Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Mariia Khamina"'
Publikováno v:
Canadian Journal of Chemistry. 100:649-659
Kinases include a wide variety of valuable drug targets, but full therapeutic exploitation requires a high degree of selectivity. A promising avenue to engineer the desired kinase selectivity relies on allosteric sites. Here, we provide a focused min
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::12549083158eea3ee2814a8e2291dfde
https://doi.org/10.1139/cjc-2021-0359
https://doi.org/10.1139/cjc-2021-0359
Publikováno v:
Journal of molecular biology. 434(17)
The cAMP- and cGMP-dependent protein kinases (PKA and PKG) are canonically activated by the corresponding cyclic nucleotides. However, both systems are also sensitive to a wide range of non-canonical allosteric effectors, such as reactive oxygen spec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb01837282d32194d03eac3eb39e4ed9
https://pubmed.ncbi.nlm.nih.gov/35427632
https://pubmed.ncbi.nlm.nih.gov/35427632
Autor:
Madoka Akimoto, Karla Martinez Pomier, Bryan VanSchouwen, Jung Ah Byun, Mariia Khamina, Giuseppe Melacini
Publikováno v:
The Biochemical journal. 479(7)
Allosteric pluripotency arises when the functional response of an allosteric receptor to an allosteric stimulus depends on additional allosteric modulators. Here, we discuss allosteric pluripotency as observed in the prototypical Protein Kinase A (PK
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35abc85ad8ac57723219dfea5b2ae1e1
https://pubmed.ncbi.nlm.nih.gov/35403669
https://pubmed.ncbi.nlm.nih.gov/35403669