Results 11 to 20 of about 119,140 (262)
Structural Diversity of Ubiquitin E3 Ligase [PDF]
The post-translational modification of proteins regulates many biological processes. Their dysfunction relates to diseases. Ubiquitination is one of the post-translational modifications that target lysine residue and regulate many cellular processes. Three enzymes are required for achieving the ubiquitination reaction: ubiquitin-activating enzyme (E1),
Toma-Fukai, Sachiko, Shimizu, Toshiyuki
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Discovery of E3 Ligase Ligands for Target Protein Degradation
Target protein degradation has emerged as a promising strategy for the discovery of novel therapeutics during the last decade. Proteolysis-targeting chimera (PROTAC) harnesses a cellular ubiquitin-dependent proteolysis system for the efficient ...
Jaeseok Lee +5 more
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A Comprehensive Atlas of E3 Ubiquitin Ligase Mutations in Neurological Disorders
Protein ubiquitination is a posttranslational modification that plays an integral part in mediating diverse cellular functions. The process of protein ubiquitination requires an enzymatic cascade that consists of a ubiquitin activating enzyme (E1 ...
Arlene J. George +4 more
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The Role of E3 Ligase Pirh2 in Disease
The p53-dependent ubiquitin ligase Pirh2 regulates a number of proteins involved in different cancer-associated processes. Targeting the p53 family proteins, Chk2, p27Kip1, Twist1 and others, Pirh2 participates in such cellular processes as proliferation, cell cycle regulation, apoptosis and cellular migration.
Alexandra Daks +5 more
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IAPs as E3 ligases of Rac1 [PDF]
Inhibitors of Apoptosis Proteins (IAPs) are well-studied E3 ubiquitin ligases predominantly known for regulation of apoptosis. We uncovered that IAPs can function as a direct E3 ubiquitin ligase of RhoGTPase Rac1. cIAP1 and XIAP directly conjugate polyubiquitin chains to Lysine 147 of activated Rac1 and target it for proteasomal degradation ...
Oberoi-Khanuja, Tripat Kaur +1 more
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Pto kinase binds two domains of AvrPtoB and its proximity to the effector E3 ligase determines if it evades degradation and activates plant immunity. [PDF]
The tomato--Pseudomonas syringae pv. tomato (Pst)--pathosystem is one of the best understood models for plant-pathogen interactions. Certain wild relatives of tomato express two closely related members of the same kinase family, Pto and Fen, which ...
Johannes Mathieu +2 more
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RING Domain E3 Ubiquitin Ligases
E3 ligases confer specificity to ubiquitination by recognizing target substrates and mediating transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to substrate. The activity of most E3s is specified by a RING domain, which binds to an E2∼ubiquitin thioester and activates discharge of its ubiquitin cargo.
Deshaies, Raymond J. +1 more
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AIRE Functions As an E3 Ubiquitin Ligase [PDF]
Autoimmune regulator (AIRE) gene mutation is responsible for the development of autoimmune-polyendocrinopathy-candidiasis ectodermal dystrophy, an organ-specific autoimmune disease with monogenic autosomal recessive inheritance. AIRE is predominantly expressed in medullary epithelial cells of the thymus and is considered to play important roles in the ...
Uchida, Daisuke +11 more
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Inhibitors of ubiquitin E3 ligase as potential new antimalarial drug leads
Background Protein ubiquitylation is an important post-translational regulation, which has been shown to be necessary for life cycle progression and survival of Plasmodium falciparum.
Jagrati Jain +3 more
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TRIM family of E3 ubiquitin ligases have an amino-terminal conserved tripartite motif consisting of RING, B-Box, coiled-coil domain and different C-terminal domain leading it to classification into 11 subclasses.
Ishita Gupta +3 more
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