Results 11 to 20 of about 231,680 (303)

Pseudophosphatase as E3 ubiquitin ligase inhibitor

Science Signaling, 2017
The pseudophosphatase STYX prevents the substrate recognition subunit FBXW7 from binding the catalytic E3 ubiquitin ligase complex.
Nancy R. Gough
core   +3 more sources

Ubiquitin E3 ligase MARCH10 targets influenza hemagglutinin for ubiquitination. [PDF]

Cell Signal
Influenza virus infection damages the airways and can cause acute lung injury. Influenza virus infection remains difficult to combat since treatment is limited to supportive care or antiviral drugs to prevent influenza early in the condition. Influenza hemagglutinin (HA) is the surface glycoprotein that facilitates viral entry by binding to sialic acid-
Tsai M, Koch D, Forchione A, Farkas L, El-Mergawy R, Londino JD, Mallampalli RK.   +6 more
europepmc   +3 more sources

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

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

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

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, 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.   +14 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

RING Domain E3 Ubiquitin Ligases

Annual Review of Biochemistry, 2009
E3 ligases confer specificity to ubiquitination by recognizing target substrates and mediating transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to substrate. The activity of most E3s is specified by a RING domain, which binds to an E2∼ubiquitin thioester and activates discharge of its ubiquitin cargo.
Deshaies, Raymond J., Joazeiro, Claudio A. P.   +1 more
openaire   +3 more sources