Results 1 to 10 of about 120,350 (347)

E3 ubiquitin ligases: styles, structures and functions

Molecular Biomedicine, 2021
E3 ubiquitin ligases are a large family of enzymes that join in a three-enzyme ubiquitination cascade together with ubiquitin activating enzyme E1 and ubiquitin conjugating enzyme E2.
Yang Wang
exaly   +2 more sources

Regulatory Roles of E3 Ubiquitin Ligases and Deubiquitinases in Bone [PDF]

Biomolecules
E3 ubiquitin ligases and deubiquitinating enzymes (DUBs) are pivotal regulators of bone homeostasis, orchestrating osteoblast differentiation, proliferation, and osteoclast activity by controlling protein degradation and stability. This review delineates
Haotian He, Lifei Wang, Bao Xian, Yayi Xia   +3 more
doaj   +2 more sources

Plant SUMO E3 Ligases: Function, Structural Organization, and Connection With DNA

Frontiers in Plant Science, 2021
Protein modification by the small ubiquitin-like modifier (SUMO) plays an important role in multiple plant processes, including growth, development, and the response to abiotic stresses.
Laurent Cappadocia, Ivana Smičiklas
exaly   +3 more sources

Cullin 3 Ubiquitin Ligases in Cancer Biology: Functions and Therapeutic Implications

Frontiers in Oncology, 2016
Cullin-RING ubiquitin ligases are the largest E3 ligase family in eukaryotes and are multi-protein complexes. In these complexes, the Cullin protein serves as a scaffold to connect two functional modules of the ligases, the catalytic subunit and ...
Hsin-yi Chen, Ruey-hwa Chen
exaly   +3 more sources

Small Molecule Modulators of RING-Type E3 Ligases: MDM and Cullin Families as Targets

Frontiers in Pharmacology, 2018
Ubiquitin–proteasome system (UPS) is a primary signaling pathway for regulation of intracellular protein levels. E3 ubiquitin ligases, substrate-specific members of the UPS, represent highly attractive protein targets for drug discovery.
Emil Bulatov, Almaz A Zagidullin, Albert A Rizvanov   +2 more
exaly   +3 more sources

E3 Ubiquitin Ligases Neurobiological Mechanisms: Development to Degeneration

Frontiers in Molecular Neuroscience, 2017
Cells regularly synthesize new proteins to replace old or damaged proteins. Deposition of various aberrant proteins in specific brain regions leads to neurodegeneration and aging.
Arun Upadhyay, Vibhuti Joshi, Amit Mishra   +2 more
exaly   +3 more sources

Role and therapeutic potential of E3s in the tumor microenvironment of hepatocellular carcinoma [PDF]

Frontiers in Immunology
Hepatocellular carcinoma (HCC) is a high-incidence, poor-prognosis malignancy worldwide, requiring new strategies for treatment. Ubiquitination, especially ubiquitination through E3 ubiquitin ligases, plays an indispensable role in the development and ...
Hailin Wang, Qiang Li, Qinqin Tang, Gang Shi, Guo Wu, Xingbo Mao, Changkang Wu, Lixin Zhang, Jie Liu, Jingdong Li, Bo Li   +10 more
doaj   +2 more sources

Identification of suitable target/E3 ligase pairs for PROTAC development using a rapamycin-induced proximity assay (RiPA) [PDF]

eLife
The development of proteolysis targeting chimeras (PROTACs), which induce the degradation of target proteins by bringing them into proximity with cellular E3 ubiquitin ligases, has revolutionized drug development. While the human genome encodes more than
Bikash Adhikari, Katharina Schneider, Mathias Diebold, Christoph Sotriffer, Elmar Wolf   +4 more
doaj   +2 more sources

E3 ubiquitin ligases in the acute leukemic signaling pathways

Frontiers in Physiology, 2022
Acute leukemia is a common hematologic tumor with highly genetic heterogeneity, and many factors are involved in the pathogenesis and drug-resistance mechanism.
Qianru Zhan, Heyang Zhang, Boquan Wu, Naijin Zhang, Lijun Zhang   +4 more
doaj   +1 more source

Functional Diversity and Structural Disorder in the Human Ubiquitination Pathway [PDF]

, 2013
The ubiquitin-proteasome system plays a central role in cellular regulation and protein quality control (PQC). The system is built as a pyramid of increasing complexity, with two E1 (ubiquitin activating), few dozen E2 (ubiquitin conjugating) and several
A Arrigoni, A Hershko, A Mohan, AE Deffenbaugh, B Bothner, B Hao, B Hess, C Guda, C Haynes, CJ Cox, CM Pickart, D Ekman, D Szklarczyk, D Van Der Spoel, D Vuzman, DM Duda, DM Duda, DW Leung, ES Zimmerman, ET Powers, F Bernassola, F Tama, F. Gisou van der Goot, FU Hartl, G Bussi, G Moncalian, G Swaminathan, G Wu, H Daub, H Dinkel, H Dou, H Shimizu, H Zhu, HC van Leeuwen, HE Niessen, HJ Dyson, HM Berman, I Szymkiewicz, I von Ossowski, J Liu, J Ma, J Prilusky, JC Rosenbaum, JH Fong, JM Huibregtse, K Peng, K Suhre, L Aravind, L Yang, LM Iakoucheva, M Christen, M Cormont, M Fuxreiter, M Fuxreiter, M Guharoy, M Hochstrasser, M Kanehisa, M Kanehisa, M Kanehisa, M Vidal, M Zhao, MA McCoy, Mainak Guharoy, MD Petroski, MD Petroski, ME Sowa, N Foray, N Mathias, N Zheng, P Tompa, P Tompa, P Tompa, P Tompa, P Tompa, Pallab Bhowmick, PE Ryan, PE Wright, Peter Tompa, PW Hildebrand, R Kiss, RG Smock, Rita Pancsa, RJ Deshaies, S Fishbain, S Vucetic, S Wiesner, SC Kales, SJ Demarest, SJ van Wijk, T Hagai, T Inobe, T Mittag, T Ravid, U Emekli, VN Uversky, W Humphrey, W Li, WY Mark, X Zhong, Y Haupt, Y Sheng, Y Xie, Z Dosztanyi, Z Dosztanyi, Z Dosztanyi   +104 more
core   +19 more sources