UMDNJ - ROBERT WOOD JOHNSON MEDICAL SCHOOL
DEPARTMENT OF PATHOLOGY AND LABORATORY MEDICINE

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  Faculty Information

Donald A. Winkelmann, Ph.D.

Position: Associate Professor of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School,

Administrative: Chief, Division of Medical Informatics, UMDNJ - Robert Wood Johnson Medical School

Co-Director of graduate programs in Molecular Biosciences, Rutgers/UMDNJ

Department: Pathology and Laboratory Medicine

Lab Url: http://pleiad.umdnj.edu/~daw/index.htm

Phone Number: (732) 235-4759

Fax Number: (732) 235-4825

Email Address: winkelma@umdnj.edu

Clinical and Research Interests
 

The focus of our research is the study of macromolecular structure and assembly with our efforts concentrated on the analysis of the protein myosin and its interaction with actin. Actin and myosin are highly conserved proteins that participate in determination of cell shape, cellular motility, cytokinesis and contractility. Our research uses the techniques of protein biochemistry, molecular genetics, immunochemistry, electron microscopy and crystallography to analyze myosin structure, assembly and function. These studies have contributed to the current understanding of myosin structure and have culminated in the determination of the structure of the myosin motor domain at 2.8 Å resolution. The molecular model of myosin is revealing exciting new insights into the fundamental mechanism of biological energy transformation. These structural studies are complemented by the use of molecular genetics and site directed mutagenesis of cloned myosin genes. In addition to its role in generating force and motion in all eukaryotic cells, myosin is a major structural component of the contractile organelle of muscle and non-muscle cells. We are investigating this role by expression of GFP-myosin chimeras and fluorescent microscopy of living cardiac and skeletal muscle cells.

 

Training

bulletUniversity of Wisconsin-Milwaukee, WI, B.S., Chemistry, 1973
bulletUniversity of Wisconsin, Madison, WI, Ph.D., Biochemistry, 1980
bulletStructural Biology Laboratory, Rosenstiel Center, Brandeis University,
Waltham, MA 1980-86
 

Honors and Awards

1973                   B.S. (Magna Cum Laude) Honors in Chemistry
1977 - 1979         NIH National Research Service Award trainee
1980- 1982          Paul Cohen Postdoctoral Fellow, the Muscular Dystrophy
1983 - 1985         Research Fellowship, The Medical Foundation, Inc., Boston
1987 - 1992         Established Investigator, The American Heart Association
 
Certifications Licensure

N.A.

  N.A.
Office Address   Mailing Address
Department of Pathology & Laboratory Medicine
675 Hoes Lane
UMDNJ - Robert Wood Johnson Medical School
Piscataway, NJ 08854, USA
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Selected Publications
  1. Xiang, X., G. Han, D.A. Winkelmann, W. Zuo and N.R. Morris. (2000) dynamics of cytoplasmic dynein in living cells and the effect of a mutation in the dynactin complex actin-related protein Arp1. Current Biology 10: 603-606.
  2. Srikakulam, R. and D.A. Winkelmann. (1999) Myosin II Folding is Mediated by a Molecular chaperonin. J. Biol. Chem. 274:27265-27273.
  3. Colognato, H., D.A. Winkelmann and P.D. Yurchenco. (1999) Laminin Polymerization Induces a receptor-cytoskeleton network. J. Cell Biol. 145:619-631.
  4. Riveline, D., A. Ott, F. Julicher, D.A. Winkelmann, O. Cardoso, J-J. Lacapere, S. Magnusfottir, J-L. Viovy, L. Gorre-Talini and J. Prost. (1998) Acting on actin: The electric motility assay. Eur. J. Biophys. 27:403-408.
  5. Birk, D.E., Zycband, E.I., Woodruff, S., Winkelmann D.A. and Trelstad, R.L. (1997). Collagen fibrillogenesis in situ: Fibril segments become long fibrils as the developing tendon matures. Dev. Dynamics. 208:291-298.
  6. Kinose, F., Wang, S.X., Kidambi, U., Moncman , C.L. and Winkelmann, D.A. (1996). Glycine 699 is pivotal for the motor activity of skeletal muscle myosin. J. Cell Biol. 134:895-909.
  7. Winkelmann, D.A., Bourdieu, L., Ott, A., Kinose, F. and Libchaber, A. (1995). The flexibility of myosin attachment to surfaces influences F-actin motion. Biophys. J. 68: 2444-2453.
  8. Bourdieu, L. Duke, T., Elowits, M.B., Winkelmann, D.A., Leibler, S. and Libchaber, A. (1995). Spiral defects in motility assays: a measure of motor protein force. Phys. Rev. Lett. 75:176-179.
  9. Bourdieu, L., Magnasco, M.O., Winkelmann, D.A., Libchaber, A. (1995). Actin filaments on myosin beds, the velocity distribution. Phys. Rev. E, 52:6573-6579.
Postdoctoral Position Available
None
 
Research Positions Available

None
 

Updated Date
08/11/2008

 

 

 

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