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Characterization of a novel dimeric variant of the amyloidogenic protein transthyretin involved in familial amyloidotic cardiomyopathy (2022)
Martins, Lucas do Amaral; Ferreira, Priscila; Lima, Cinthia; Vasques, João; Jager, Marcus; Monteiro, Cecilia; Pereira, Humberto d'Muniz ; Palhano, Fernando; Kelly, Jeffery; Waddington-Cruz, Márcia; Foguel, Debora
Source: Abstract book. Conference titles: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology - SBBq. Unidade: IFSC
Subjects: MIOCARDIOPATIAS, AMILOIDOSE, PROTEÍNAS
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ABNT
MARTINS, Lucas do Amaral et al. Characterization of a novel dimeric variant of the amyloidogenic protein transthyretin involved in familial amyloidotic cardiomyopathy. 2022, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq, 2022. Disponível em: https://repositorio.usp.br/directbitstream/e156b1ee-7526-4d5e-8bc8-e90c2b185157/3100577.pdf. Acesso em: 29 maio 2024.
APA
Martins, L. do A., Ferreira, P., Lima, C., Vasques, J., Jager, M., Monteiro, C., et al. (2022). Characterization of a novel dimeric variant of the amyloidogenic protein transthyretin involved in familial amyloidotic cardiomyopathy. In Abstract book. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq. Recuperado de https://repositorio.usp.br/directbitstream/e156b1ee-7526-4d5e-8bc8-e90c2b185157/3100577.pdf
NLM
Martins L do A, Ferreira P, Lima C, Vasques J, Jager M, Monteiro C, Pereira H d'M, Palhano F, Kelly J, Waddington-Cruz M, Foguel D. Characterization of a novel dimeric variant of the amyloidogenic protein transthyretin involved in familial amyloidotic cardiomyopathy [Internet]. Abstract book. 2022 ;[citado 2024 maio 29 ] Available from: https://repositorio.usp.br/directbitstream/e156b1ee-7526-4d5e-8bc8-e90c2b185157/3100577.pdf
Vancouver
Martins L do A, Ferreira P, Lima C, Vasques J, Jager M, Monteiro C, Pereira H d'M, Palhano F, Kelly J, Waddington-Cruz M, Foguel D. Characterization of a novel dimeric variant of the amyloidogenic protein transthyretin involved in familial amyloidotic cardiomyopathy [Internet]. Abstract book. 2022 ;[citado 2024 maio 29 ] Available from: https://repositorio.usp.br/directbitstream/e156b1ee-7526-4d5e-8bc8-e90c2b185157/3100577.pdf
Artigo de periodico
Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity (2014)
Araujo, Thaís L. S.; Borges, Julio Cesar ; Ramos, Carlos Henrique Inacio; Meyer-Fernandes, José Roberto; Oliveira Júnior, Reinaldo S; Pascutti, Pedro Geraldo; Foguel, Debora; Palhano, Fernando L
Source: Biochemistry. Unidade: IQSC
Assunto: BIOLOGIA MOLECULAR
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ABNT
ARAUJO, Thaís L. S. et al. Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity. Biochemistry, v. 53, n. 18, p. 2884-2889, 2014Tradução . . Disponível em: https://doi.org/10.1021/bi500004q. Acesso em: 29 maio 2024.
APA
Araujo, T. L. S., Borges, J. C., Ramos, C. H. I., Meyer-Fernandes, J. R., Oliveira Júnior, R. S., Pascutti, P. G., et al. (2014). Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity. Biochemistry, 53( 18), 2884-2889. doi:10.1021/bi500004q
NLM
Araujo TLS, Borges JC, Ramos CHI, Meyer-Fernandes JR, Oliveira Júnior RS, Pascutti PG, Foguel D, Palhano FL. Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity [Internet]. Biochemistry. 2014 ; 53( 18): 2884-2889.[citado 2024 maio 29 ] Available from: https://doi.org/10.1021/bi500004q
Vancouver
Araujo TLS, Borges JC, Ramos CHI, Meyer-Fernandes JR, Oliveira Júnior RS, Pascutti PG, Foguel D, Palhano FL. Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity [Internet]. Biochemistry. 2014 ; 53( 18): 2884-2889.[citado 2024 maio 29 ] Available from: https://doi.org/10.1021/bi500004q
Artigo de periodico
Inhibition of human transthyretin aggregation by non-steroidal anti-inflammatory compounds: a structural and thermodynamic analysis (2013)
Sant'Anna, Ricardo O.; Braga, Carolina A.; Polikarpov, Igor; Ventura, Salvador; Lima, Luis Mauricio T. R.; Foguel, Debora
Source: International Journal of Molecular Sciences. Unidade: IFSC
Subjects: ANTI-INFLAMATÓRIOS NÃO ESTEROIDES, PROTEÍNAS, CRISTALOGRAFIA
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ABNT
SANT'ANNA, Ricardo O. et al. Inhibition of human transthyretin aggregation by non-steroidal anti-inflammatory compounds: a structural and thermodynamic analysis. International Journal of Molecular Sciences, v. 14, n. 3, p. 5284-5311, 2013Tradução . . Disponível em: https://doi.org/10.3390/ijms14035284. Acesso em: 29 maio 2024.
