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

 
Specialties
  • Molecular Biology/Biochemistry

​Publications

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

Publications
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 (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 (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 (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 (33):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 (14):3542-52. [Full Text/Abstract]
Sharma D, Martineau CN, Le Dall MT, Reidy M, Masison DC, Kabani M. Function of SSA subfamily of Hsp70 within and across species varies widely in complementing Saccharomyces cerevisiae cell growth and prion propagation. PLoS One. 2009 Aug 14; 4 (8):e6644. [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 (2):611-20. [Full Text/Abstract]
Tutar Y, Song Y, Masison DC. Primate chaperones Hsc70 (constitutive) and Hsp70 (induced) differ functionally in supporting growth and prion propagation in Saccharomyces cerevisiae. Genetics. 2006 Feb; 172 (2):851-61. [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 (40):34178-85. [Full Text/Abstract]
Song Y, Wu YX, Jung G, Tutar Y, Eisenberg E, Greene LE, Masison DC. Role for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication. Eukaryot Cell. 2005 Feb; 4 (2):289-97. [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):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):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 (11):3590-8. [Full Text/Abstract]