Results 21 to 30 of about 120,302 (311)

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

Identification of a MicroRNA‐E3 Ubiquitin Ligase Regulatory Network for Hepatocyte Death in Alcohol‐Associated Hepatitis

Hepatology Communications, 2021
We aimed to identify a microRNA (miRNA)‐E3 ubiquitin ligase regulatory network for protein substrates enriched in cell death pathways and investigate the underlying molecular mechanisms in alcohol‐associated hepatitis (AH).
Xiude Fan, Jianguo Wu, Kyle L. Poulsen, Adam Kim, Xiaoqin Wu, Emily Huang, Tatsunori Miyata, Carlos Sanz‐Garcia, Laura E. Nagy   +8 more
doaj   +1 more source

Research progress of E3 ubiquitin ligase regulating biological behavior of human placental trophoblast cells

Frontiers in Endocrinology, 2023
E3 ubiquitin ligases are important components of the ubiquitin protease system. This family includes many proteins, which can catalyze the ubiquitination of a variety of protein substrates and promote the degradation of them by the proteasome system ...
Jun Feng, Huimei Yin, Baturuhu, Yonghui Dai, Fuxiao Dai, Junjun Xu, Zhili Chen, Yanyan Liu   +7 more
doaj   +1 more source

Structural studies of the coiled-coil domain of TRIM75 reveal a tetramer architecture facilitating its E3 ligase complex

Computational and Structural Biotechnology Journal, 2022
Protein ubiquitination plays a vital role in controlling the degradation of intracellular proteins and in regulating cell signaling pathways. Functionally, E3 ubiquitin ligases control the transfer of ubiquitin to the target substrates. As a major family
Xiaohua Lou, Binbin Ma, Yuan Zhuang, Xiang Xiao, Laurie J. Minze, Junji Xing, Zhiqiang Zhang, Xian C. Li   +7 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

BRCA1 is a histone-H2A-specific ubiquitin ligase [PDF]

, 2014
The RING domain proteins BRCA1 and BARD1 comprise a heterodimeric ubiquitin (E3) ligase that is required for the accumulation of ubiquitin conjugates at sites of DNA damage and for silencing at DNA satellite repeat regions. Despite its links to chromatin,
Donna L. Mallery, Mallery, D., Conor Larkin, Huang, Jeffrey T.J., Kalb, R., Kevin Hiom, Kalb, Reinhard, Reinhard Kalb, Huang, Jeffrey T. J.; id_orcid, Hiom, Kevin, Hiom, K., Jeffrey T.J. Huang, Larkin, C., Mallery, Donna L., Larkin, Conor, Huang, J.   +15 more
core   +1 more source

A Comprehensive Atlas of E3 Ubiquitin Ligase Mutations in Neurological Disorders

Frontiers in Genetics, 2018
Protein ubiquitination is a posttranslational modification that plays an integral part in mediating diverse cellular functions. The process of protein ubiquitination requires an enzymatic cascade that consists of a ubiquitin activating enzyme (E1 ...
Arlene J. George, Yarely C. Hoffiz, Antoinette J. Charles, Ying Zhu, Angela M. Mabb   +4 more
doaj   +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

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, Surendra K. Jain, Larry A. Walker, Babu L. Tekwani   +3 more
doaj   +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