Roberto Dominguez, PhD

Professor Of Physiology

Lab Web Site

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728 Clinical Research Building

415 Curie Boulevard

Philadelphia, PA 19104

215-573-4559

Lab: 215-573-0983

Fax: 215-573-2273

droberto@mail.med.upenn.edu

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Roberto Dominguez, PhD


Professor Of Physiology

Other Perelman School of Medicine Affiliations


Degrees & Education

  • PhD, Pasteur Institute and Paris-Sud University, France, 1996

  • MS, Odessa State University, formerly-USSR, 1987


Honors

  • 2006-2010 NIH Study Section (MSFC),

  • 2006 Co-Chair Motility Subgroup of the Biophysical Societ

  • 2002 American Heart Association, Established Investigator Award

  • 1999 American Heart Association, Grant-in-Aid Junior Investigator Award

  • 1998 March of Dimes, Basil O’Connor Scholar

  • 1992 Fellow of the German Academic Exchange Service (DAAD)

  • 1989 Fellow of the Société Française de Belgique

  • Member of the Editorial Board of Biophysical Journal


Professional Affiliations

  • The American Society for Cell Biology

  • American Crystallographic Association

  • Biophysical Society

  • American Heart Association

  • American Association for the Advancement of Science


Research Description

The actin cytoskeleton plays an essential role in multiple cellular functions, including cytokinesis, vesicular trafficking and the maintenance of cell shape and polarity. To accomplish these functions, the cytoskeleton undergoes constant remodeling into various forms of structural and functional networks, such as lamellipodia, filopodia, stress fibers and focal adhesions. Remodeling of the cytoskeleton is a tightly regulated process, involving hundreds of actin-binding and signaling proteins. The main focus of the research in our lab is to understand the molecular basis for how protein-protein interaction networks bring together cytoskeleton scaffolding, nucleation, elongation, and signaling proteins to accomplish specific cellular functions.

Our primary research tool is protein X-ray crystallography. The atomic “snapshots” resulting from the X-ray crystal structures of proteins provide a wealth of knowledge, but lack information about the dynamic aspects of protein-protein interactions. To obtain this kind of information we also use a host of other approaches, including mutagenesis, bio-informatics, biophysical and biochemical methods.


Click here for a full list of publications.
(searches the National Library of Medicine's PubMed database.)


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