Cloning, recombinant expression and refolding of pulchelin binding domain, from Abrus pulchellus seeds (2001)
- Autores:
- Autores USP: BELTRAMINI, LEILA MARIA - IFSC ; ARAUJO, ANA PAULA ULIAN DE - IFSC
- Unidade: IFSC
- Assuntos: PROTEÍNAS; BIOQUÍMICA
- Idioma: Inglês
- Imprenta:
- Fonte:
- Título do periódico: Program and abstracts
- Nome do evento: International Conference on Biology and Synchrotron Radiation
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ABNT
GOTO, Leandro Seiji et al. Cloning, recombinant expression and refolding of pulchelin binding domain, from Abrus pulchellus seeds. 2001, Anais.. Sao Pedro: Instituto de Física de São Carlos, Universidade de São Paulo, 2001. . Acesso em: 25 set. 2024. -
APA
Goto, L. S., Beltramini, L. M., Moraes, D. I., & Araújo, A. P. U. de. (2001). Cloning, recombinant expression and refolding of pulchelin binding domain, from Abrus pulchellus seeds. In Program and abstracts. Sao Pedro: Instituto de Física de São Carlos, Universidade de São Paulo. -
NLM
Goto LS, Beltramini LM, Moraes DI, Araújo APU de. Cloning, recombinant expression and refolding of pulchelin binding domain, from Abrus pulchellus seeds. Program and abstracts. 2001 ;[citado 2024 set. 25 ] -
Vancouver
Goto LS, Beltramini LM, Moraes DI, Araújo APU de. Cloning, recombinant expression and refolding of pulchelin binding domain, from Abrus pulchellus seeds. Program and abstracts. 2001 ;[citado 2024 set. 25 ] - Interaction of internal peptides from the bovine DGAT1 enzyme with membrane models
- Genomic cloning, expression and spectroscopyc characterization of the pulchellin 'alfa'-chain, preliminary studies
- Use of peptides to investigate the binding sites of the diacylglycerol acyltransferase1 enzyme
- Synchrotron radiation circular dichroism to study the binding of the DGAT1 peptides with substrates
- Cloning, recombinant expression and protein characterization of pulchelin binding domain from Abrus pulchellus seeds
- Pulchellin, a highly toxic type 2 ribosome-inactivating protein from Abrus pulchellus cloning: heterologous expression of A-chain and structural studies
- Heterologous expression, characterization and structural studies of a highly hydrophobic peptide from the HIV-1 capsid protein (P24)
- Deconstructing the DGAT1 enzyme: binding sites and substrate interactions
- Heterologous expression, characterization and structural studies of a hydrophobic peptide from the HIV-1 p24 protein
- Production of Abrus pulchellus ribosome-inactivating protein from seeds callus culture
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