APA
Sant'Anna, R. O., Braga, C. A., Polikarpov, I., Ventura, S., Lima, L. M. T. R., & Foguel, D. (2013). Inhibition of human transthyretin aggregation by non-steroidal anti-inflammatory compounds: a structural and thermodynamic analysis. International Journal of Molecular Sciences, 14( 3), 5284-5311. doi:10.3390/ijms14035284
NLM
Sant'Anna RO, Braga CA, Polikarpov I, Ventura S, Lima LMTR, Foguel D. Inhibition of human transthyretin aggregation by non-steroidal anti-inflammatory compounds: a structural and thermodynamic analysis [Internet]. International Journal of Molecular Sciences. 2013 ; 14( 3): 5284-5311.[citado 2024 maio 29 ] Available from: https://doi.org/10.3390/ijms14035284
Vancouver
Sant'Anna RO, Braga CA, Polikarpov I, Ventura S, Lima LMTR, Foguel D. Inhibition of human transthyretin aggregation by non-steroidal anti-inflammatory compounds: a structural and thermodynamic analysis [Internet]. International Journal of Molecular Sciences. 2013 ; 14( 3): 5284-5311.[citado 2024 maio 29 ] Available from: https://doi.org/10.3390/ijms14035284
Artigo de periodico
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: 29 maio 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 maio 29 ] 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 maio 29 ] Available from: https://doi.org/10.1021/bi201365r
Artigo de periodico
The binding of synthetic triiodo L-thyronine analogs to human transthyretin: Molecular basis of cooperative and non-cooperative ligand recognition (2011)
Trivella, Daniela B. B.; Sairre, Mirela I.; Foguel, Debora; Lima, Luis Mauricio T. R.; Polikarpov, Igor
Source: Journal of Structural Biology. Unidade: IFSC
Subjects: CRISTALOGRAFIA, HORMÔNIOS TIREOIDIANOS, RECEPTORES
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ABNT
TRIVELLA, Daniela B. B. et al. The binding of synthetic triiodo L-thyronine analogs to human transthyretin: Molecular basis of cooperative and non-cooperative ligand recognition. Journal of Structural Biology, v. 173, n. 2, p. 323-332, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2010.10.003. Acesso em: 29 maio 2024.
APA
Trivella, D. B. B., Sairre, M. I., Foguel, D., Lima, L. M. T. R., & Polikarpov, I. (2011). The binding of synthetic triiodo L-thyronine analogs to human transthyretin: Molecular basis of cooperative and non-cooperative ligand recognition. Journal of Structural Biology, 173( 2), 323-332. doi:10.1016/j.jsb.2010.10.003
NLM
Trivella DBB, Sairre MI, Foguel D, Lima LMTR, Polikarpov I. The binding of synthetic triiodo L-thyronine analogs to human transthyretin: Molecular basis of cooperative and non-cooperative ligand recognition [Internet]. Journal of Structural Biology. 2011 ; 173( 2): 323-332.[citado 2024 maio 29 ] Available from: https://doi.org/10.1016/j.jsb.2010.10.003
Vancouver
Trivella DBB, Sairre MI, Foguel D, Lima LMTR, Polikarpov I. The binding of synthetic triiodo L-thyronine analogs to human transthyretin: Molecular basis of cooperative and non-cooperative ligand recognition [Internet]. Journal of Structural Biology. 2011 ; 173( 2): 323-332.[citado 2024 maio 29 ] Available from: https://doi.org/10.1016/j.jsb.2010.10.003

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