Detection of MNCF lectin in mast cell (2008)
- Authors:
- USP affiliated authors: BARREIRA, MARIA CRISTINA ROQUE ANTUNES - FMRP ; OLIVER, CONSTANCE - FMRP
- Unidade: FMRP
- Subjects: CÉLULAS-TRONCO; MICROSCOPIA DE FLUORESCÊNCIA
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Programa e Resumos
- Conference titles: Congresso da Sociedade Brasileira de Biologia Celular
-
ABNT
PEREIRA, Fernando Lourenço et al. Detection of MNCF lectin in mast cell. 2008, Anais.. São Paulo: SBBC, 2008. . Acesso em: 20 set. 2024. -
APA
Pereira, F. L., Bernardes, E. S., Jamur, M. C., Oliver, C., & Roque-Barreira, M. C. (2008). Detection of MNCF lectin in mast cell. In Programa e Resumos. São Paulo: SBBC. -
NLM
Pereira FL, Bernardes ES, Jamur MC, Oliver C, Roque-Barreira MC. Detection of MNCF lectin in mast cell. Programa e Resumos. 2008 ;[citado 2024 set. 20 ] -
Vancouver
Pereira FL, Bernardes ES, Jamur MC, Oliver C, Roque-Barreira MC. Detection of MNCF lectin in mast cell. Programa e Resumos. 2008 ;[citado 2024 set. 20 ] - KM+ attractant lectin intracts with a glycoprotein on the surface of human neutrophils
- Km+ attractant lectin interacts with a Glycoprotein on the surface of human neutrophils
- Paracoccin, A N-acetyl-glucosamine binding lectin released by Paracoccidioides brasiliensis, is expressed on yeast surface and binds selectively to laminin
- MNCF and KM+ interact with glycosolated components of the mast cell surface
- Lectinas KM+, CONA e WGA induzem um aumento de mastócitos na medula óssea após depleção da cavidade peritoneal
- Distribuição dos mastócitos na medula óssea do femur de ratos
- Neutrophil haptotaxis induced by 'KM POT.+' interactions estabilished on cell surface
- Lack of galectin-3 alters the balance of innate immune cytokines and confers resistance to Rhodococcus equi infection
- Interaction of the animal lectin MNCF with glycosylated components on the neutrophil surface induces morphological and functional changes
- MNCF and 'KM POT.+' induce mast cell degranulation by interaction with glycosylated components on the cell surface: the role of this action in neutrophil migration
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