Results 151 to 160 of about 72,591 (191)

DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on nucleic acids. [PDF]

Nucleic Acids Res
Zhu K, Suskiewicz MJ, Chatrin C, Strømland Ø, Dorsey BW, Aucagne V, Ahel D, Ahel I.   +7 more
europepmc   +1 more source

Deltex family E3 ligases specifically ubiquitinate the terminal ADP-ribose of poly(ADP-ribosyl)ation. [PDF]

Biochem Biophys Res Commun
Kelly M, Dietz C, Kasson S, Zhang Y, Holtzman MJ, Kim IK.   +5 more
europepmc   +1 more source

Arabidopsis HECT and RING-type E3 Ligases Promote MAPKKK18 Degradation to Regulate Abscisic Acid Signaling. [PDF]

Plant Cell Physiol
Tajdel-Zielińska M, Janicki M, Marczak M, Ludwików A.   +3 more
europepmc   +1 more source

TRIM52 is a primate-specific player in the DNA repair process under tight proteolytic control by a triad of giant E3 ligases

Shulkina A, Hacker K, Ehrmann JF, Budroni V, Mandlbauer A, Bock J, Grabarczyk DB, Cochella L, Clausen T, Versteeg GA.   +9 more
europepmc   +1 more source

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E3 ubiquitin ligases

Essays in Biochemistry, 2005
The selectivity of the ubiquitin–26 S proteasome system (UPS) for a particular substrate protein relies on the interaction between a ubiquitin-conjugating enzyme (E2, of which a cell contains relatively few) and a ubiquitin–protein ligase (E3, of which there are possibly hundreds).
Helen C, Ardley, Philip A, Robinson
openaire   +2 more sources

E3 ligases team up

Nature Reviews Molecular Cell Biology, 2010
Katharine H Wrighton
exaly   +2 more sources

RBR E3 ubiquitin ligases in tumorigenesis

Seminars in Cancer Biology, 2020
RING-in-between-RING (RBR) E3 ligases are one class of E3 ligases that is characterized by the unique RING-HECT hybrid mechanism to function with E2s to transfer ubiquitin to target proteins for degradation. Emerging evidence has demonstrated that RBR E3 ligases play essential roles in neurodegenerative diseases, infection, inflammation and cancer ...
Peter, Wang, Xiaoming, Dai, Wenxiao, Jiang, Yuyun, Li, Wenyi, Wei   +4 more
openaire   +2 more sources

The Role of Ubiquitin E3 Ligase in Atherosclerosis

Current Medicinal Chemistry, 2020
Atherosclerosis is a chronic inflammatory vascular disease. Atherosclerotic cardiovascular disease is the main cause of death in both developed and developing countries. Many pathophysiological factors, including abnormal cholesterol metabolism, vascular inflammatory response, endothelial dysfunction and vascular smooth muscle cell proliferation and ...
Zhi-Xiang Zhou, Zhong Ren, Bin-Jie Yan, Shun-Lin Qu, Zhi-Han Tang, Dang-Heng Wei, Lu-Shan Liu, Min-Gui Fu, Zhi-Sheng Jiang   +8 more
openaire   +2 more sources

E3 ubiquitin ligases for MHC molecules

Current Opinion in Immunology, 2009
Recently, novel E3 ubiquitin ligases that target MHC molecules for lysosomal degradation have been discovered by several groups. All these E3s are membrane-bound and possess a variant type RING domain, termed the RING-CH or RING variant (RINGv) domain. They belong to a new E3 family designated Modulator of Immune Recognition (MIR), based on the name of
Satoshi, Ishido, Eiji, Goto, Yohei, Matsuki, Mari, Ohmura-Hoshino   +3 more
openaire   +2 more sources

Inhibitors for E3 ubiquitin ligases

Nature Biotechnology, 2010
Two studies show that specific cullin-RING E3 ubiquitin ligases can be targeted with small molecules.
J Wade Harper
exaly   +2 more sources