Results 21 to 30 of about 349,913 (393)
Role of Nse1 Subunit of SMC5/6 Complex as a Ubiquitin Ligase
Cells, 2022 Structural Maintenance of Chromosomes (SMC) complexes are important for many aspects of the chromosomal organization. Unlike cohesin and condensin, the SMC5/6 complex contains a variant RING domain carried by its Nse1 subunit.
Peter Kolesar +4 more
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A Ubiquitin-like Protein Unleashes Ubiquitin Ligases [PDF]
Cell, 2008 Modification of cullin-RING ubiquitin ligases by the ubiquitin-like molecule Nedd8 promotes substrate ubiquitination. A crystal structure of a cullin modified by Nedd8 recently reported in Cell (Duda et al., 2008) and a biochemical study in Molecular Cell (Saha and Deshaies, 2008) reveal the dramatic impact on the ligase machinery by conjugation of ...
Saifee, Nabiha Huq, Zheng, Ning
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G3BP1 modulates SPOP to promote prostate tumorigenesis
Molecular & Cellular Oncology, 2022 Speckle-type POZ protein (SPOP), a Cullin 3-based ubiquitin ligase (CUL3SPOP), acts as a prostate-specific tumor suppressor. Loss-of-function mutations in SPOP occur in 10% of primary prostate cancer with a high Gleason grade and poor prognosis. However,
Chandrani Mukhopadhyay, Pengbo Zhou
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Trim25 restricts rabies virus replication by destabilizing phosphoprotein
Cell Insight, 2022 Tripartite motif-containing protein 25 (Trim25) is an E3 ubiquitin ligase that activates retinoid acid-inducible gene I (RIG-I) and promotes the antiviral interferon response.
Yueming Yuan +11 more
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Cbl-c ubiquitin ligase activity is increased via the interaction of its RING finger domain with a LIM domain of the paxillin homolog, Hic 5. [PDF]
PLoS ONE, 2012 Cbl proteins (Cbl, Cbl-b and Cbl-c) are ubiquitin ligases that are critical regulators of tyrosine kinase signaling. In this study we identify a new Cbl-c interacting protein, Hydrogen peroxide Induced Construct 5 (Hic-5).
Philip E Ryan +5 more
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Stealing the spotlight: CUL4-DDB1 ubiquitin ligase docks WD40-repeat proteins to destroy
Cell Division, 2007 Recent investigation of Cullin 4 (CUL4) has ushered this class of multiprotein ubiquitin E3 ligases to center stage as critical regulators of diverse processes including cell cycle regulation, developmental patterning, DNA replication, DNA damage and ...
Zhang Hui, Higa Leigh
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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.
Alejandro Rojas-Fernandez +64 more
core +3 more sources
Inhibitors of ubiquitin E3 ligase as potential new antimalarial drug leads
BMC Pharmacology and Toxicology, 2017 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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PLoS Genetics, 2023 The tumor suppressor BRCA1-BARD1 complex regulates many cellular processes; of critical importance to its tumor suppressor function is its role in genome integrity.
Qianyan Li +4 more
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Dysregulation of ubiquitin ligases in cancer [PDF]
Drug Resistance Updates, 2015 Ubiquitin ligases (UBLs) are critical components of the ubiquitin proteasome system (UPS), which governs fundamental processes regulating normal cellular homeostasis, metabolism, and cell cycle in response to external stress signals and DNA damage. Among multiple steps of the UPS system required to regulate protein ubiquitination and stability, UBLs ...
Jianfei, Qi, Ze'ev A, Ronai
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