Results 41 to 50 of about 49,650 (285)

AIRE Functions As an E3 Ubiquitin Ligase [PDF]

The Journal of Experimental Medicine, 2004
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, Hatakeyama, Shigetsugu, Matsushima, Akemi, Han, Hongwei, Ishido, Satoshi, Hotta, Hak, Kudoh, Jun, Shimizu, Nobuyoshi, Doucas, Vassilis, Nakayama, Keiichi I., Kuroda, Noriyuki, Matsumoto, Mitsuru   +11 more
openaire   +2 more sources

Activation of the E3 ubiquitin ligase Parkin [PDF]

Biochemical Society Transactions, 2015
The PINK1 (phosphatase and tensin homologue-induced putative kinase 1)/Parkin-dependent mitochondrial quality control pathway mediates the clearance of damaged organelles, but appears to be disrupted in Parkinson's disease (PD) [Springer and Kahle (2011) Autophagy 7, 266–278].
Thomas R, Caulfield, Fabienne C, Fiesel, Wolfdieter, Springer   +2 more
openaire   +2 more sources

E3 Ubiquitin Ligases in Breast Cancer Metastasis: A Systematic Review of Pathogenic Functions and Clinical Implications

Frontiers in Oncology, 2021
Female breast cancer has become the most commonly occurring cancer worldwide. Although it has a good prognosis under early diagnosis and appropriate treatment, breast cancer metastasis drastically causes mortality.
Yingshuang Wang, Yingshuang Wang, Jiawen Dai, Jiawen Dai, Youqin Zeng, Youqin Zeng, Jinlin Guo, Jinlin Guo, Jie Lan   +8 more
doaj   +1 more source

WWP2 is an E3 ubiquitin ligase for PTEN [PDF]

Nature Cell Biology, 2011
PTEN, a lipid phosphatase, is one of the most frequently mutated tumour suppressors in human cancer. Several recent studies have highlighted the importance of ubiquitylation in regulating PTEN tumour-suppressor function, but the enzymatic machinery required for PTEN ubiquitylation is not clear.
Subbareddy, Maddika, Sridhar, Kavela, Neelam, Rani, Vivek Reddy, Palicharla, Jenny L, Pokorny, Jann N, Sarkaria, Junjie, Chen   +6 more
openaire   +2 more sources

SUMO chain-induced dimerization activates RNF4 [PDF]

, 2014
Dimeric RING E3 ligases interact with protein substrates and conformationally restrain the ubiquitin-E2-conjugating enzyme thioester complex such that it is primed for catalysis.
Hay, Ronald T, Rojas-Fernandez, Alejandro, Hattersley, Neil, Plechanovová, Anna, Tatham, Michael H, Jaffray, Ellis   +5 more
core   +1 more source

Structure of the Human FANCL RING-Ube2T Complex Reveals Determinants of Cognate E3-E2 Selection [PDF]

, 2014
The combination of an E2 ubiquitin-conjugating enzyme with an E3 ubiquitin-ligase is essential for ubiquitin modification of a substrate. Moreover, the pairing dictates both the substrate choice and the modification type. The molecular details of generic
Miles, Jennifer Anne, Hodson, Charlotte, Purkiss, Andrew, Walden, Helen   +3 more
core   +1 more source

TRIM32 is an E3 ubiquitin ligase for dysbindin [PDF]

Human Molecular Genetics, 2009
Mutations in the gene encoding tripartite motif protein 32 (TRIM32) cause two seemingly diverse diseases: limb-girdle muscular dystrophy type 2H (LGMD2H) or sarcotubular myopathy (STM) and Bardet-Biedl syndrome type 11(BBS11). Although TRIM32 is involved in protein ubiquitination, its substrates and the molecular consequences of disease-causing ...
Locke, Matthew, Tinsley, Caroline L., Benson, Matthew A., Blake, Derek J.   +3 more
openaire   +3 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

The molecular basis of CRL4 ubiquitin ligase architecture, targeting and regulation [PDF]

, 2013
Members of the CUL4-RBX1-DDB1 (CRL4) E3 ubiquitin ligase family regulate multiple cellular processes including development, transcription, and DNA repair.
Fischer, Eric Sebastian
core   +1 more source

Structure of the HHARI catalytic domain shows glimpses of a HECT E3 ligase. [PDF]

PLoS ONE, 2013
The ubiquitin-signaling pathway utilizes E1 activating, E2 conjugating, and E3 ligase enzymes to sequentially transfer the small modifier protein ubiquitin to a substrate protein.
Donald E Spratt, Pascal Mercier, Gary S Shaw   +2 more
doaj   +1 more source