Zobrazeno 1 - 10
of 59
pro vyhledávání: '"Sonia Huecas"'
Autor:
Phong Quoc Nguyen, Sonia Huecas, Amna Asif-Laidin, Adrián Plaza-Pegueroles, Beatrice Capuzzi, Noé Palmic, Christine Conesa, Joël Acker, Juan Reguera, Pascale Lesage, Carlos Fernández-Tornero
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-13 (2023)
Cryo-EM structures of Ty1 integrase-Pol III complexes reveal determinants of Ty1 targeting upstream of Pol III-transcribed genes, and a functional impact of the integrase on Pol III activity that may increase the probability of Ty1 integration.
Externí odkaz:
https://doaj.org/article/ae5e1040373b42eb93f7571525af5479
Autor:
Federico M. Ruiz, Sonia Huecas, Alicia Santos-Aledo, Elena A. Prim, José M. Andreu, Carlos Fernández-Tornero
Publikováno v:
PLoS Biology, Vol 20, Iss 3 (2022)
Treadmilling protein filaments perform essential cellular functions by growing from one end while shrinking from the other, driven by nucleotide hydrolysis. Bacterial cell division relies on the primitive tubulin homolog FtsZ, a target for antibiotic
Externí odkaz:
https://doaj.org/article/e0ab14b027274bd5a31576d5b6b10c5c
Publikováno v:
Biomedicines, Vol 10, Iss 8, p 1825 (2022)
The global spread of bacterial antimicrobial resistance is associated to millions of deaths from bacterial infections per year, many of which were previously treatable. This, combined with slow antibiotic deployment, has created an urgent need for de
Externí odkaz:
https://doaj.org/article/6c4741ba230e405dbf6823e950c7041a
Autor:
Federico M. Ruiz, Andrea Escobar-Peña, María L. López-Rodríguez, José Manuel Andreu, Mar Martín-Fontecha, Sonia Huecas, Marta Artola, Henar Vázquez-Villa, Laura B. Ruiz-Avila, Lidia Araújo-Bazán, R Fernando Martínez, Carlos Fernández-Tornero
Publikováno v:
Journal of Medicinal Chemistry
E-Prints Complutense. Archivo Institucional de la UCM
instname
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
Digital.CSIC. Repositorio Institucional del CSIC
E-Prints Complutense. Archivo Institucional de la UCM
instname
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
Digital.CSIC. Repositorio Institucional del CSIC
51 p.-6 fig.-1 tab.-4 schem.-1 graph. abst.
Bacterial resistance to antibiotics makes previously manageable infections again disabling and lethal, highlighting the need for new antibacterial strategies. In this regard, inhibition of the bacteria
Bacterial resistance to antibiotics makes previously manageable infections again disabling and lethal, highlighting the need for new antibacterial strategies. In this regard, inhibition of the bacteria
Autor:
Phong Quoc Nguyen, Sonia Huecas, Amna Asif-Laidin, Adrián Plaza-Pegueroles, Noé Palmic, Joël Acker, Juan Reguera, Pascale Lesage, Carlos Fernández-Tornero
SummaryThe yeast Ty1 retrotransposon integrates upstream of genes transcribed by RNA polymerase III (Pol III). Specificity of integration is mediated by an interaction between the Ty1 integrase (IN1) and Pol III, currently uncharacterized at the atom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7497fda6a62427370447da274cd2e646
https://doi.org/10.1101/2022.03.07.483246
https://doi.org/10.1101/2022.03.07.483246
Publikováno v:
Frontiers in Microbiology, Vol 7 (2016)
Cell division protein FtsZ is the organizer of the cytokinetic ring in almost all bacteria and a target for the discovery of new antibacterial agents that are needed to counter widespread antibiotic resistance. Bacterial cytological profiling, using
Externí odkaz:
https://doaj.org/article/18a9a56db6f6485888947145383f872a
Autor:
Sonia Huecas, Federico M. Ruiz, José Manuel Andreu, Elena A. Prim, Alicia Santos-Aledo, Carlos Fernández-Tornero
Treadmilling protein filaments perform essential cellular functions by growing from one end while shrinking from the other, driven by nucleotide hydrolysis. Bacterial cell division relies on the primitive tubulin homolog FtsZ, a target for antibiotic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::be3f7a38b4d8779879194244f8e0ecc2
https://doi.org/10.1101/2021.11.29.470395
https://doi.org/10.1101/2021.11.29.470395
Autor:
Federico M. Ruiz, Alejandro J. Canosa-Valls, Carlos Fernández-Tornero, Lidia Araújo-Bazán, Sonia Huecas, Douglas V. Laurents, José Manuel Andreu
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
48 p.-6 fig.-1 tab.-9 fig-supl.-3 tab.supl.
The essential bacterial division protein FtsZ uses GTP binding and hydrolysis to assemble into dynamic filaments that treadmill around the Z-ring, guiding septal wall synthesis and cell division. FtsZ
The essential bacterial division protein FtsZ uses GTP binding and hydrolysis to assemble into dynamic filaments that treadmill around the Z-ring, guiding septal wall synthesis and cell division. FtsZ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a614d7ba0227ddc715729cd0d67a998
http://hdl.handle.net/10261/200180
http://hdl.handle.net/10261/200180
Autor:
Carlos Fernández-Tornero, Rocío González-Corrochano, Srdja Drakulic, Nicholas M.I. Taylor, Sonia Huecas, Mercedes Spínola-Amilibia, Federico M. Ruiz
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
'Nucleic Acids Research ', vol: 48, pages: 9943-9958 (2020)
Nucleic Acids Research
instname
'Nucleic Acids Research ', vol: 48, pages: 9943-9958 (2020)
Nucleic Acids Research
16 p.-7 fig.-1 tab.
Nucleotide excision repair (NER) is an essential pathway to remove bulky lesions affecting one strand of DNA. Defects in components of this repair system are at the ground of genetic diseases such as xeroderma pigmentosum (XP
Nucleotide excision repair (NER) is an essential pathway to remove bulky lesions affecting one strand of DNA. Defects in components of this repair system are at the ground of genetic diseases such as xeroderma pigmentosum (XP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::318ad8c5db8b212aff09badee0a2db93
http://hdl.handle.net/10261/218655
http://hdl.handle.net/10261/218655
Autor:
Erney Ramírez-Aportela, Sonia Huecas, J. Fernando Díaz, Patricia Castellen, David Juan-Rodríguez, Oscar Llorca, Rafael Núñez-Ramírez, José Manuel Andreu, María A. Oliva, Albert Vergoñós
Publikováno v:
Biophysical Journal. 113:1831-1844
32 p.-6 fig.+ 26 p. mat.supl.
FtsZ is a self-assembling GTPase that forms, below the inner membrane, the mid-cell Z-ring guiding bacterial division. FtsZ monomers polymerize head to tail forming tubulin-like dynamic protofilaments, whose organiz
FtsZ is a self-assembling GTPase that forms, below the inner membrane, the mid-cell Z-ring guiding bacterial division. FtsZ monomers polymerize head to tail forming tubulin-like dynamic protofilaments, whose organiz