Results 301 to 310 of about 254,188 (362)

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
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A giant ubiquitin ligase

Nature Chemical Biology, 2021
The structure of a giant ubiquitin E3 ligase sheds light on its activation in a substrate-dependent manner and shows how a single E3 enzyme uses distinct recognition modules to confer substrate specificity.
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On ubiquitin ligases and cancer

Human Mutation, 2005
Protein kinase genes account for almost 10% of all currently known cancer genes, highlighting the role of signal transduction in oncogenesis. A reexamination of the literature and available databases shows that E3 ubiquitin ligases are also key mediators of tumorigenesis. Altogether kinase and E3 genes represent more than 15% of the known cancer genes,
Jacques S, Beckmann, Fabienne, Maurer, Mauro, Delorenzi, Laurent, Falquet   +3 more
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E3 ubiquitin ligase Siah1 aggravates NAFLD through Scp2 ubiquitination

International Immunopharmacology, 2023
Nonalcoholic fatty liver disease (NAFLD) is one of the most common liver disorders and accompanied by multiple metabolic dysfunctions. Although excessive lipid accumulation in hepatocytes has been identified as a crucial mediator of NAFLD development, the underlying mechanisms are very complicated and remain largely unknown.
Zhu, Zhu, Xiao, Hu, Kehan, Liu, Jingpei, Li, Kun, Fan, Huafei, Wang, Li, Wang, Lulu, He, Yihui, Ma, Ruijuan, Guan, Zhengyang, Wang   +10 more
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Ubiquitin Ligases in Malignant Lymphoma

Leukemia & Lymphoma, 2004
The highly controlled degradation of proteins via the ubiquitin-proteasome pathway represents a key mechanism for cell regulation and homeostasis. Ubiquitin-dependent proteolysis, carried out in large part by the E3 ubiquitin ligases, is a critical mode of post-translational modification that is important in regulation of cell cycle progression, signal
Megan S, Lim, Kojo S J, Elenitoba-Johnson   +1 more
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Monitoring MHC Ubiquitination by MARCH Ubiquitin Ligases

2019
Ubiquitination is a reversible process that controls the intracellular transport of many transmembrane molecules. Ubiquitination of MHC I, MHC II, and CD1a by different members of the MARCH family of E3 ubiquitin ligases is a key event in the regulation of the potent immunostimulatory properties of activated dendritic cells. We describe here methods to
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Comprehensive Ubiquitin E2 Profiling of Ten Ubiquitin E3 Ligases

Cell Biochemistry and Biophysics, 2013
The ubiquitin pathway regulates diverse functions including protein localization and stability. The complexity of the pathway involving nearly 40 identified E2 conjugating enzymes and over 600 E3 ligases raises the issue of specificity. With the E2s and E3s fitting into a limited number of classes based on bioinformatics, structures, and proven ...
Jeffrey G, Marblestone, Samir, Butt, Devin M, McKelvey, David E, Sterner, Michael R, Mattern, Benjamin, Nicholson, Michael J, Eddins   +6 more
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Parkin: a multifaceted ubiquitin ligase

Biochemical Society Transactions, 2006
Mutations in the parkin gene are a common cause of autosomal recessive early-onset parkinsonism. Parkin functions as an E3 ubiquitin ligase where it can polyubiquitinate a number of its protein substrates, thus targeting them for degradation by the 26 S proteasomal complex.
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Ubiquitin Ligase RBX2/SAG Regulates Mitochondrial Ubiquitination and Mitophagy

Circulation Research
BACKGROUND: Clearance of damaged mitochondria via mitophagy is crucial for cellular homeostasis. Apart from Parkin, little is known about additional Ub (ubiquitin) ligases that mediate mitochondrial ubiquitination and turnover, particularly in highly metabolically active organs such as the heart.
Wenjuan Wang, Ermin Li, Jianqiu Zou, Chen Qu, Juan Ayala, Yuan Wen, Md Sadikul Islam, Neal L. Weintraub, David J.R. Fulton, Qiangrong Liang, Jiliang Zhou, Jinbao Liu, Jie Li, Yi Sun, Huabo Su   +14 more
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