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pro vyhledávání: '"Melek Cemre Manav"'
Publikováno v:
Protein Science. 26:1474-1492
The PIN (PilT N-terminus) domain is a compact RNA-binding protein domain present in all domains of life. This 120-residue domain consists of a central and parallel β sheet surrounded by α helices, which together organize 4-5 acidic residues in an a
Autor:
Melek Cemre Manav, Dukas Jurėnas, Kenn Gerdes, Kathryn Jane Turnbull, Abel Garcia-Pino, Ditlev E. Brodersen
Publikováno v:
Structure 27(11), 1675-1685.e3 (2019). doi:10.1016/j.str.2019.08.008
Manav, M C, Turnbull, K J, Jurėnas, D, Garcia-Pino, A, Gerdes, K & Brodersen, D E 2019, ' The E. coli HicB Antitoxin Contains a Structurally Stable Helix-Turn-Helix DNA Binding Domain ', Structure, vol. 27, no. 11, pp. 1675-1685, e1-e3 . https://doi.org/10.1016/j.str.2019.08.008
Structure, 27 (11
Manav, C, Turnbull, K J, Jurėnas, D, Garcia-Pino, A, Gerdes, K & Brodersen, D E 2019, ' The E. coli HicB Antitoxin Contains a Structurally Stable Helix-Turn-Helix DNA Binding Domain ', Structure, vol. 27, no. 11, pp. 1675-1685.e3 . https://doi.org/10.1016/j.str.2019.08.008
Manav, M C, Turnbull, K J, Jurėnas, D, Garcia-Pino, A, Gerdes, K & Brodersen, D E 2019, ' The E. coli HicB Antitoxin Contains a Structurally Stable Helix-Turn-Helix DNA Binding Domain ', Structure, vol. 27, no. 11, pp. 1675-1685, e1-e3 . https://doi.org/10.1016/j.str.2019.08.008
Structure, 27 (11
Manav, C, Turnbull, K J, Jurėnas, D, Garcia-Pino, A, Gerdes, K & Brodersen, D E 2019, ' The E. coli HicB Antitoxin Contains a Structurally Stable Helix-Turn-Helix DNA Binding Domain ', Structure, vol. 27, no. 11, pp. 1675-1685.e3 . https://doi.org/10.1016/j.str.2019.08.008
Structure 27(11), 1675-1685.e3 (2019). doi:10.1016/j.str.2019.08.008
The E. coli hicAB type II toxin-antitoxin locus is unusual by being controlled by two promoters and by having the toxin encoded upstream of the antitoxin. HicA toxins contain a
The E. coli hicAB type II toxin-antitoxin locus is unusual by being controlled by two promoters and by having the toxin encoded upstream of the antitoxin. HicA toxins contain a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d9f9ff6247e21de85088e09307905be
https://bib-pubdb1.desy.de/record/425977
https://bib-pubdb1.desy.de/record/425977
Autor:
Martin Saxtorph Bojer, Melek Cemre Manav, Jelena Beljantseva, Vasili Hauryliuk, Tanel Tenson, Hanne Ingmer, Ditlev E. Brodersen
Publikováno v:
Journal of Biological Chemistry
Manav, M C, Beljantseva, J, Bojer, M S, Tenson, T, Ingmer, H, Hauryliuk, V & Brodersen, D E 2018, ' Structural basis for (p)ppGpp synthesis by the Staphylococcus aureus small alarmone synthetase RelP ', Journal of Biological Chemistry, vol. 293, no. 9, pp. 3254-3264 . https://doi.org/10.1074/jbc.RA117.001374
The journal of biological chemistry 293(9), 3254-3264 (2018). doi:10.1074/jbc.RA117.001374
Manav, M C, Beljantseva, J, Bojer, M S, Tenson, T, Ingmer, H, Hauryliuk, V & Brodersen, D E 2018, ' Structural basis for (p)ppGpp synthesis by the Staphylococcus aureus small alarmone synthetase RelP ', Journal of Biological Chemistry, vol. 293, no. 9, pp. 3254-3264 . https://doi.org/10.1074/jbc.RA117.001374
The journal of biological chemistry 293(9), 3254-3264 (2018). doi:10.1074/jbc.RA117.001374
The stringent response is a global reprogramming of bacterial physiology that renders cells more tolerant to antibiotics and induces virulence gene expression in pathogens in response to stress. This process is driven by accumulation of the intracell