Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Project (R01)
Project #
5R01CA064394-03
Application #
2106831
Study Section
Experimental Immunology Study Section (EI)
Project Start
1994-07-01
Project End
1997-04-30
Budget Start
1996-05-01
Budget End
1997-04-30
Support Year
3
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Fordham University
Department
Biology
Type
Other Domestic Higher Education
DUNS #
City
Bronx
State
NY
Country
United States
Zip Code
10458
Basu, Sreyashi; Srivastava, Pramod (2005) Immunological role of neuronal receptor vanilloid receptor 1 expressed on dendritic cells. Proc Natl Acad Sci U S A 102:5120-5
Chandawarkar, Rajiv Y; Wagh, Mihir S; Kovalchin, Joseph T et al. (2004) Immune modulation with high-dose heat-shock protein gp96: therapy of murine autoimmune diabetes and encephalomyelitis. Int Immunol 16:615-24
Basu, Sreyashi; Srivastava, Pramod K (2003) Fever-like temperature induces maturation of dendritic cells through induction of hsp90. Int Immunol 15:1053-61
Panjwani, Naveed N; Popova, Lana; Srivastava, Pramod K (2002) Heat shock proteins gp96 and hsp70 activate the release of nitric oxide by APCs. J Immunol 168:2997-3003
Robert, J; Menoret, A; Srivastava, P K et al. (2001) Immunological properties of heat shock proteins are phylogenetically conserved. Adv Exp Med Biol 484:237-49
Robert, J; Menoret, A; Basu, S et al. (2001) Phylogenetic conservation of the molecular and immunological properties of the chaperones gp96 and hsp70. Eur J Immunol 31:186-95
Basu, S; Binder, R J; Ramalingam, T et al. (2001) CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity 14:303-13
Matsutake, T; Srivastava, P K (2001) The immunoprotective MHC II epitope of a chemically induced tumor harbors a unique mutation in a ribosomal protein. Proc Natl Acad Sci U S A 98:3992-7
Binder, R J; Blachere, N E; Srivastava, P K (2001) Heat shock protein-chaperoned peptides but not free peptides introduced into the cytosol are presented efficiently by major histocompatibility complex I molecules. J Biol Chem 276:17163-71
Menoret, A; Li, Z; Niswonger, M L et al. (2001) An endoplasmic reticulum protein implicated in chaperoning peptides to major histocompatibility of class I is an aminopeptidase. J Biol Chem 276:33313-8

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