Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Agustín Ormazábal"'
Autor:
Agustín Ormazábal, Matías Sebastián Carletti, Tadeo Enrique Saldaño, Martín Gonzalez Buitron, Julia Marchetti, Nicolas Palopoli, Alex Bateman
Publikováno v:
PLoS ONE, Vol 18, Iss 9, p e0290890 (2023)
Protein regions consisting of arrays of tandem repeats are known to bind other molecular partners, including nucleic acid molecules. Although the interactions between repeat proteins and DNA are already widely explored, studies characterising tandem
Externí odkaz:
https://doaj.org/article/180d40a969e948da946ddf3eefafa688
Publikováno v:
Journal of Chemical Information and Modeling. 62:6614-6627
CsrA/RsmE is a post-transcriptional regulator protein widely distributed in bacteria. It impedes the expression of target mRNAs by attaching their 5' untranslated region. The translation is restored by small, noncoding RNAs that sequester CsrA/RsmE a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::434d5d58e84a70d79a965bb1048dc335
https://doi.org/10.1021/acs.jcim.2c00037
https://doi.org/10.1021/acs.jcim.2c00037
Autor:
Agustín Ormazábal, Matías Sebastián Carletti, Tadeo Enrique Saldaño, Martín Gonzalez-Buitron, Julia Marchetti, Nicolas Palopoli, Alex Bateman
Protein regions consisting of arrays of tandem repeats are known to bind other molecular partners, including nucleic acid molecules. Although the interactions between repeat proteins and DNA are already widely explored, studies characterising tandem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3b8043d9f388d7ca5abe7c5ff6f7ae35
https://doi.org/10.1101/2022.09.12.507642
https://doi.org/10.1101/2022.09.12.507642
Publikováno v:
The Journal of Physical Chemistry B. 125:3045-3056
CsrA/RsmE are dimeric proteins that bind to targeted mRNAs repressing translation. This mechanism modulates several metabolic pathways and allows bacteria to efficiently adjust their responses to environmental changes. In turn, small RNAs (sRNA) such
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19c2dc69eecad794fd9e2742017b793e
https://doi.org/10.1021/acs.jpcb.0c09770
https://doi.org/10.1021/acs.jpcb.0c09770
Publikováno v:
Journal of Chemical Information and Modeling. 60:923-932
P2X receptors are a family of trimeric cationic channels located in the membrane of mammalian cells. They open in response to the binding of ATP. The differences between the closed and open structures have been described in detail for some members of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c913d13e78b7caf361037214d80766dc
https://doi.org/10.1021/acs.jcim.9b00856
https://doi.org/10.1021/acs.jcim.9b00856
Publikováno v:
The journal of physical chemistry. B. 123(5)
P2X receptors are a group of trimeric cationic channels that are activated by adenosine 5'-triphosphate. They perform critical roles in the membranes of mammalian cells, and their improper functioning is associated with numerous diseases. Despite the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b3ae903dcd657b9975b9cf0a376403f1
https://pubmed.ncbi.nlm.nih.gov/30624928
https://pubmed.ncbi.nlm.nih.gov/30624928