Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Fabio C.L. Almeida"'
Publikováno v:
Journal of Magnetic Resonance Open, Vol 16, Iss , Pp 100106- (2023)
Plant defensins (PDs) display a CSαβ-fold that lacks a canonical hydrophobic core. They display almost all hydrophobic residues on the protein surface. The exposed hydrophobic residues form surface clusters stabilized by the vicinity of hydrophilic
Externí odkaz:
https://doaj.org/article/3ce7447ff5d9484a96ee2a693689fb00
Autor:
Thais C. Neves-Martins, Nathane C. Mebus-Antunes, Carlos H.G. Neto, Glauce M. Barbosa, Fabio C.L. Almeida, Icaro P. Caruso, Andrea T. Da Poian
Publikováno v:
iScience, Vol 26, Iss 3, Pp 106197- (2023)
Summary: Nucleocapsid (NC) assembly is an essential step of the virus replication cycle. It ensures genome protection and transmission among hosts. Flaviviruses are human viruses for which envelope structure is well known, whereas no information on N
Externí odkaz:
https://doaj.org/article/308c5dd8cc91422d955ed3d55a7cf83e
Autor:
Lorena O. Fernandes-Siqueira, Bruna G. Sousa, Carlos E. Cleto, Luciana S. Wermelinger, Beatriz L.L. Caetano, Agatha R. Pacheco, Simone M. Costa, Fabio C.L. Almeida, Gustavo C. Ferreira, Didier Salmon, Ada M.B. Alves, Andrea T. Da Poian
Publikováno v:
Journal of Clinical Virology Plus, Vol 2, Iss 4, Pp 100121- (2022)
Background: Vaccination against COVID-19 was implemented very quickly, but the emergence of new variants that can evade the previous acquired immunological protection highlights the importance of understanding the mechanisms involved in the immune re
Externí odkaz:
https://doaj.org/article/b9920b9f634a4c629aa5cd026992bb9d
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 19, Iss , Pp 6255-6262 (2021)
Defensins are small proteins, usually ranging from 3 to 6 kDa, amphipathic, disulfide-rich, and with a small or even absent hydrophobic core. Since a hydrophobic core is generally found in globular proteins that fold in an aqueous solvent, the peculi
Externí odkaz:
https://doaj.org/article/364db1b553094418b55135f39f28ed16
Autor:
Icaro Putinhon Caruso, Vitor dos Santos Almeida, Mariana Juliani do Amaral, Guilherme Caldas de Andrade, Gabriela Rocha de Araújo, Talita Stelling de Araújo, Jéssica Moreira de Azevedo, Glauce Moreno Barbosa, Leonardo Bartkevihi, Peter Reis Bezerra, Katia Maria dos Santos Cabral, Isabella Otênio de Lourenço, Clara L.F. Malizia-Motta, Aline de Luna Marques, Nathane Cunha Mebus-Antunes, Thais Cristtina Neves-Martins, Jéssica Maróstica de Sá, Karoline Sanches, Marcos Caique Santana-Silva, Ariana Azevedo Vasconcelos, Marcius da Silva Almeida, Gisele Cardoso de Amorim, Cristiane Dinis Anobom, Andrea T. Da Poian, Francisco Gomes-Neto, Anderson S. Pinheiro, Fabio C.L. Almeida
Publikováno v:
International Journal of Biological Macromolecules
Scopus
Repositório Institucional da UNESP
Universidade Estadual Paulista (UNESP)
instacron:UNESP
Scopus
Repositório Institucional da UNESP
Universidade Estadual Paulista (UNESP)
instacron:UNESP
Made available in DSpace on 2022-04-28T19:50:20Z (GMT). No. of bitstreams: 0 Previous issue date: 2022-04-01 Fundação de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ) Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9da129dd3672638f549062cfbab7f04d
https://pubmed.ncbi.nlm.nih.gov/35077748
https://pubmed.ncbi.nlm.nih.gov/35077748
Publikováno v:
Genetics and Molecular Biology, Vol 29, Iss 4, Pp 762-770 (2006)
With the advent of structural genomics, the need for fast structural information about unknown proteins has increased. We describe a new methodology, based on 13C, 15N and ¹H chemical shift dispersion to predict the amount of secondary structure of
Externí odkaz:
https://doaj.org/article/a15f8e9b6c06434f94343926f1fb6809