Zobrazeno 1 - 10
of 58
pro vyhledávání: '"David A. Dougan"'
Publikováno v:
Frontiers in Molecular Biosciences, Vol 10 (2023)
Externí odkaz:
https://doaj.org/article/34916ee468624348926a480d8f1c96e2
Autor:
Dimce Micevski, Kornelius Zeth, Terrence D. Mulhern, Verena J. Schuenemann, Jessica E. Zammit, Kaye N. Truscott, David A. Dougan
Publikováno v:
Biomolecules, Vol 10, Iss 4, p 615 (2020)
In Escherichia coli, SigmaS (σS) is the master regulator of the general stress response. The cellular levels of σS are controlled by transcription, translation and protein stability. The turnover of σS, by the AAA+ protease (ClpXP), is tightly reg
Externí odkaz:
https://doaj.org/article/3061c2710e154054b61b81872d5ac77c
Publikováno v:
Frontiers in Molecular Biosciences, Vol 4 (2017)
The bacterial cytosol is a complex mixture of macromolecules (proteins, DNA, and RNA), which collectively are responsible for an enormous array of cellular tasks. Proteins are central to most, if not all, of these tasks and as such their maintenance
Externí odkaz:
https://doaj.org/article/c13cdeba3cd04446acfd00e4905231c4
Publikováno v:
The FEBS Journal. 288:95-98
Protein degradation plays a vital role in the correct maintenance of a cell, not only under normal physiological conditions but also in response to stress. In the human pathogen Mtb, this crucial cellular task is performed by several ATPase associate
The N-degron pathways are a set of proteolytic systems that relate the half-life of a protein to its N-terminal (Nt) residue. In Escherchia coli the principal N-degron pathway is known as the Leu/N-degron pathway of which an Nt Leu is a key feature o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::907179ad5add1bbf756f6bcece21a0d4
https://doi.org/10.1101/2021.07.26.453911
https://doi.org/10.1101/2021.07.26.453911
Publikováno v:
FEBS Letters. 593:962-970
The prokaryotic N-degron pathway depends on the Clp chaperone-protease system and the ClpS adaptor for recognition of N-degron bearing substrates. Plant chloroplasts contain a diversified Clp protease, including the ClpS homolog ClpS1. Several candid
Autor:
Pierre Genevaux, Anne-Marie Cirinesi, Patricia Bordes, Ambre Sala, Jyotsna Nagpal, Pauline Texier, David A. Dougan, Xibing Xu, Moise Mansour
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, 2021, 433 (5), pp.166815. ⟨10.1016/j.jmb.2021.166815⟩
Journal of Molecular Biology, Elsevier, 2021, 433 (5), pp.166815. ⟨10.1016/j.jmb.2021.166815⟩
Journal of Molecular Biology, 2021, 433 (5), pp.166815. ⟨10.1016/j.jmb.2021.166815⟩
Journal of Molecular Biology, Elsevier, 2021, 433 (5), pp.166815. ⟨10.1016/j.jmb.2021.166815⟩
Bacterial toxin-antitoxin (TA) systems are composed of a deleterious toxin and its antagonistic antitoxin. They are widespread in bacterial genomes and mobile genetic elements, and their functions remain largely unknown. Some TA systems, known as TAC
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7cd5d4bb07516fcd5ce1ae4e083b241
https://hal.science/hal-03364320
https://hal.science/hal-03364320
Autor:
David A. Dougan, Liz J. Valente, Hanmiao Zhan, Kornelius Zeth, Lauren M. Angley, Kaye N. Truscott, Erica J. Brodie, Matthew A. Perugini, Tamanna Saiyed, Philip R. Strack, Verena J. Schuenemann, Bradley R. Lowth
Publikováno v:
Communications Biology
Communications Biology, Vol 3, Iss 1, Pp 1-12 (2020)
Communications Biology, Vol 3, Iss 1, Pp 1-12 (2020)
Over a decade ago Polymerase δ interacting protein of 38 kDa (PDIP38) was proposed to play a role in DNA repair. Since this time, both the physiological function and subcellular location of PDIP38 has remained ambiguous and our present understanding
Autor:
Verena J. Schuenemann, David A. Dougan, Kornelius Zeth, Tamanna Saiyed, Philip R. Strack, Liz J. Valente, Hanmiao Zhan, Erica J. Brodie, Kaye N. Truscott
SummaryPolymerase δ interacting protein of 38 kDa (PDIP38) was originally identified in a yeast two hybrid screen as an interacting protein of DNA polymerase delta, more than a decade ago. Since this time several subcellular locations have been repo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4228cad8977aec24b11fed9bfb44b7af
https://doi.org/10.1101/2020.05.19.105320
https://doi.org/10.1101/2020.05.19.105320