Deconstructing the DGAT1 enzyme: binding sites and substrate interactions (2014)
- Authors:
- USP affiliated authors: BELTRAMINI, LEILA MARIA - IFSC ; ARAUJO, ANA PAULA ULIAN DE - IFSC
- Unidade: IFSC
- DOI: 10.1016/j.bbamem.2014.08.017
- Subjects: ENZIMAS; FILMES FINOS; ESPECTROSCOPIA
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Biochimica et Biophysica Acta : Proteins and Proteomics
- ISSN: 1570-9639
- Volume/Número/Paginação/Ano: v. 1838, n. 12, p. 3145-3152, Dec. 2014
- Este periódico é de assinatura
- Este artigo é de acesso aberto
- URL de acesso aberto
- Cor do Acesso Aberto: hybrid
- Licença: publisher-specific-oa
-
ABNT
LOPES, José L. S. et al. Deconstructing the DGAT1 enzyme: binding sites and substrate interactions. Biochimica et Biophysica Acta : Proteins and Proteomics, v. 1838, n. 12, p. 3145-3152, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.bbamem.2014.08.017. Acesso em: 23 abr. 2024. -
APA
Lopes, J. L. S., Nobre, T. M., Cilli, E. M., Beltramini, L. M., Araújo, A. P. U. de, & Wallace, B. A. (2014). Deconstructing the DGAT1 enzyme: binding sites and substrate interactions. Biochimica et Biophysica Acta : Proteins and Proteomics, 1838( 12), 3145-3152. doi:10.1016/j.bbamem.2014.08.017 -
NLM
Lopes JLS, Nobre TM, Cilli EM, Beltramini LM, Araújo APU de, Wallace BA. Deconstructing the DGAT1 enzyme: binding sites and substrate interactions [Internet]. Biochimica et Biophysica Acta : Proteins and Proteomics. 2014 ; 1838( 12): 3145-3152.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1016/j.bbamem.2014.08.017 -
Vancouver
Lopes JLS, Nobre TM, Cilli EM, Beltramini LM, Araújo APU de, Wallace BA. Deconstructing the DGAT1 enzyme: binding sites and substrate interactions [Internet]. Biochimica et Biophysica Acta : Proteins and Proteomics. 2014 ; 1838( 12): 3145-3152.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1016/j.bbamem.2014.08.017 - Solubility studies and Circular Dichroism analysis of the Adenine phosphoribosyltransferase(APRT), as a PH function
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Informações sobre o DOI: 10.1016/j.bbamem.2014.08.017 (Fonte: oaDOI API)
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