Sorghum bicolor SbHSP110 has an elongated shape and is able of protecting against aggregation and replacing human HSPH1/HSP110 in refolding and disaggregation assays (2023)
- Authors:
- Autor USP: BARBOSA, LEANDRO RAMOS SOUZA - IF
- Unidade: IF
- DOI: 10.1002/bip.23532
- Subjects: BIOFÍSICA; BIOPOLÍMEROS; PROTEÍNAS; BIOLOGIA MOLECULAR
- Keywords: HSP70 heat shock protein; molecular chaperones; protein aggregates; protein disaggregation; HSP110
- Agências de fomento:
- Language: Inglês
- Imprenta:
- Publisher place: New Jersey
- Date published: 2023
- Source:
- Título: Biopolymers
- ISSN: 1097-0282
- Volume/Número/Paginação/Ano: v. 114, n. 2, fevereiro de 2023, número do artigo: e23532, online
- Este periódico é de assinatura
- Este artigo é de acesso aberto
- URL de acesso aberto
- Cor do Acesso Aberto: bronze
-
ABNT
FRANCO, Juliana C. e BARBOSA, Leandro Ramos Souza. Sorghum bicolor SbHSP110 has an elongated shape and is able of protecting against aggregation and replacing human HSPH1/HSP110 in refolding and disaggregation assays. Biopolymers, v. 114, n. 2, 2023Tradução . . Disponível em: https://doi.org/10.1002/bip.23532. Acesso em: 28 dez. 2025. -
APA
Franco, J. C., & Barbosa, L. R. S. (2023). Sorghum bicolor SbHSP110 has an elongated shape and is able of protecting against aggregation and replacing human HSPH1/HSP110 in refolding and disaggregation assays. Biopolymers, 114( 2). doi:10.1002/bip.23532 -
NLM
Franco JC, Barbosa LRS. Sorghum bicolor SbHSP110 has an elongated shape and is able of protecting against aggregation and replacing human HSPH1/HSP110 in refolding and disaggregation assays [Internet]. Biopolymers. 2023 ; 114( 2):[citado 2025 dez. 28 ] Available from: https://doi.org/10.1002/bip.23532 -
Vancouver
Franco JC, Barbosa LRS. Sorghum bicolor SbHSP110 has an elongated shape and is able of protecting against aggregation and replacing human HSPH1/HSP110 in refolding and disaggregation assays [Internet]. Biopolymers. 2023 ; 114( 2):[citado 2025 dez. 28 ] Available from: https://doi.org/10.1002/bip.23532 - Urea, guanidine hydrocloride and 2,2,2-trifluoroethanol can change the amyloid fibril formation of model proteins: a spectroscopic study
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Informações sobre o DOI: 10.1002/bip.23532 (Fonte: oaDOI API)
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