Results 11 to 20 of about 223,344 (207)

Pseudophosphatase as E3 ubiquitin ligase inhibitor

open access: yesScience 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]

open access: yesCell 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   +6 more
europepmc   +3 more sources

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

open access: yesComputational 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   +7 more
doaj   +1 more source

Activation of the E3 ubiquitin ligase Parkin [PDF]

open access: yesBiochemical 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   +2 more
openaire   +2 more sources

AIRE Functions As an E3 Ubiquitin Ligase [PDF]

open access: yesThe 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   +11 more
openaire   +2 more sources

Rsp5 Ubiquitin Ligase Is Required for Protein Trafficking in Saccharomyces cerevisiae COPI Mutants [PDF]

open access: yes, 2012
Retrograde trafficking from the Golgi to the endoplasmic reticulum (ER) depends on the formation of vesicles coated with the multiprotein complex COPI.
Joanna Kaminska   +7 more
core   +3 more sources

WWP2 is an E3 ubiquitin ligase for PTEN [PDF]

open access: yesNature 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   +6 more
openaire   +2 more sources

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

open access: yes, 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   +15 more
core   +1 more source

A Comprehensive Atlas of E3 Ubiquitin Ligase Mutations in Neurological Disorders

open access: yesFrontiers 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   +4 more
doaj   +1 more source

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

open access: yes, 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

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