Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI032966-04
Application #
2067915
Study Section
Tropical Medicine and Parasitology Study Section (TMP)
Project Start
1992-07-01
Project End
1996-12-14
Budget Start
1995-05-01
Budget End
1996-12-14
Support Year
4
Fiscal Year
1995
Total Cost
Indirect Cost

  Institution

Name
New York University
Department
Pathology
Type
Schools of Medicine
DUNS #
004514360
City
New York
State
NY
Country
United States
Zip Code
10012

  Publications

Coppel, R L; Brown, G V; Nussenzweig, V (1998) Adhesive proteins of the malaria parasite. Curr Opin Microbiol 1:472-81
Raper, J; Nussenzweig, V; Tomlinson, S (1996) The main lytic factor of Trypanosoma brucei brucei in normal human serum is not high density lipoprotein. J Exp Med 183:1023-9
Medina-Acosta, E; Franco, A M; Jansen, A M et al. (1994) Trans-sialidase and sialidase activities discriminate between morphologically indistinguishable trypanosomatids. Eur J Biochem 225:333-9
Tomlinson, S; Pontes de Carvalho, L C; Vandekerckhove, F et al. (1994) Role of sialic acid in the resistance of Trypanosoma cruzi trypomastigotes to complement. J Immunol 153:3141-7
Schenkman, S; Eichinger, D; Pereira, M E et al. (1994) Structural and functional properties of Trypanosoma trans-sialidase. Annu Rev Microbiol 48:499-523
Pontes de Carvalho, L C; Tomlinson, S; Vandekerckhove, F et al. (1993) Characterization of a novel trans-sialidase of Trypanosoma brucei procyclic trypomastigotes and identification of procyclin as the main sialic acid acceptor. J Exp Med 177:465-74
Tomlinson, S; Pontes de Carvalho, L; Vandekerckhove, F et al. (1992) Resialylation of sialidase-treated sheep and human erythrocytes by Trypanosoma cruzi trans-sialidase: restoration of complement resistance of desialylated sheep erythrocytes. Glycobiology 2:549-51