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)
- Authors:
- USP affiliated authors: PEREIRA, HUMBERTO D'MUNIZ - IFSC ; GARRATT, RICHARD CHARLES - IFSC
- Unidade: IFSC
- DOI: 10.1021/bi201365r
- Subjects: PROTEÍNAS (ESTUDO); CRISTALOGRAFIA ESTRUTURAL; MODELOS (ESTRUTURA)
- Language: Inglês
- Imprenta:
- Publisher place: Washington, DC
- Date published: 2011
- Source:
- Título do periódico: Biochemistry
- ISSN: 0006-2960
- Volume/Número/Paginação/Ano: v. 50, n. 51, p. 11070-11083, Dec. 2011
- Este periódico é de assinatura
- Este artigo NÃO é de acesso aberto
- Cor do Acesso Aberto: closed
-
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: 24 abr. 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 abr. 24 ] 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 abr. 24 ] Available from: https://doi.org/10.1021/bi201365r - The crystal complex of phosphofructokinase-2 of Escherichia coli with fructose-6-phosphate: kinetic and structural analysis of the allosteric ATP inhibition
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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
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Informações sobre o DOI: 10.1021/bi201365r (Fonte: oaDOI API)
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