Zobrazeno 1 - 10
of 126
pro vyhledávání: '"Michael H. Glickman"'
Autor:
Inbal Maniv, Mahasen Sarji, Anwar Bdarneh, Alona Feldman, Roi Ankawa, Elle Koren, Inbar Magid-Gold, Noa Reis, Despina Soteriou, Shiran Salomon-Zimri, Tali Lavy, Ellina Kesselman, Naama Koifman, Thimo Kurz, Oded Kleifeld, Daniel Michaelson, Fred W. van Leeuwen, Bert M. Verheijen, Yaron Fuchs, Michael H. Glickman
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-14 (2023)
Abstract Alzheimer’s disease (AD) is characterized by toxic protein accumulation in the brain. Ubiquitination is essential for protein clearance in cells, making altered ubiquitin signaling crucial in AD development. A defective variant, ubiquitin
Externí odkaz:
https://doaj.org/article/74e57d7f81c342d092153d856a153d11
Autor:
Indrajit Sahu, Sachitanand M. Mali, Prasad Sulkshane, Cong Xu, Andrey Rozenberg, Roni Morag, Manisha Priyadarsini Sahoo, Sumeet K. Singh, Zhanyu Ding, Yifan Wang, Sharleen Day, Yao Cong, Oded Kleifeld, Ashraf Brik, Michael H. Glickman
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-21 (2021)
The 20S particle is part of the 26S proteasome, but also exists as a free complex. Here, the authors outline signature activities of the 20S and combine chemical, structural, functional and proteomic assays to show that the 20S can degrade ubiquitin
Externí odkaz:
https://doaj.org/article/46cc92bf4c3f4fcfb5bb5b4fa465398a
Autor:
Indrajit Sahu, Monika Bajorek, Xiaolin Tan, Madabhushi Srividya, Daria Krutauz, Noa Reis, Pawel A. Osmulski, Maria E. Gaczynska, Michael H. Glickman
Publikováno v:
Biomolecules, Vol 13, Iss 3, p 480 (2023)
The proteolytic active sites of the 26S proteasome are sequestered within the catalytic chamber of its 20S core particle (CP). Access to this chamber is through a narrow channel defined by the seven outer α subunits. In the resting state, the N-term
Externí odkaz:
https://doaj.org/article/7c0c5628f9aa492282204b57b9a318f5
Publikováno v:
Redox Biology, Vol 45, Iss , Pp 102047- (2021)
The contribution of the Ubiquitin-Proteasome System (UPS) to mitophagy has been largely attributed to the E3 ubiquitin ligase Parkin. Here we show that in response to the oxidative stress associated with hypoxia or the hypoxia mimic CoCl2, the damage
Externí odkaz:
https://doaj.org/article/66e0520f3f11463c89055c15954f6ac4
Publikováno v:
Molecules, Vol 27, Iss 15, p 4867 (2022)
Deciphering the protein posttranslational modification (PTM) code is one of the greatest biochemical challenges of our time. Phosphorylation and ubiquitylation are key PTMs that dictate protein function, recognition, sub-cellular localization, stabil
Externí odkaz:
https://doaj.org/article/f5b12faaa7ff40d189963dd5bf099dbf
Autor:
Indrajit Sahu, Michael H. Glickman
Publikováno v:
Biomolecules, Vol 11, Iss 2, p 148 (2021)
Four decades of proteasome research have yielded extensive information on ubiquitin-dependent proteolysis. The archetype of proteasomes is a 20S barrel-shaped complex that does not rely on ubiquitin as a degradation signal but can degrade substrates
Externí odkaz:
https://doaj.org/article/537a68b3c73d4a9bad8bfe75245e9e97
Autor:
Tal Keren-Kaplan, Lee Zeev Peters, Olga Levin-Kravets, Ilan Attali, Oded Kleifeld, Noa Shohat, Shay Artzi, Ori Zucker, Inbar Pilzer, Noa Reis, Michael H. Glickman, Shay Ben-Aroya, Gali Prag
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
Ubiquitin (Ub) receptors are responsible for the recognition of ubiquitylated proteins. Here the authors describe the crystal structure of the ubiquitylated form of the Ub-receptor Rpn10, which suggest that ubiquitylation of Rpn10 promotes its dissoc
Externí odkaz:
https://doaj.org/article/8431d5b994ec4a4ca5d12daa3a68d3a3
Autor:
Nurit Livnat-Levanon, Éva Kevei, Oded Kleifeld, Daria Krutauz, Alexandra Segref, Teresa Rinaldi, Zoi Erpapazoglou, Mickael Cohen, Noa Reis, Thorsten Hoppe, Michael H. Glickman
Publikováno v:
Cell Reports, Vol 7, Iss 5, Pp 1371-1380 (2014)
In eukaryotic cells, proteasomes exist primarily as 26S holoenzymes, the most efficient configuration for ubiquitinated protein degradation. Here, we show that acute oxidative stress caused by environmental insults or mitochondrial defects results in
Externí odkaz:
https://doaj.org/article/8196f51a328140d98f9926595f205bc6
Autor:
Laylan Bramasole, Abhishek Sinha, Dana Harshuk, Angela Cirigliano, Gurevich Sylvia, Zanlin Yu, Rinat Lift Carmeli, Michael H. Glickman, Teresa Rinaldi, Elah Pick
Publikováno v:
Biomolecules, Vol 9, Iss 9, p 449 (2019)
The class of Cullin−RING E3 ligases (CRLs) selectively ubiquitinate a large portion of proteins targeted for proteolysis by the 26S proteasome. Before degradation, ubiquitin molecules are removed from their conjugated proteins by deubiquitinating e
Externí odkaz:
https://doaj.org/article/fb2309b1301d4e8786277a08077d00d6
Publikováno v:
Biochemistry Research International, Vol 2012 (2012)
Externí odkaz:
https://doaj.org/article/000fc886191e4e008839f4cdc59ccbd8