Zobrazeno 1 - 10
of 37
pro vyhledávání: '"Josué Gómez Blanco"'
Autor:
Alba Guarné, Yao Shen, Michael T. Petassi, Joaquin Ortega, Joseph E. Peters, Josué Gómez-Blanco
Publikováno v:
Nature Structural & Molecular Biology. 29:143-151
Tn7 transposable elements are unique for their highly specific, and sometimes programmable, target-site selection mechanisms and precise insertions. All the elements in the Tn7-family utilize a AAA+ adaptor (TnsC) to coordinates target-site selection
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e8564a216a4f23be3b76d1d1b0ec3ad
https://doi.org/10.1038/s41594-022-00724-8
https://doi.org/10.1038/s41594-022-00724-8
Autor:
Carlos P Mata, Daniel Luque, Josué Gómez-Blanco, Javier M Rodríguez, José M González, Nobuhiro Suzuki, Said A Ghabrial, José L Carrascosa, Benes L Trus, José R Castón
Publikováno v:
PLoS Pathogens, Vol 13, Iss 12, p e1006755 (2017)
Unlike their counterparts in bacterial and higher eukaryotic hosts, most fungal viruses are transmitted intracellularly and lack an extracellular phase. Here we determined the cryo-EM structure at 3.7 Å resolution of Rosellinia necatrix quadrivirus
Externí odkaz:
https://doaj.org/article/a684d248d6a64880960c9e1f7e29af8c
Autor:
Carmen San Martín, Roberto Marabini, Mart Krupovic, Josué Gómez-Blanco, Rosa Menéndez-Conejero, Gabriela N. Condezo
Publikováno v:
Science Advances
Science Advances, 2021, 7 (14), pp.eabe6008. ⟨10.1126/sciadv.abe6008⟩
Science Advances, American Association for the Advancement of Science (AAAS), 2021, 7 (14), pp.eabe6008. ⟨10.1126/sciadv.abe6008⟩
Biblos-e Archivo. Repositorio Institucional de la UAM
instname
Science Advances, 2021, 7 (14), pp.eabe6008. ⟨10.1126/sciadv.abe6008⟩
Science Advances, American Association for the Advancement of Science (AAAS), 2021, 7 (14), pp.eabe6008. ⟨10.1126/sciadv.abe6008⟩
Biblos-e Archivo. Repositorio Institucional de la UAM
instname
The first high-resolution structure of an adenovirus with nonmammalian host provides information on adenovirus evolution.
Of five known adenovirus genera, high-resolution structures are available only for mammalian-infecting mastadenoviruses. We
Of five known adenovirus genera, high-resolution structures are available only for mammalian-infecting mastadenoviruses. We
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6db795a1ae55948d98133ad49ba3f598
https://doi.org/10.1126/sciadv.abe6008
https://doi.org/10.1126/sciadv.abe6008
Little is known about the basic biology of non-human adenoviruses, which could be alternative vectors free of issues posed by preexisting immunity to human adenoviruses. We present the cryo-EM structure of a lizard atadenovirus, LAdV-2, at 3.4 Å res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::743a8e205eca62d7ebd814d7745ecb10
https://doi.org/10.1101/2020.07.24.220046
https://doi.org/10.1101/2020.07.24.220046
Autor:
Khanh Huy Bui, Rubén J. Sánchez-García, Jason S. McLellan, Satinder Kaur, Daniel Wrapp, Swathi Adinarayanan, Javier Vargas, Josué Gómez-Blanco, Ahmad Abdelzaher Zaki Khalifa
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Digital.CSIC. Repositorio Institucional del CSIC
Universidad Pontificia Comillas ICAI-ICADE
Nature Communications
Digital.CSIC. Repositorio Institucional del CSIC
Universidad Pontificia Comillas ICAI-ICADE
Nature Communications
Cryo-electron microscopy (cryo-EM) maps usually show heterogeneous distributions of B-factors and electron density occupancies and are typically B-factor sharpened to improve their contrast and interpretability at high-resolutions. However, ‘over-s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0333ff618bd816aabca7dce6f34da037
http://hdl.handle.net/10261/217233
http://hdl.handle.net/10261/217233
Autor:
Vikash Jha, Josué Gómez-Blanco, Joaquin Ortega, Javier Vargas, Kaustuv Basu, Dushyant Jahagirdar
Publikováno v:
RNA
It is only after recent advances in cryo-electron microscopy that is now possible to describe at high resolution structures of large macromolecules that do not crystalize. Purified 30S subunits interconvert between the “active” and “inactive”
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::288b88c89f3d715b65c2090ad6a4d2d1
https://pubmed.ncbi.nlm.nih.gov/32989043
https://pubmed.ncbi.nlm.nih.gov/32989043
Autor:
Juha T. Huiskonen, Josué Gómez-Blanco, Vijay S. Reddy, José Miguel de la Rosa-Trevín, Ilona Rissanen, Serban L. Ilca, Vahid Abrishami, José María Carazo
Publikováno v:
Progress in Biophysics and Molecular Biology
Technological advances in transmission electron microscopes and detectors have turned cryogenic electron microscopy (cryo-EM) into an essential tool for structural biology. A commonly used cryo-EM data analysis method, single particle analysis, avera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a7930f2a8551e2398c3de703a74712f
Autor:
E. Fernández-Giménez, José Luis Vilas, Javier Vargas, Gabriel Caffarena, Carlos Oscar S. Sorzano, V. Peredo-Robinson, L. del Cano, Roberto Marabini, Joaquín Otón, Remedios Melero, Josué Gómez-Blanco, Pablo Conesa, Tomáš Majtner, J. Cuenca, J.M. de la Rosa-Trevín, José María Carazo
Publikováno v:
Journal of Structural Biology. 203:90-93
The introduction of Direct Electron Detector (DED) videos in the Electron Microscope field has boosted Single Particle Analysis to a point in which it is currently considered to be a key technique in Structural Biology. In this article we introduce a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07c7afb3ce6192641d2b366dff9a77ea
https://doi.org/10.1016/j.jsb.2018.03.007
https://doi.org/10.1016/j.jsb.2018.03.007
Publikováno v:
Journal of structural biology. 208(3)
Structural information from macromolecules provides key insights into the way complexes perform their biological functions. The reconstruction process leading to the final three-dimensional (3D) map is iterative and requires an initial volume to prim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da35eb473bb9522d7870379e36b2bdbc
https://pubmed.ncbi.nlm.nih.gov/31568828
https://pubmed.ncbi.nlm.nih.gov/31568828
Autor:
Javier Vargas, Nikhil Jain, Alba Guarné, James R. Williamson, Kaustuv Basu, Dushyant Jahagirdar, Robert A. Britton, Joseph H. Davis, Brett Thurlow, Aida Razi, Yumeng Hao, Sarah A. Woodson, Joaquin Ortega, Josué Gómez-Blanco
SUMMARYTo reveal the role of the essential protein Era in the assembly of the 30S ribosomal subunit, we analyzed assembly intermediates that accumulated in Era-depletedEscherichia colicells using quantitative mass spectrometry, cryo-electron microsco
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::83ba7fc32eb2236ed23e827d30d8c29d
https://doi.org/10.1101/525360
https://doi.org/10.1101/525360