Results 41 to 50 of about 135,650 (305)

Structural basis for the RING-catalyzed synthesis of K63-linked ubiquitin chains [PDF]

open access: yes, 2015
This work was supported by grants from Cancer Research UK (C434/A13067), the Wellcome Trust (098391/Z/12/Z) and Biotechnology and Biological Sciences Research Council (BB/J016004/1).The RING E3 ligase catalysed formation of lysine 63 linked ubiquitin ...
Naismith, Jim   +12 more
core   +1 more source

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

A pathogen type III effector with a novel E3 ubiquitin ligase architecture.

open access: yesPLoS Pathogens, 2013
Type III effectors are virulence factors of Gram-negative bacterial pathogens delivered directly into host cells by the type III secretion nanomachine where they manipulate host cell processes such as the innate immunity and gene expression.
Alexander U Singer   +12 more
doaj   +1 more source

A viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defence [PDF]

open access: yes, 2011
Intrinsic antiviral resistance represents the first line of intracellular defence against virus infection. During herpes simplex virus type-1 (HSV-1) infection this response can lead to the repression of viral gene expression but is counteracted by the ...
Delphine Cuchet-Lourenço   +21 more
core   +1 more source

Genome-wide identification and transcriptome profiling reveal that E3 ubiquitin ligase genes relevant to ethylene, auxin and abscisic acid are differentially expressed in the fruits of melting flesh and stony hard peach varieties

open access: yesBMC Genomics, 2019
Background Ubiquitin ligases (E3) are the enzymes in the ubiquitin/26S proteasome pathway responsible for targeting proteins to the degradation pathway and play major roles in multiple biological activities. However, the E3 family and their functions are
Bin Tan   +10 more
doaj   +1 more source

Trim25 restricts rabies virus replication by destabilizing phosphoprotein

open access: yesCell 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
doaj   +1 more source

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

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

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   +1 more source

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

An integrated bioinformatics platform for investigating the human E3 ubiquitin ligase-substrate interaction network

open access: yesNature Communications, 2017
Protein stability modulation by E3 ubiquitin ligases is an important layer of functional regulation, but screening for E3 ligase-substrate interactions is time-consuming and costly.
Yang Li   +12 more
doaj   +1 more source

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