Vesicles shed by Trypanosoma cruzi modulate pro-inflammatory cytokines and mice infection by the parasite (2006)
- Authors:
- USP affiliated authors: SILVA, JOÃO SANTANA DA - FMRP ; COLLI, WALTER - IQ ; ALVES, MARIA JULIA MANSO - IQ
- Unidades: FMRP; IQ
- Subjects: TRYPANOSOMA CRUZI; BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Publisher: Sociedade Brasileira de Protozoologia-SBPz
- Publisher place: São Paulo
- Date published: 2006
- Source:
- Título: Abstracts
- Conference titles: Annual Meeting of the Brazilian Society of Protozoology
-
ABNT
TORRECILHAS, Ana Claudia Trocoli et al. Vesicles shed by Trypanosoma cruzi modulate pro-inflammatory cytokines and mice infection by the parasite. 2006, Anais.. São Paulo: Sociedade Brasileira de Protozoologia-SBPz, 2006. . Acesso em: 07 out. 2024. -
APA
Torrecilhas, A. C. T., Tonelli, R. R., Pavanelli, W. R., Silva, J. S. da, Colli, W., & Alves, M. J. M. (2006). Vesicles shed by Trypanosoma cruzi modulate pro-inflammatory cytokines and mice infection by the parasite. In Abstracts. São Paulo: Sociedade Brasileira de Protozoologia-SBPz. -
NLM
Torrecilhas ACT, Tonelli RR, Pavanelli WR, Silva JS da, Colli W, Alves MJM. Vesicles shed by Trypanosoma cruzi modulate pro-inflammatory cytokines and mice infection by the parasite. Abstracts. 2006 ;[citado 2024 out. 07 ] -
Vancouver
Torrecilhas ACT, Tonelli RR, Pavanelli WR, Silva JS da, Colli W, Alves MJM. Vesicles shed by Trypanosoma cruzi modulate pro-inflammatory cytokines and mice infection by the parasite. Abstracts. 2006 ;[citado 2024 out. 07 ] - Trypanosoma cruzi: vesicles shed by the parasite generate intense inflammatory response and higher number of amastigote nests in infected heart tissue
- Trypanosoma cruzi: modificacion estrutural de las cadenas N-glisidicas de la glicoproteina TC-85 cuando es liberada al medio de cultivo
- Turnover and shedding of the tc-85 surface glycoprotein of trypanosoma cruzi trypomastigotes
- Biosynthesis and expression of tc-85, a glycoprotein involved in cell invasion by t. Cruzi
- Structural studies on the glycoinositolphospholipid anchor of the trypanosoma cruzi trypomastigote tc-85 glycoprotein
- Heterogeneity of t. Cruzi surface antigens detected by monoclonal antibodies
- Trypanosoma cruzi binds to laminin in a carbohydrate-independent way
- A fragment of the T. cruzi surface glycoprotein Tc-85 enhances endocytic and secretory activities of host epithelial cells
- The N-domain of the T. cruzi surface glycoprotein Tc85-11 interacts with laminin
- Evidence for a trypanothione-dependent peroxidase system in Trypanosoma cruzi
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