Source: Biochemistry. Unidade: IFSC
Subjects: PROTEÍNAS (ESTUDO), CRISTALOGRAFIA ESTRUTURAL, MODELOS (ESTRUTURA)
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AZEVEDO, Estefania P. C. et al. Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis: identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid. Biochemistry, v. 50, n. 51, p. 11070-11083, 2011Tradução . . Disponível em: https://doi.org/10.1021/bi201365r. Acesso em: 18 nov. 2024.APA
Azevedo, E. P. C., Pereira, H. D. 'M., Garratt, R. C., Kelly, J. W., Foguel, D., & Palhano, F. L. (2011). Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis: identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid. Biochemistry, 50( 51), 11070-11083. doi:10.1021/bi201365rNLM
Azevedo EPC, Pereira HD'M, Garratt RC, Kelly JW, Foguel D, Palhano FL. Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis: identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid [Internet]. Biochemistry. 2011 ; 50( 51): 11070-11083.[citado 2024 nov. 18 ] Available from: https://doi.org/10.1021/bi201365rVancouver
Azevedo EPC, Pereira HD'M, Garratt RC, Kelly JW, Foguel D, Palhano FL. Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis: identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid [Internet]. Biochemistry. 2011 ; 50( 51): 11070-11083.[citado 2024 nov. 18 ] Available from: https://doi.org/10.1021/bi201365r