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COBRE-PSF Celebrates Successes

At KU, an NIH-funded center has been making real progress toward its goals. The Center of Biomedical Research Excellence in Protein Structure and Function (COBRE-PSF) pursues basic research, but also assists junior faculty to establish both their laboratories and their biomedical research careers. The Center is open to junior faculty at any of these four Kansas institutions: Kansas State University (KSU), The University of Kansas (KU), The University of Kansas Medical Center (KUMC) and Wichita State University (WSU). The program began in late 2002 with six junior investigators and one collaborating investigator spread among three campuses (KSU, KU, and WSU). After only three years these original six investigators have already “graduated” by obtaining their own independent (NIH) research funding.

When they achieve independent funding, the junior faculty member moves from the assisted and mentored portion of the program to another role, providing leadership and support to the new investigators that are added as the program continues to grow. In addition to the six graduates, the Center has now grown to include another 17 junior faculty investigators in 13 departments on four campuses.

The names of six “graduated” COBRE-PSF researchers and descriptions of their independent research projects are listed below.

Brian Blagg, KU Assistant Professor of Medicinal Chemistry
HTS Assays for Hsp90 Inhibitors
Dr. Blagg’s grant supports his research on the protein Hsp90, a molecular chaperone responsible for folding newly synthesized proteins into their biologically active, three-dimensional conformations. Hsp90 inhibition offers a promising new target for the development of anticancer chemotherapeutic.

 

Heather Desaire, KU Assistant Professor, Chemistry
Comparative Glycomics of the HIV Protein gp120
The glycoprotein gp120, which covers the surface of the HIV virus, binds to receptor sites in the body. Dr. Desaire’s research focuses on the carbohydrates or glycans on gp120 that block antibody attack and prevent the immune system from destroying the virus. The results may be used toward creating a HIV vaccine.

 

Susan Egan, KU Associate Professor of Molecular Biosciences
Transcription Activation at the rhaBAD Operon
Antibiotics have dramatically reduced deaths caused by bacterial infections. However this advantage over our bacterial foes is declining as antibiotic resistance becomes increasingly prevalent. Dr. Egan’s work involves finding novel targets for antibacterial agents to avoid the rise again of deaths due to bacterial infections. She is investigating AraC/XylS transcription activators, which have been indicated as potential targets.

 

William Picking, KU Associate Professor of Molecular Biosciences
Structure and Function of IpaC from Shigella flexneri
Shigella flexneri is a pathogen that causes bacillary dysentery (shigellosis), which continues to be an important worldwide public health problem. An essential step in how shigellosis causes dysentery is its bacterial invasion of the epithelial cells of the colon. Dr. Picking is studying invasion plasmid antigen C (IpaC), the effector protein that allows Shigella to be absorbed into the body. Picking’s research is to determine the organization of IpaC and how it subverts the host cell cytoskeleton.

 

Jeffrey L. Staudinger, KU Assistant Professor of Pharmacology and Toxicology
Cell Signaling, PXR Phosphorylation & Drug Disposition
The pregnane X receptor (PXR), a ligand-activated transcription factor regulates the drug-inducible expression of drug-transporting and drug-metabolizing proteins. PXR-target gene expression can be repressed in people undergoing invasive surgery due to inflammation, which can produce potentially life-threatening drug-drug interactions. Dr. Staudinger’s research focuses on understanding the molecular basis of the repression of PXR-target genes to help predict and prevent these drug interactions.

 

Anna Zolkiewska, KSU Associate Professor of Biochemistry
Molecular Analysis of Metalloprotease Disintegrin ADAM12
ADAMs is a family of cell surface proteins that play important roles in many biological processes involving cell surface proteolysis, cell-cell, or cell-matrix interactions. Zolkiewska is focusing her studies on ADAM12, an ADAM family member involved in skeletal muscle development and/or regeneration. These studies may explain the biology of satellite cells and their role in muscle growth and repair.

 

Higuchi Biosciences Center
University of Kansas
2099 Constant Avenue
Lawrence, KS 66047-2535
785-864-5183
hbc@ku.edu

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