This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Cysteine proteases are present in nearly all groups of eukaryotes and play vital roles in a wide range of biological processes and diseases, including antigen processing, bacterial infection, arthritis, osteoporosis, Alzheimer?s disease and cancer cell invasion. Several cysteine proteases of the papain superfamily are critical to the life-cycle progression of many pathogenic protozoa and therefore they represent potential targets for selective inhibitor design. It has also been determined that members of this same class of enzyme are required for human allergic and asthmatic response to the common house dust mite. High-resolution structural studies have provided valuable information for the design of anti-parasitic therapeutics that selectively regulate the cysteine protease cruzain, a key enzyme in the lifecycle of T. cruzi, the causative agent of Chagas? disease. The studies detailed in this program will expand our understanding and ability to regulate several new protease targets indicated in a variety of parasitic infections as well as proteases of dust mite allergy induced asthma.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR001209-31
Application #
8169926
Study Section
Special Emphasis Panel (ZRG1-BCMB-P (40))
Project Start
2010-05-01
Project End
2011-02-28
Budget Start
2010-05-01
Budget End
2011-02-28
Support Year
31
Fiscal Year
2010
Total Cost
$3,735
Indirect Cost
Name
Stanford University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
009214214
City
Stanford
State
CA
Country
United States
Zip Code
94305
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