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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 (2011)

Azevedo, Estefania P. C.; Pereira, Humberto D'Muniz; Garratt, Richard Charles ; Kelly, Jeffery W.; Foguel, Debora; Palhano, Fernando L.

Source: Biochemistry. Unidade: IFSC

Subjects: PROTEÍNAS (ESTUDO), CRISTALOGRAFIA ESTRUTURAL, MODELOS (ESTRUTURA)

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ABNT
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: 06 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/bi201365r
NLM
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. 06 ] Available from: https://doi.org/10.1021/bi201365r
Vancouver
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. 06 ] Available from: https://doi.org/10.1021/bi201365r

Conformational differences between the wild type and V30M mutant transthyretin modulate its binding to genistein: implications to tetramer stability and ligand-binding (2010)

Trivella, Daniela B. B.; Bleicher, Lucas; Palmieri, Leonardo de Castro; Wiggers, Helton José; Montanari, Carlos Alberto ; Kelly, Jeffery W.; Lima, Luis Maurício T. R.; Foguel, Débora; Polikarpov, Igor

Source: Journal of Structural Biology. Unidades: IQSC, IFSC

Subjects: CRISTALOGRAFIA (ESTRUTURA), SOJA (ENZIMOLOGIA), PROTEÍNAS (ESTUDO), AMILOIDOSE (ESTUDO;TRATAMENTO)

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