Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Kenrick A. Waite"'
Autor:
Kenrick A Waite, Jeroen Roelofs
Publikováno v:
Autophagy Reports, Vol 1, Iss 1, Pp 21-24 (2022)
Externí odkaz:
https://doaj.org/article/59bbadec34d94b439d937b66234718e3
Autor:
Kenrick A. Waite, Jeroen Roelofs
Publikováno v:
The FASEB Journal. 36
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8cd8979a88592db14e17854334d23313
https://doi.org/10.1096/fasebj.2022.36.s1.r4796
https://doi.org/10.1096/fasebj.2022.36.s1.r4796
Publikováno v:
The FASEB Journal. 36
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ba9c9d3f2a077ad160672fe82f2f575c
https://doi.org/10.1096/fasebj.2022.36.s1.r6279
https://doi.org/10.1096/fasebj.2022.36.s1.r6279
Autor:
Kenrick A. Waite, Jeroen Roelofs
Publikováno v:
Journal of cell science. 135(17)
In the yeast Saccharomyces cerevisiae, proteasomes are enriched in cell nuclei, in which they execute important cellular functions. Nutrient stress can change this localization, indicating that proteasomes respond to the metabolic state of the cell.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4deb4fa643a1ba2368235fa3981096e1
https://pubmed.ncbi.nlm.nih.gov/35975718
https://pubmed.ncbi.nlm.nih.gov/35975718
Proteasome granular localization is regulated through mitochondrial respiration and kinase signaling
Autor:
Kenrick A Waite, Jeroen Roelofs
In yeast, proteasomes are enriched in cell nuclei where they execute important cellular functions. Nutrient-stress can change this localization indicating proteasomes respond to the cell’s metabolic state. However, the signals that connect these pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f39639b17989f1442af4c84c5c929cdd
https://doi.org/10.1101/2022.01.13.476202
https://doi.org/10.1101/2022.01.13.476202
Publikováno v:
Scientific Reports
Scientific Reports, Vol 10, Iss 1, Pp 1-11 (2020)
Scientific Reports, Vol 10, Iss 1, Pp 1-11 (2020)
The efficient and timely degradation of proteins is crucial for many cellular processes and to maintain general proteostasis. The proteasome, a complex multisubunit protease, plays a critical role in protein degradation. Therefore, it is important to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cdda346860a2182b06286191283e929c
http://europepmc.org/articles/PMC7582879
http://europepmc.org/articles/PMC7582879
Publikováno v:
The Journal of Biological Chemistry
Changing physiological conditions can increase the need for protein degradative capacity in eukaryotic cells. Both the ubiquitin-proteasome system and autophagy contribute to protein degradation. However, these processes can be differently regulated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::91cf769d42b57519d86297cd9d2eeafb
https://doi.org/10.1016/j.jbc.2021.101494
https://doi.org/10.1016/j.jbc.2021.101494
Publikováno v:
The Journal of Biological Chemistry
The proteasome selectively degrades proteins. It consists of a core particle (CP), which contains proteolytic active sites that can associate with different regulators to form various complexes. How these different complexes are regulated and affecte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::586c1f16e192297ca41c552e98e8f86a
https://doi.org/10.1016/j.jbc.2021.100468
https://doi.org/10.1016/j.jbc.2021.100468
Publikováno v:
Methods in Molecular Biology ISBN: 9781493987054
Proteasomes are complex molecular machines that consist of 66 subunits. The assembly of these complexes is highly coordinated in a process that requires at least ten proteasome-specific molecular chaperones. One of the challenges in studying assembly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c67e3b74f49c572e93ec332cd3b23d14
https://doi.org/10.1007/978-1-4939-8706-1_16
https://doi.org/10.1007/978-1-4939-8706-1_16
Publikováno v:
The Journal of Biological Chemistry
The proteasome is responsible for the degradation of many cellular proteins. If and how this abundant and normally stable complex is degraded by cells is largely unknown. Here we show that in yeast, upon nitrogen starvation, proteasomes are targeted
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93f120b59d021759e0443c8b239439d4
http://europepmc.org/articles/PMC4751371
http://europepmc.org/articles/PMC4751371