Zobrazeno 1 - 10
of 49
pro vyhledávání: '"D Thomas Rutkowski"'
Autor:
Javier A Gomez, D Thomas Rutkowski
Publikováno v:
eLife, Vol 5 (2016)
Endoplasmic reticulum (ER) stress is implicated in many chronic diseases, but very little is known about how the unfolded protein response (UPR) responds to persistent ER stress in vivo. Here, we experimentally reconstituted chronic ER stress in the
Externí odkaz:
https://doaj.org/article/3e2ae8e91a2542eea34c931282ed71c5
Autor:
Janice M Staber, Molly J Pollpeter, Angela Arensdorf, Patrick L Sinn, D Thomas Rutkowski, Paul B McCray, Jr
Publikováno v:
Molecular Therapy: Methods & Clinical Development, Vol 1, Iss C (2014)
Hemophilia A, caused by a deficiency in factor VIII (FVIII), is the most severe inherited bleeding disorder. Hemophilia A is an attractive gene therapy candidate because even small increases in FVIII levels will positively alter the phenotype. While
Externí odkaz:
https://doaj.org/article/8a13042e6ecb4028aa741177a9c51d67
Publikováno v:
Frontiers in Genetics, Vol 4 (2013)
The unfolded protein response (UPR) responds to disruption of endoplasmic reticulum (ER) function by initiating signaling cascades that ultimately culminate in extensive transcriptional regulation. Classically, this regulation includes genes encoding
Externí odkaz:
https://doaj.org/article/879aa4ac819e4f74888ecc6514d44c27
Autor:
Diane DeZwaan-McCabe, Jesse D Riordan, Angela M Arensdorf, Michael S Icardi, Adam J Dupuy, D Thomas Rutkowski
Publikováno v:
PLoS Genetics, Vol 9, Iss 12, p e1003937 (2013)
Viral hepatitis, obesity, and alcoholism all represent major risk factors for hepatocellular carcinoma (HCC). Although these conditions also lead to integrated stress response (ISR) or unfolded protein response (UPR) activation, the extent to which t
Externí odkaz:
https://doaj.org/article/607b8f25d76e47069dd9b7ccf42ab584
Autor:
D Thomas Rutkowski, Stacey M Arnold, Corey N Miller, Jun Wu, Jack Li, Kathryn M Gunnison, Kazutoshi Mori, Amir A Sadighi Akha, David Raden, Randal J Kaufman
Publikováno v:
PLoS Biology, Vol 4, Iss 11, p e374 (2006)
The accumulation of unfolded proteins in the endoplasmic reticulum (ER) activates a signaling cascade known as the unfolded protein response (UPR). Although activation of the UPR is well described, there is little sense of how the response, which ini
Externí odkaz:
https://doaj.org/article/a026c3ed14ba4c9a93f5af077eeaf9c4
Publikováno v:
bioRxiv
Cellular stresses elicit signaling cascades that are capable of both mitigating the inciting dysfunction and initiating cell death when the stress cannot be overcome. During endoplasmic reticulum (ER) stress, the transcription factor CHOP is widely r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b6256b3ab826a9227c18227927aaa5e
https://europepmc.org/articles/PMC10055232/
https://europepmc.org/articles/PMC10055232/
Autor:
Anit Shah, Ian Huck, Kaylia Duncan, Erica R. Gansemer, Udayan Apte, Mark A. Stamnes, D. Thomas Rutkowski
Publikováno v:
bioRxiv
In all eukaryotic cell types, the unfolded protein response (UPR) upregulates factors that promote protein folding and misfolded protein clearance to help alleviate endoplasmic reticulum (ER) stress. Yet ER stress in the liver is uniquely accompanied
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bcf04abed3696da0817e349b47200b3
https://doi.org/10.1101/2023.02.09.527889
https://doi.org/10.1101/2023.02.09.527889
Autor:
Erica R. Gansemer, D. Thomas Rutkowski
Publikováno v:
Frontiers in molecular biosciences. 9
The endoplasmic reticulum (ER) lumen is highly oxidizing compared to other subcellular compartments, and maintaining the appropriate levels of oxidizing and reducing equivalents is essential to ER function. Both protein oxidation itself and other ess
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14415c318d50a0679fd6715399771488
https://pubmed.ncbi.nlm.nih.gov/35601828
https://pubmed.ncbi.nlm.nih.gov/35601828
Autor:
Kyle S. McCommis, Erica R. Gansemer, Abdul Qaadir King-McAlpin, Eric B. Taylor, Michael R. Martino, Brian N. Finck, Matthew J. Potthoff, D. Thomas Rutkowski
Publikováno v:
iScience, Vol 23, Iss 5, Pp-(2020)
iScience
iScience
Summary Many metabolic diseases disrupt endoplasmic reticulum (ER) homeostasis, but little is known about how metabolic activity is communicated to the ER. Here, we show in hepatocytes and other metabolically active cells that decreasing the availabi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e2fc083454e014a2d2870902931c763
http://www.sciencedirect.com/science/article/pii/S2589004220303011
http://www.sciencedirect.com/science/article/pii/S2589004220303011
Autor:
D. Thomas Rutkowski
Publikováno v:
The FEBS Journal. 286:356-378
The unfolded protein response (UPR) improves endoplasmic reticulum (ER) protein folding in order to alleviate stress. Yet it is becoming increasingly clear that the UPR regulates processes well beyond those directly involved in protein folding, in so
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68f3e01fa9237efce5edd5ec2e27dc78
https://doi.org/10.1111/febs.14389
https://doi.org/10.1111/febs.14389