Results 31 to 40 of about 149,506 (292)

RING Domain E3 Ubiquitin Ligases

open access: yesAnnual 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.   +1 more
openaire   +3 more sources

Structure of the Human FANCL RING-Ube2T Complex Reveals Determinants of Cognate E3-E2 Selection [PDF]

open access: yes, 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   +3 more
core   +1 more source

Functional Diversity and Structural Disorder in the Human Ubiquitination Pathway [PDF]

open access: yes, 2013
The ubiquitin-proteasome system plays a central role in cellular regulation and protein quality control (PQC). The system is built as a pyramid of increasing complexity, with two E1 (ubiquitin activating), few dozen E2 (ubiquitin conjugating) and several
Mainak Guharoy   +15 more
core   +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

TRIM32 is an E3 ubiquitin ligase for dysbindin [PDF]

open access: yesHuman Molecular Genetics, 2009
Mutations in the gene encoding tripartite motif protein 32 (TRIM32) cause two seemingly diverse diseases: limb-girdle muscular dystrophy type 2H (LGMD2H) or sarcotubular myopathy (STM) and Bardet-Biedl syndrome type 11(BBS11). Although TRIM32 is involved in protein ubiquitination, its substrates and the molecular consequences of disease-causing ...
Locke, Matthew   +3 more
openaire   +3 more sources

E3 ubiquitin ligases in the acute leukemic signaling pathways

open access: yesFrontiers in Physiology, 2022
Acute leukemia is a common hematologic tumor with highly genetic heterogeneity, and many factors are involved in the pathogenesis and drug-resistance mechanism.
Qianru Zhan   +4 more
doaj   +1 more source

Disruption of the autoinhibited state primes the E3 ligase parkin for activation and catalysis [PDF]

open access: yes, 2015
The PARK2 gene is mutated in 50% of autosomal recessive juvenile parkinsonism (ARJP) cases. It encodes parkin, an E3 ubiquitin ligase of the RBR family.
R Julio Martinez‐Torres   +26 more
core   +1 more source

Research Progress on the Role of E3 Ubiquitin Ligases in Regulating the Growth, Development and Stress Response of Fruits and Vegetables [PDF]

open access: yesShipin Kexue
Protein ubiquitination, an important post-translational modification, plays a wide role in the life activities of eukaryotic cells. E3 ubiquitin ligases specifically recognize target proteins in the ubiquitin-proteasome degradation system and play a ...
DING Jun, LI Fujun, LI Xiao’an, ZHANG Xinhua
doaj   +1 more source

Structure of the HHARI catalytic domain shows glimpses of a HECT E3 ligase. [PDF]

open access: yesPLoS 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   +2 more
doaj   +1 more source

Erioflorin stabilizes the tumor suppressor Pdcd4 by inhibiting its interaction with the E3-ligase β-TrCP1 [PDF]

open access: yes, 2012
Loss of the tumor suppressor Pdcd4 was reported for various tumor entities and proposed as a prognostic marker in tumorigenesis. We previously characterized decreased Pdcd4 protein stability in response to mitogenic stimuli, which resulted from p70S6K1 ...
Bernhard Brüne   +35 more
core   +1 more source

Home - About - Disclaimer - Privacy