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University of Maryland School of Medicine Division of Infectious Diseases

 
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Michael E. Kleinberg, MD, PhD
Associate Professor of Medicine

MD: Albert Einstein College of Medicine, 1984
PhD: Albert Einstein College of Medicine, 1984

Phone: (410) 328-2679
Fax: (410) 706-8700
E-mail: mkleinbe@umaryland.edu
Address:
Division of Infectious Diseases
University of Maryland School of Medicine
10 S. Pine St., MSTF 900
Baltimore, MD 21201

RESEARCH INTERESTS

Dr. Kleinberg's basic science research interests are focused on the roles of neutrophil-generated oxidants in host defense and inflammation.  Neutrophils (and other white blood cells) deploy a number of strategies to combat infectious microorganisms.  Oxidants, such as superoxide and hydrogen peroxide, are particularly potent weapons for killing pathogens.  However, these oxidants have been implicated in some inflammatory diseases when they are produced inadvertently in the absence of infection.  Dr. Kleinberg's laboratory investigates what signals turn on and off oxidant production specifically in the face of an infection.  In his clinical practice, Dr. Kleinberg specializes in treating infections that complicate treatment of patients with cancer, particularly patients with leukemia or receiving a bone marrow transplant.  A transient reduction in neutrophils and other white blood cells secondary to the effects of chemotherapy leaves cancers patients and potentially high risk for life-threatening infections.  Dr. Kleinberg along with other Infectious Diseases faculty in the Greenebaum Cancer Center run an active clinical research program investigating the potential benefits of new antibiotics to fight infections as well as developing new approaches to optimizing use of antibiotics already available.  Dr. Kleinberg also collaborates with Dr. Cross in developing new therapies for boosting the immune response in cancer patients.

RECENT PUBLICATIONS

Faris, S.L., Rinckel, L.A., Huang, J., Hong, Y-R., and Kleinberg, M.E.  1998.  Phagocyte NADPH Oxidase p67-phox Possesses a Novel Carboxylterminal Binding Site for the GTPases Rac2 and Cdc42.  Biochem. Biophys. Res. Comm. 247:271-276.

Huang, J., and Kleinberg, M.E. 1999.  Activation of NADPH Oxidase p47-phox Involves Disruption of Internal Binding Between the p47-phox SH3 Domains and the Arginine/Lysine-Rich p47-phox C-terminus.  J. Biol. Chem. 274:19731-19737.

Rinckel, L.A., Faris, S.L., Hitt, N., and Kleinberg, M.E. 1999. Rac1 Disrupts p67-phox/p40-phox Binding: A Novel Role for Rac in NADPH Oxidase Activation. Biochem. Biophys. Res. Comm. 263:118-122.

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To contact us:

Phone: 410-706-7560
Fax: 410-706-4619
E-mail: kvardjan@ihv.umaryland.edu

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