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Daniel                         Gewirth

Daniel T. Gewirth PhD

Department of Structural Biology

Principal Research Scientist, Hauptman-Woodward Institute


Education and Training:
  • PhD, Molecular Biophysics and Biochemistry, Yale University (1988)
  • BS, Chemistry, University of Chicago, Honors (1982)
  • Senior Research Scientist, Hauptman-Woodward Institute (2005-present)
  • Associate Professor, Structural Biology, SUNY-Buffalo (2005-present)
  • Assistant Professor, Biochemistry, Duke University, School of Medicine (1997–2005)
  • Post Doctoral Fellow, Molecular Biophysics and Biochemistry, Yale University (1989–1997)
  • Postdoctoral Research Associate, Biochemistry and Molecular Biology, Harvard University (1988–1989)
  • Graduate Student, Molecular Biophysics and Biochemistry, Yale University (1982–1988)
Awards and Honors:
  • Leukemia Society of America, Special Fellow, 1993-1996 (1993)
  • American Cancer Society, Postdoctoral Fellowship, 1990-1991 (1990)

Research Expertise:
  • Structure and Function of Molecular Chaperones: My lab has been at the forefront of detailed structure/function analyses of GRP94, the ER hsp90. Over the past 10 years we have determined the high resolution X-ray structure of the intact chaperone, its isolated regulatory domain, and its bi-domain constructs. We have discovered the structural features that render this chaperone unique among the hsp90 family and maintain an active research program focused on analyzing these structural discoveries, exploiting them in the development of novel inhibitors, and probing the interaction of GRP94 and other hsp90s with clients and co-chaperones. We have initiated collaborations with leading cell biologists and medicinal chemists in this field with the goal of exploiting novel assays of hsp90 function and developing and analyzing new inhibitors with therapeutic and research potential.
  • Structure and Function of Steroid and Nuclear Hormone Receptors: My lab has a long history of detailed structure/function analyses of steroid and nuclear hormone receptors. Our earlier work has focused on understanding the DNA binding specificity of the Thyroid hormone receptor, the Vitamin D receptor, and the Androgen receptor, and we have maintained a long-running program to determine the structure of intact hormone receptors as well. The advent of rapid in silico screening protocols has now opened the possibility of exploiting these earlier structural studies for inhibitor development. We have initiated collaborations with leading cell biologists and medicinal chemists with the goal of developing and analyzing new inhibitors with therapeutic and research potential.
Grants and Sponsored Research:
  • July 2014–June 2017
    Development of a New Class of Drugs to Inhibit All Forms of Androgen Receptor in Castration-Resistant Prostate Cancers
    U.S. Army Medical Research & Materiel Command
    Role: Co-Investigator
  • June 2013–June 2016
    New Approaches to Fighting Difficult Bacterial Pathogens
    Goode Foundation
    Role: Principal Investigator
  • May 2005–March 2016
    Structure and Regulation of hsp90 Chaperones (R01-CA095130)
    Role: Principal Investigator
  • August 2008–July 2012
    Studies of hsp90 Mechanism and Function
    Role: Co-Investigator
  • July 2010–June 2011
    Focal Adhesion Kinase-Tumor biology and therapeutics
    Role: Co-Investigator
  • April 2002–March 2009
    Structural Studies of the Vitamin D Receptor (R01-DK058857)
    Role: Principal Investigator
  • November 2004–July 2008
    Nanoliter Lab-on-a-Chip Protein Crystallization
    Role: Co-Investigator
  • February 2002–March 2005
    Structural and Functional Analysis of Androgen Receptor-DNA Interactions (DAMD17-02-1-0050)
    US Army
    Role: Principal Investigator
  • Isolated GRP94 ligand binding domain polypeptide and nucleic acid encoding The present invention relates to compositions and methods pertaining to the modulation of molecular chaperone function by regulatory ligands. In a preferred embodiment, the present invention relates to an isolated and purified GRP94 ligand binding domain (LBD) polypeptide, to an isolated nucleic acid encoding the same, and to screening methods associated therewith. (2007)

Journal Articles:
See all (13 more)

Service Activities:
  • Jacobs School of Medicine & Biomedical Sciences Admissions Committee; Member (2009)
  • Scientific Governance Council, Hauptman-Woodward Institute; Vice-Chair (2007–present)
  • Faculty Search Committee, Dept. of Structural Biology/HWI; Member (2006–2007)
  • Faculty Search Committee, Duke University, Dept of Biochemistry; Member (2000–2004)
  • Seminar Committee, Dept. of Biochemistry, Duke University; Chair (2000–2004)
  • Graduate Admissions Committe, Dept. of Biochemistry, Duke University; Member (1999–2004)
  • Mentor, Project SEED, American Chemical Society; Project SEED mentor, summer 1999 (Roshanda Bullock), 2001 (Bryant Price), 2002 (Bryant Price), 2003 (Cara Oxendine). Project SEED is a program sponsored by the American Chemical Society that places minority students from local high schools in university research labs with the goal of encouraging their interest in scientific careers. I mentored students for 4 summers. Two of these students were African-American (Bullock, Price) and the third was Native American (Oxendine). Neither the PI nor the lab was compensated for our involvement in this program.; Sponsor (1999–2003)

School News:
In the Media:

Clinical Specialties:
Clinical Offices:
Insurance Accepted:

Contact Information

1 Hauptman-Woodward Institute
700 Ellicott Street
Buffalo, NY 14203
Phone: (716) 898-8635
Fax: 716-898-8660

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