

Reidy M, Sharma R, Roberts BL, Masison DC. Human J-protein DnaJB6b Cures a Subset of Saccharomyces cerevisiae Prions and Selectively Blocks Assembly of Structurally Related Amyloids. J Biol Chem. 2015 Dec 23; 291 (291; 8; 2015 Dec 23):4035-47. [Full Text/Abstract]
Reidy M, Sharma R, Shastry S, Roberts BL, Albino-Flores I, Wickner S, Masison DC. Hsp40s specify functions of hsp104 and hsp90 protein chaperone machines. PLoS Genet. 2014 Oct; 10 (2014 Oct; 10):e1004720. [Full Text/Abstract]
Park YN, Zhao X, Yim YI, Todor H, Ellerbrock R, Reidy M, Eisenberg E, Masison DC, Greene LE. Hsp104 overexpression cures yeast [PSI+] by causing dissolution of the prion seeds. Eukaryot Cell. 2014 May; 13 (2014 May; 13; 5):635-47. [Full Text/Abstract]
Kumar N, Gaur D, Masison DC, Sharma D. The BAG Homology Domain of Snl1 Cures Yeast Prion [URE3] Through Regulation of Hsp70 Chaperones. G3 (Bethesda). 2014 Mar 20; 4 (2014 Mar 20; 4; 3):461-70. [Full Text/Abstract]
Reidy M, Miot M, Masison DC. Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions. Genetics. 2012 Sep; 192 (2012 Sep; 192; 1):185-93. [Full Text/Abstract]
Sharma D, Masison DC. Single methyl group determines prion propagation and protein degradation activities of yeast heat shock protein (Hsp)-70 chaperones Ssa1p and Ssa2p. Proc Natl Acad Sci U S A. 2011 Aug 16; 108 (108; 33; 2011 Aug 16):13665-70. [Full Text/Abstract]
Reidy M, Masison DC. Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104. Mol Cell Biol. 2010 Jul; 30 (30; 14; 2010 Jul):3542-52. [Full Text/Abstract]
Hung GC, Masison DC. N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression. Genetics. 2006 Jun; 173 (2006 Jun; 2; 173):611-20. [Full Text/Abstract]
Song Y, Masison DC. Independent regulation of Hsp70 and Hsp90 chaperones by Hsp70/Hsp90-organizing protein Sti1 (Hop1). J Biol Chem. 2005 Oct 7; 280 (280; 40; 2005 Oct 7):34178-85. [Full Text/Abstract]
Jones G, Song Y, Chung S, Masison DC. Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate binding. Mol Cell Biol. 2004 May; 24 (9; 24; 2004 May):3928-37. [Full Text/Abstract]
Jung G, Jones G, Masison DC. Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance. Proc Natl Acad Sci U S A. 2002 Jul 23; 99 (15; 99; 2002 Jul 23):9936-41. [Full Text/Abstract]
Schwimmer C, Masison DC. Antagonistic interactions between yeast [PSI(+)] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p. Mol Cell Biol. 2002 Jun; 22 (2002 Jun; 22; 11):3590-8. [Full Text/Abstract]