Zobrazeno 1 - 10
of 516
pro vyhledávání: '"beta-helix"'
Autor:
Rebecca L Newcomer, Jason R Schrad, Eddie B Gilcrease, Sherwood R Casjens, Michael Feig, Carolyn M Teschke, Andrei T Alexandrescu, Kristin N Parent
Publikováno v:
eLife, Vol 8 (2019)
The major coat proteins of dsDNA tailed phages (order Caudovirales) and herpesviruses form capsids by a mechanism that includes active packaging of the dsDNA genome into a precursor procapsid, followed by expansion and stabilization of the capsid. Th
Externí odkaz:
https://doaj.org/article/a94a86477c72462ea6b6085239e80eb8
Akademický článek
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Akademický článek
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Autor:
Javier Ellena, Richard F. D'Vries, Elizabeth Castro-Giraldo, Camila A. García-Carreño, Camila Cardona-Restrepo, Oscar E. Rojas-Alvarez
Publikováno v:
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Universidade de São Paulo (USP)
instacron:USP
La estructura cristalina del compuesto ácido 2-E-((4-hidroxifenil) diazenil) benzóico se resolvió por medio del método de fase intrínseca usando datos de difracción de rayos X de monocristal, encontrando que la molécula cristaliza en el sistem
Publikováno v:
International Journal of Biological Sciences
Myelin gene regulatory factor (MyRF), a novel membrane transcription factor expressed on the endoplasmic reticulum membrane, functions as a trimer. The trimerization of MyRF is associated with a fragment between the DNA binding domain and transmembra
Akademický článek
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Publikováno v:
Pantier, R, Mullin, N P, Hall-Ponsele, E & Chambers, I 2020, ' TET1 interacts directly with NANOG via independent domains containing hydrophobic and aromatic residues ', Journal of Molecular Biology, vol. 432, no. 23, pp. 6075-6091 . https://doi.org/10.1016/j.jmb.2020.10.008
Journal of Molecular Biology
Journal of Molecular Biology
Graphical abstract
Highlights • TET1 and NANOG interact via multiple independent binding regions. • TET1 and NANOG interactions are mediated by aromatic and hydrophobic residues. • TET1 residues that bind NANOG are highly conserved in mamm
Highlights • TET1 and NANOG interact via multiple independent binding regions. • TET1 and NANOG interactions are mediated by aromatic and hydrophobic residues. • TET1 residues that bind NANOG are highly conserved in mamm
Publikováno v:
PLoS ONE, Vol 15, Iss 12, p e0244315 (2020)
Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA-Alice)
Empresa Brasileira de Pesquisa Agropecuária (Embrapa)
instacron:EMBRAPA
PLoS ONE
Scopus
Repositório Institucional da UNESP
Universidade Estadual Paulista (UNESP)
instacron:UNESP
Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA-Alice)
Empresa Brasileira de Pesquisa Agropecuária (Embrapa)
instacron:EMBRAPA
PLoS ONE
Scopus
Repositório Institucional da UNESP
Universidade Estadual Paulista (UNESP)
instacron:UNESP
Made available in DSpace on 2021-06-25T10:48:39Z (GMT). No. of bitstreams: 0 Previous issue date: 2020-12-01 Secondary structure elements are generally found in almost all protein structures revealed so far. In general, there are more β-sheets than
Autor:
Broto Chakrabarty, Nita Parekh
Publikováno v:
Protein Sci
Recent interest in repeat proteins has arisen due to stable structural folds, high evolutionary conservation and repertoire of functions provided by these proteins. However, repeat proteins are poorly characterized because of high sequence variation
Pantoea stewartii WceF is a glycan biofilm modifying enzyme with a bacteriophage tailspike-like fold
Publikováno v:
Journal of Biological Chemistry
The Journal of Biological Chemistry
The Journal of Biological Chemistry
Pathogenic microorganisms often reside in glycan-based biofilms. Concentration and chain length distribution of these mostly anionic exopolysaccharides (EPS) determine the overall biophysical properties of a biofilm and result in a highly viscous env
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cfde56bf2a51c79505dc179be351ce54
https://hdl.handle.net/21.11116/0000-0007-FE66-921.11116/0000-0007-D517-F
https://hdl.handle.net/21.11116/0000-0007-FE66-921.11116/0000-0007-D517-F