Results 71 to 80 of about 80,046 (337)

The testis-specific E3 ubiquitin ligase RNF133 is required for fecundity in mice

BMC Biology, 2022
Background Ubiquitination is a post-translational modification required for a number of physiological functions regulating protein homeostasis, such as protein degradation.
Kaori Nozawa, Yoshitaka Fujihara, Darius J. Devlin, Ricardo E. Deras, Katarzyna Kent, Irina V. Larina, Kohei Umezu, Zhifeng Yu, Courtney M. Sutton, Qiuji Ye, Laura K. Dean, Chihiro Emori, Masahito Ikawa, Thomas X. Garcia, Martin M. Matzuk   +14 more
doaj   +1 more source

The COP9 SIGNALOSOME is required for postembryonic meristem maintenance in Arabidopsis thaliana [PDF]

, 2015
Cullin-RING E3 ligases (CRLs) regulate different aspects of plant development, and are activated by modification of their cullin subunit with the ubiquitin-like protein NEDD8 (NEural precursor cell expressed Developmentally Down-regulated 8) (neddylation)
Boccaccini, Alessandra, Butera, Simone, Costantino, Paolo, Du, Kaiqi, Franciosini, Anna, Jenik, Pablo D, Matari, Nahill H, Moubayidin, Laila, Sabatini, Sabrina, Serino, Giovanna, Vittorioso, Paola   +10 more
core   +1 more source

Turning the RING Domain Protein MdmX into an Active Ubiquitin-Protein Ligase* [PDF]

Journal of Biological Chemistry, 2010
The related RING domain proteins MdmX and Mdm2 are best known for their role as negative regulators of the tumor suppressor p53. However, although Mdm2 functions as a ubiquitin ligase for p53, MdmX does not have appreciable ubiquitin ligase activity.
Iyappan, Saravanakumar, Wollscheid, Hans-Peter, Rojas-Fernandez, Alejandro, Tang, Hao-Chen, Singh, Rajesh Kumar, Marquardt, Andreas, Scheffner, Martin   +6 more
openaire   +4 more sources

Integrative miRNOMe profiling reveals the miR‐195‐5p–CHEK1 axis and its impact on luminal breast cancer outcomes

Molecular Oncology, EarlyView.
In luminal (ER+) breast carcinoma (BC), miRNA profiling identified miR‐195‐5p as a key regulator of proliferation that targets CHEK1, CDC25A, and CCNE1. High CHEK1 expression correlates with worse relapse‐free survival after chemotherapy, especially in patients with luminal A subtype.
Veronika Boušková, Marie Ehrlichová, Alžběta Spálenková, Ivona Krus, Simona Šůsová, Viktor Hlaváč, Vlasta Němcová, Renata Koževnikovová, Markéta Trnková, David Vrána, Jiří Gatěk, Kateřina Kopečková, Marcela Mrhalová, Soňa Měšťáková, Pavel Souček   +14 more
wiley   +1 more source

The Role of the Cullin-5 E3 Ubiquitin Ligase in the Regulation of Insulin Receptor Substrate-1

Biochemistry Research International, 2012
Background. SOCS proteins are known to negatively regulate insulin signaling by inhibiting insulin receptor substrate-1 (IRS1). IRS1 has been reported to be a substrate for ubiquitin-dependent proteasomal degradation.
Christine Zhiwen Hu, Jaswinder K. Sethi, Thilo Hagen   +2 more
doaj   +1 more source

Sec16A, a key protein in COPII vesicle formation, regulates the stability and localization of the novel ubiquitin ligase RNF183. [PDF]

PLoS ONE, 2018
We identified 37 ubiquitin ligases containing RING-finger and transmembrane domains. Of these, we found that RNF183 is abundantly expressed in the kidney. RNF183 predominantly localizes to the endoplasmic reticulum (ER), Golgi, and lysosome.
Yan Wu, Xiao Peng Guo, Soshi Kanemoto, Yujiro Maeoka, Atsushi Saito, Rie Asada, Koji Matsuhisa, Yosuke Ohtake, Kazunori Imaizumi, Masayuki Kaneko   +9 more
doaj   +1 more source

Development of Protacs to Target Cancer-promoting Proteins for Ubiquitination and Degradation [PDF]

, 2003
The proteome contains hundreds of proteins that in theory could be excellent therapeutic targets for the treatment of human diseases. However, many of these proteins are from functional classes that have never been validated as viable candidates for the ...
Crews, Craig M., Deshaies, Raymond J., Kim, Kyung B., Ransick, Andy, Sakamoto, Kathleen M., Stein, Bernd, Verma, Rati   +6 more
core   +1 more source

Mammalian HECT ubiquitin-protein ligases: Biological and pathophysiological aspects

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2014
Members of the HECT family of E3 ubiquitin-protein ligases are characterized by a C-terminal HECT domain that catalyzes the covalent attachment of ubiquitin to substrate proteins and by N-terminal extensions of variable length and domain architecture that determine the substrate spectrum of a respective HECT E3.
Martin Scheffner, Sharad Kumar, Sharad Kumar, Sharad Kumar   +3 more
openaire   +6 more sources

The protein substrate binding site of the ubiquitin-protein ligase system. [PDF]

Journal of Biological Chemistry, 1986
In order to gain insight into the mechanisms that determine the selectivity of the ubiquitin proteolytic pathway, the protein substrate binding site of the ubiquitin-protein ligase system was identified and examined. Previous studies had shown that the ligase system consists of three components: a ubiquitin-activating enzyme (E1), ubiquitin-carrier ...
Hannah Heller, Avram Hershko, Esther Eytan, Yuval Reiss   +3 more
openaire   +2 more sources

β‐TrCP overexpression enhances cisplatin sensitivity by depleting BRCA1

Molecular Oncology, EarlyView.
Low levels of β‐TrCP (Panel A) allow the accumulation of BRCA1 and CtIP, which facilitate the repair of cisplatin‐induced DNA damage via homologous recombination (HR) and promote tumor cell survival. In contrast, high β‐TrCP expression (Panel B) leads to BRCA1 and CtIP degradation, impairing HR repair, resulting in persistent DNA damage and apoptosis ...
Rocío Jiménez‐Guerrero, Alejandro Belmonte‐Fernández, Mónica González‐Moreno, Laura Rodríguez‐Cordero, Begoña Pérez‐Valderrama, Joaquín Herrero‐Ruíz, Francisco Romero, Carmen Sáez, Miguel Á. Japón   +8 more
wiley   +1 more source