|1.||Sun, Yi: 12 articles (01/2015 - 07/2003)|
|2.||Ohh, Michael: 12 articles (08/2014 - 03/2003)|
|3.||Penninger, Josef M: 11 articles (03/2014 - 02/2005)|
|4.||Tanaka, Keiji: 10 articles (10/2015 - 03/2003)|
|5.||Dawson, Ted M: 10 articles (12/2014 - 05/2004)|
|6.||Boutell, Chris: 9 articles (11/2015 - 01/2002)|
|7.||Brice, Alexis: 9 articles (09/2014 - 06/2003)|
|8.||Jia, Lijun: 8 articles (10/2015 - 01/2009)|
|9.||Wei, Wenyi: 8 articles (09/2015 - 09/2010)|
|10.||Langdon, Wallace Y: 8 articles (03/2015 - 11/2004)|
11/03/2015 - "In this study, we report that SOX10 is a direct substrate of Fbxw7α E3 ubiquitin ligase, a tumor suppressor in multiple cancers. "
01/01/2015 - "Recent studies have shown that WW domain containing E3 ubiquitin protein ligase 1 (WWP1) is frequently amplified in various cancers. "
01/01/2015 - "Although early studies show that Mdm2 is the primary E3 ubiquitin ligase for the p53 tumor suppressor, an increasing amount of data suggests that p53 ubiquitination and degradation are more complex than once thought. "
12/01/2014 - "This study for the first time demonstrated the role of TRIM13, ER resident RING E3 ligase as a novel regulator of NEMO ubiquitination, negative regulator of NF-κB signaling and its role as a tumor suppressor. "
10/30/2014 - "Taken together, our study, using both genetic and pharmaceutical approaches, demonstrates that Sag is essential for embryonic vasculogenesis and tumor angiogenesis, and provides the proof-of-concept evidence that targeting Sag E3 ubiquitin ligase may have clinical value for anti-angiogenesis therapy of human cancer."
05/03/2012 - "The VHL protein is best known as an E3 ubiquitin ligase that targets hypoxia-inducible factor-α (HIF-α), but many diverse, non-canonical cellular functions have also been assigned to VHL, mainly based on studies in cell culture systems. "
10/14/2010 - "In this study we identify PIASy as a specific E3 ligase for hypoxia-induced HIF1α SUMOylation. "
06/16/2015 - "E3 Ubiquitin Ligase VHL Regulates Hypoxia-Inducible Factor-1α to Maintain Regulatory T Cell Stability and Suppressive Capacity."
01/15/2015 - "Thus, we identified Wwox as a novel molecule in the HIF-1α-HDM2 regulatory loop, necessary for the dynamic regulation of the HIF-1α amount, and we suggested that the reduction of endogenous Wwox free pool under hypoxia might also be due to the interaction with HDM2, sequestering the E3 ubiquitin ligase. "
01/01/2015 - "We demonstrate that the E3 ubiquitin ligase SIAH2 stimulates YAP by destabilizing LATS2, a critical component of the Hippo pathway, in response to hypoxia. "
07/08/2015 - "These studies describe an unreported innate immune pathway and suggest that mutation or antagonism of the E3 ligase HECTD2 results in reduced severity of lung inflammation by selectively modulating the abundance of the anti-inflammatory protein PIAS1. "
05/01/2011 - "The results provide a unique model of calcium-regulated intermolecular competition between an E3 ligase subunit and an antagonist that is critically relevant to pneumonia and lipid homeostasis."
07/08/2015 - "We discovered a ubiquitin E3 ligase, HECTD2, which ubiquitinated and mediated the degradation of PIAS1, thus increasing inflammation in an experimental pneumonia model. "
04/24/2014 - "E3 ligase subunit Fbxo15 and PINK1 kinase regulate cardiolipin synthase 1 stability and mitochondrial function in pneumonia."
01/01/2014 - "Lafora disease can be caused by defects in the EPM2A gene, which encodes the laforin protein phosphatase, or in the NHLRC1 gene (also called EPM2B) codifying the malin E3 ubiquitin ligase. "
06/14/2005 - "Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin."
07/01/2012 - "Mutations in either EPM2A, the gene encoding a dual-specificity phosphatase named laforin, or NHLRC1, the gene encoding an E3 ubiquitin ligase named malin, cause Lafora disease in humans. "
12/01/2010 - "Lafora disease is caused by deficiency of either the laforin glycogen phosphatase or the malin E3 ubiquitin ligase. "
07/25/2014 - "Lafora disease is a progressive myoclonus epilepsy caused by mutations in the EPM2A or EPM2B genes that encode a glycogen phosphatase, laforin, and an E3 ubiquitin ligase, malin, respectively. "
|5.||Heart Diseases (Heart Disease)
01/01/2008 - "Appetite for destruction: E3 ubiquitin-ligase protection in cardiac disease."
01/01/2008 - "Therefore, focusing on specific regulatory components of the proteasome, such as members of the E3 ubiquitin-ligase family of proteins, may hold promise for targeted therapeutics of cardiac disease. "
|1.||Proteins (Proteins, Gene)
|3.||Proteasome Endopeptidase Complex (Proteasome)
|4.||Transcription Factors (Transcription Factor)
|5.||Staphylococcal Protein A (A, Protein)
|7.||Vascular Endothelial Growth Factor A (Vascular Endothelial Growth Factor)
|10.||DNA (Deoxyribonucleic Acid)
|2.||Drug Therapy (Chemotherapy)
|5.||Heterologous Transplantation (Xenotransplantation)