Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Gabriela Garcia Rodriguez"'
Autor:
Charlotte Vanmarsenille, Jelle Elseviers, Charlotte Yvanoff, Gholamreza Hassanzadeh-Ghassabeh, Gabriela Garcia Rodriguez, Edo Martens, Ann Depicker, An Martel, Freddy Haesebrouck, Frank Pasmans, Jean-Pierre Hernalsteens, Henri De Greve
Publikováno v:
PLoS ONE, Vol 13, Iss 9, p e0204222 (2018)
Campylobacteriosis is a widespread infectious disease, leading to a major health and economic burden. Chickens are considered as the most common infection source for humans. Campylobacter mainly multiplies in the mucus layer of their caeca. No effect
Externí odkaz:
https://doaj.org/article/a6d41a5650e74a7e92787ba0005d4e71
Publikováno v:
'Nucleic Acids Research ', vol: 49, pages: 7164-7178 (2021)
Nucleic Acids Research
Nucleic Acids Research
The rnlAB toxin-antitoxin operon from Escherichia coli functions as an anti-phage defense system. RnlA was recently identified as a member of the HEPN (Higher Eukaryotes and Prokaryotes Nucleotide-binding domain) superfamily of ribonucleases. The act
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d735896f710d22bf2017fc21449e277c
https://lirias.kuleuven.be/handle/123456789/676609
https://lirias.kuleuven.be/handle/123456789/676609
Autor:
Frank Sobott, Alexander N. Volkov, Albert Konijnenberg, Girardin Y, Ranjan Kumar Singh, Daniel Charlier, Gabriela Garcia-Rodriguez, Remy Loris
The parDE2 operon of Vibrio cholerae encodes a type II TA system, which is one of three loci in the superintegron of small chromosome II that show modest similarity to the parDE operon of plasmid RK2. ParE2, like plasmid RK2-encoded ParE, inhibits DN
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aa03310e3789b2655b85665765b9fcb7
https://doi.org/10.1101/2021.03.22.436508
https://doi.org/10.1101/2021.03.22.436508
Autor:
Wim Versées, Ranjan Kumar Singh, Gopinath Muruganandam, Yana Girardin, Jeroen Van Dyck, Frank Sobott, Daniel Charlier, Remy Loris, Oleksandr Volkov, Gabriela Garcia Rodriguez
ParD2 is the antitoxin component of the parDE2 toxin-antitoxin module from Vibrio cholerae and consists of an ordered DNA binding domain followed by an intrinsically disordered ParE-neutralizing domain. In absence of the C-terminal IDP domain, VcParD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f8f038b81691eed0d2f9453d11fb5387
https://doi.org/10.1101/2021.03.09.434581
https://doi.org/10.1101/2021.03.09.434581
Autor:
Yana Girardin, Wim Versées, Frank Sobott, Alexander N. Volkov, Jeroen Van Dyck, Remy Loris, Ranjan Kumar Singh, Gabriela Garcia-Rodriguez, Gopinath Muruganandam, Daniel Charlier
Publikováno v:
Acta Crystallographica. Section D, Structural Biology
Acta crystallographica. Section D, Structural biology
Acta crystallographica. Section D, Structural biology
ParD2 forms an open oligomer in solution, the size of which is limited by the presence of an intrinsically disordered tail. In the absence of this tail, ParD2 forms a circular hexadecamer.
ParD2 is the antitoxin component of the parDE2 toxin–a
ParD2 is the antitoxin component of the parDE2 toxin–a
Autor:
Albert Konijnenberg, Jan Michiels, Ariel Talavera Perez, Remy Loris, Frank Sobott, Gabriela Garcia-Rodriguez
Publikováno v:
Acta Crystallogr F Struct Biol Commun
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
The Escherichia coli rnlAB operon encodes a toxin–antitoxin module that is involved in protection against infection by bacteriophage T4. The full-length RnlA–RnlB toxin–antitoxin complex as well as the toxin RnlA were purified to homogeneity an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4ea19060ec7fd53c379fa5e39cee3af
https://doi.org/10.1107/s2053230x19017175
https://doi.org/10.1107/s2053230x19017175
Autor:
Gabriela Garcia-Rodriguez
Publikováno v:
Vrije Universiteit Brussel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::6fcb1968abd14e6e461a156ada549b0e
https://researchportal.vub.be/en/publications/0edd84d1-36ca-41ce-99fe-09df1ef2e145
https://researchportal.vub.be/en/publications/0edd84d1-36ca-41ce-99fe-09df1ef2e145