Results 11 to 20 of about 187,561 (340)

Ubiquitination regulates ER-phagy and remodelling of endoplasmic reticulum

open access: yesNature, 2023
The endoplasmic reticulum (ER) undergoes continuous remodelling via a selective autophagy pathway, known as ER-phagy^ 1 . ER-phagy receptors have a central role in this process^ 2 , but the regulatory mechanism remains largely unknown.
Alexis González   +18 more
semanticscholar   +1 more source

Ubiquitination in the regulation of inflammatory cell death and cancer

open access: yesCell Death and Differentiation, 2021
The ubiquitin system is complex, multifaceted, and is crucial for the modulation of a vast number of cellular processes. Ubiquitination is tightly regulated at different levels by a range of enzymes including E1s, E2s, and E3s, and an array of DUBs.
Peter E Cockram   +5 more
semanticscholar   +1 more source

Identification of a small molecule as inducer of ferroptosis and apoptosis through ubiquitination of GPX4 in triple negative breast cancer cells

open access: yesJournal of Hematology & Oncology, 2021
Background TNBC is the most aggressive breast cancer with higher recurrence and mortality rate than other types of breast cancer. There is an urgent need for identification of therapeutic agents with unique mode of action for overcoming current ...
Yahui Ding   +8 more
semanticscholar   +1 more source

The role of ubiquitination and deubiquitination in tumor invasion and metastasis

open access: yesInternational Journal on Biological Sciences, 2022
Ubiquitination is vital for multiple cellular processes via dynamic modulation of proteins related to cell growth, proliferation, and survival. Of the ubiquitination system components, E3 ubiquitin ligases and deubiquitinases have the most prominent ...
Shuang Han   +8 more
semanticscholar   +1 more source

To Be or Not to Be...Ubiquitinated? [PDF]

open access: yesCell Cycle, 2004
Levels of p21, a cyclin-dependent kinase (CDK) inhibitor, are controlled in part at the post-translational level by protein degradation. Although the signaling pathways leading to p21 degradation have not yet been fully elucidated, it is evident that p21 ubiquitination is an essential factor in its degradation.
Michele Pagano, Joanna Bloom
openaire   +3 more sources

Beyond K48 and K63: non-canonical protein ubiquitination

open access: yesCellular & Molecular Biology Letters, 2021
Protein ubiquitination has become one of the most extensively studied post-translational modifications. Originally discovered as a critical element in highly regulated proteolysis, ubiquitination is now regarded as essential for many other cellular ...
M. Tracz, W. Białek
semanticscholar   +1 more source

Cracking the Ubiquitin Code: The Ubiquitin Toolbox [PDF]

open access: yesCurrent Issues in Molecular Biology, 2019
Ubiquitination, a post-translational modification, regulates a vast array of fundamental biological processes with dysregulation of the dedicated enzymes giving rise to pathologies such as cancer and neurodegenerative diseases. Assembly and its ensuing removal of this post-translational modification, determining a large variety of biological functions,
Mulder, M.P.C., Witting, K.F., Ovaa, H.
openaire   +3 more sources

Ubiquitination is essential for recovery of cellular activities after heat shock

open access: yesScience, 2021
Tailoring stress responses When faced with environmental stress, cells respond by shutting down cellular processes such as translation and nucleocytoplasmic transport.
Brian A. Maxwell   +7 more
semanticscholar   +1 more source

Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination [PDF]

open access: yesCell, 2016
Conventional ubiquitination involves the ATP-dependent formation of amide bonds between the ubiquitin C terminus and primary amines in substrate proteins. Recently, SdeA, an effector protein of pathogenic Legionella pneumophila, was shown to mediate NAD-dependent and ATP-independent ubiquitin transfer to host proteins.
Ivan Dikic   +7 more
openaire   +4 more sources

To Ubiquitinate or Not to Ubiquitinate: TRIM17 in Cell Life and Death [PDF]

open access: yesCells, 2021
TRIM17 is a member of the TRIM family, a large class of RING-containing E3 ubiquitin-ligases. It is expressed at low levels in adult tissues, except in testis and in some brain regions. However, it can be highly induced in stress conditions which makes it a putative stress sensor required for the triggering of key cellular responses.
Meenakshi Basu-Shrivastava   +3 more
openaire   +5 more sources

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