Results 31 to 40 of about 17,753 (213)

Structural basis for Cul3 protein assembly with the BTB-Kelch family of E3 ubiquitin ligases. [PDF]

open access: yes, 2013
Cullin-RING ligases are multisubunit E3 ubiquitin ligases that recruit substrate-specific adaptors to catalyze protein ubiquitylation. Cul3-based Cullin-RING ligases are uniquely associated with BTB adaptors that incorporate homodimerization, Cul3 ...
Bullock, AN   +30 more
core   +1 more source

Trim17, novel E3 ubiquitin-ligase, initiates neuronal apoptosis [PDF]

open access: yes, 2010
Accumulating data indicate that the ubiquitin-proteasome system controls apoptosis by regulating the level and the function of key regulatory proteins. In this study, we identified Trim17, a member of the TRIM/RBCC protein family, as one of the critical ...
Rahmeh, R   +47 more
core   +1 more source

CTLs, a new class of RING-H2 ubiquitin ligases uncovered by YEELL, a motif close to the RING domain that is present across eukaryotes. [PDF]

open access: yesPLoS ONE, 2018
RING ubiquitin E3 ligases enclose a RING domain for ubiquitin ligase activity and associated domains and/or conserved motifs outside the RING domain that collectively facilitate their classification and usually reveal some of key information related to ...
Domingo Jiménez-López   +4 more
doaj   +1 more source

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

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

How to Inactivate Human Ubiquitin E3 Ligases by Mutation

open access: yesFrontiers in Cell and Developmental Biology, 2020
E3 ubiquitin ligases are the ultimate enzymes involved in the transfer of ubiquitin to substrate proteins, a process that determines the fate of the modified protein.
Cristina Garcia-Barcena   +4 more
doaj   +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 fanconi anemia DNA repair pathway is regulated by an interaction between ubiquitin and the E2-like fold domain of FANCL [PDF]

open access: yes, 2015
The Fanconi Anemia (FA) DNA repair pathway is essential for the recognition and repair of DNA interstrand crosslinks (ICL). Inefficient repair of these ICL can lead to leukemia and bone marrow failure.
Howard, