Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Kirandeep K Deol"'
Autor:
Jiale Du, Sandor Babik, Yanfeng Li, Kirandeep K Deol, Stephen J Eyles, Jasna Fejzo, Marco Tonelli, Eric Strieter
Publikováno v:
eLife, Vol 11 (2022)
Degradation by the 26 S proteasome is an intricately regulated process fine tuned by the precise nature of ubiquitin modifications attached to a protein substrate. By debranching ubiquitin chains composed of K48 linkages, the proteasome-associated ub
Externí odkaz:
https://doaj.org/article/a5611065aa5d4190afa2914863fc3cc3
Publikováno v:
Biology Open, Vol 11, Iss 12 (2022)
Externí odkaz:
https://doaj.org/article/f39bbdaee2ad4652b68906347a8bfdfe
Publikováno v:
STAR Protocols, Vol 2, Iss 2, Pp 100579- (2021)
Summary: Lipid droplets are endoplasmic reticulum-derived neutral lipid storage organelles that play critical roles in cellular lipid and energy homeostasis. Here, we present a protocol for the identification of high-confidence lipid droplet proteome
Externí odkaz:
https://doaj.org/article/b2c07c0ec1364c289400ecb1cdc62f52
Publikováno v:
Frontiers in Physiology, Vol 10 (2019)
Protein ubiquitination impacts virtually every biochemical pathway in eukaryotic cells. The fate of a ubiquitinated protein is largely dictated by the type of ubiquitin modification with which it is decorated, including a large variety of polymeric c
Externí odkaz:
https://doaj.org/article/bde925a1c58443aea6ef0a67aca009ad
Autor:
Joseph M. Hendricks, Cody E. Doubravsky, Eddie Wehri, Zhipeng Li, Melissa A. Roberts, Kirandeep K. Deol, Mike Lange, Irene Lasheras-Otero, Jeremiah D. Momper, Scott J. Dixon, Kirill Bersuker, Julia Schaletzky, James A. Olzmann
Publikováno v:
Cell Chemical Biology.
Autor:
Kirandeep K. Deol, Eric R. Strieter
Publikováno v:
Curr Opin Chem Biol
The diversity of ubiquitin modifications is immense. A protein can be monoubiquitylated, multi-monoubiquitylated, and polyubiquitylated with chains varying in size and shape. Ubiquitin itself can be adorned with other ubiquitin-like proteins and smal
Autor:
Melissa A. Roberts, Kirandeep K. Deol, Mike Lange, Dara E. Leto, Alyssa J. Mathiowetz, Julian Stevenson, Sayed Hadi Hashemi, David W. Morgens, Emilee Easter, Kartoosh Heydari, Mike A. Nalls, Michael C. Bassik, Martin Kampmann, Ron R. Kopito, Faraz Faghri, James A. Olzmann
Lipid droplets (LDs) are lipid storage organelles that consist of a central core of neutral lipids surrounded by a phospholipid monolayer decorated with a unique set of integral and peripheral proteins. Invariably, at least one member of the perilipi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f2b8d123d58171067b82812f3e8c603f
https://doi.org/10.1101/2022.08.27.505556
https://doi.org/10.1101/2022.08.27.505556
Autor:
Zhipeng Li, Lucas Ferguson, Kirandeep K. Deol, Melissa A. Roberts, Leslie Magtanong, Joseph M. Hendricks, Gergey Alzaem Mousa, Seda Kilinc, Kaitlin Schaefer, James A. Wells, Michael C. Bassik, Andrei Goga, Scott J. Dixon, Nicholas T. Ingolia, James A. Olzmann
Publikováno v:
Nature chemical biology, vol 18, iss 7
The selenoprotein glutathione peroxidase 4 (GPX4) prevents ferroptosis by converting lipid peroxides into nontoxic lipid alcohols. GPX4 has emerged as a promising therapeutic target for cancer treatment, but some cancer cells are resistant to ferropt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2096209c46df26a9ae0bef17401800c0
https://escholarship.org/uc/item/80v3t2bt
https://escholarship.org/uc/item/80v3t2bt
Autor:
Zhipeng Li, Lucas Ferguson, Kirandeep K. Deol, Melissa A. Roberts, Leslie Magtanong, Michael C. Bassik, Scott J. Dixon, Nicholas T. Ingolia, James A. Olzmann
Ferroptosis is a regulated, iron-dependent form of necrosis that is triggered by the accumulation of oxidatively damaged phospholipids1–3. Glutathione peroxidase 4 (GPX4) prevents ferroptosis by converting phospholipid hydroperoxides into non-toxic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::52dc46b14a416d6a16083ef5297bb128
https://doi.org/10.1101/2022.04.11.487892
https://doi.org/10.1101/2022.04.11.487892