Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Philipp Kimmig"'
Autor:
Weihan Li, Voytek Okreglak, Jirka Peschek, Philipp Kimmig, Meghan Zubradt, Jonathan S Weissman, Peter Walter
Publikováno v:
eLife, Vol 7 (2018)
The endoplasmic reticulum (ER) protein folding capacity is balanced with the protein folding burden to prevent accumulation of un- or misfolded proteins. The ER membrane-resident kinase/RNase Ire1 maintains ER protein homeostasis through two fundamen
Externí odkaz:
https://doaj.org/article/06938f16955246289af878b85e81e6ce
Publikováno v:
eLife, Vol 6 (2017)
The unfolded protein response (UPR) monitors and adjusts the protein folding capacity of the endoplasmic reticulum (ER). In S. pombe, the ER membrane-resident kinase/endoribonuclease Ire1 utilizes a mechanism of selective degradation of ER-bound mRNA
Externí odkaz:
https://doaj.org/article/e2311e0be31d43d19f18dadee113fec8
Autor:
Agnès H Michel, Riko Hatakeyama, Philipp Kimmig, Meret Arter, Matthias Peter, Joao Matos, Claudio De Virgilio, Benoît Kornmann
Publikováno v:
eLife, Vol 6 (2017)
Yeast is a powerful model for systems genetics. We present a versatile, time- and labor-efficient method to functionally explore the Saccharomyces cerevisiae genome using saturated transposon mutagenesis coupled to high-throughput sequencing. SAturat
Externí odkaz:
https://doaj.org/article/c9c8b85971e64a0b8c2907d500bae38d
Autor:
Philipp Kimmig, Marcy Diaz, Jiashun Zheng, Christopher C Williams, Alexander Lang, Tomas Aragón, Hao Li, Peter Walter
Publikováno v:
eLife, Vol 1 (2012)
The unfolded protein response (UPR) monitors the protein folding capacity of the endoplasmic reticulum (ER). In all organisms analyzed to date, the UPR drives transcriptional programs that allow cells to cope with ER stress. The non-conventional spli
Externí odkaz:
https://doaj.org/article/c91323c6c56c4923a9dbdfd8e493f3d4
Autor:
Philipp Kimmig, Meghan Zubradt, Peter Walter, Jonathan S. Weissman, Weihan Li, Jirka Peschek, Voytek Okreglak
Publikováno v:
eLife
eLife, 7
eLife, Vol 7 (2018)
eLife, 7
eLife, Vol 7 (2018)
The endoplasmic reticulum (ER) protein folding capacity is balanced with the protein folding burden to prevent accumulation of un- or misfolded proteins. The ER membrane-resident kinase/RNase Ire1 maintains ER protein homeostasis through two fundamen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6ec2c1e77ee6c64d0b86fd9ac37c3bf
http://europepmc.org/articles/PMC6037481
http://europepmc.org/articles/PMC6037481
Publikováno v:
The FASEB Journal. 32
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::64bf190b4ec35c7496942f95c85bfcf5
https://doi.org/10.1096/fasebj.2018.32.1_supplement.653.9
https://doi.org/10.1096/fasebj.2018.32.1_supplement.653.9
Publikováno v:
eLife
eLife, Vol 6 (2017)
eLife, 6
eLife, Vol 6 (2017)
eLife, 6
The unfolded protein response (UPR) monitors and adjusts the protein folding capacity of the endoplasmic reticulum (ER). In S. pombe, the ER membrane-resident kinase/endoribonuclease Ire1 utilizes a mechanism of selective degradation of ER-bound mRNA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e66d83b25bcb046aa2da4791aa1792d
https://doi.org/10.7554/elife.29216
https://doi.org/10.7554/elife.29216
Autor:
Avi Ashkenazi, David A. Lawrence, Peter Walter, James C. Paton, Adrienne W. Paton, Aaron S Mendez, Diego Acosta-Alvear, Philipp Kimmig, Scot A. Marsters, Min Lu
Publikováno v:
Science (New York, N.Y.), vol 345, iss 6192
Life and death and quality control When cells are subjected to too much stress, they curl up their toes and die. Lu et al. describe a clever strategy cells use to stay alive as long as they are not stressed for too long. The cells' quality-control ma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba2f21156d3c47be03f34b3522de8097
https://pubmed.ncbi.nlm.nih.gov/25027654
https://pubmed.ncbi.nlm.nih.gov/25027654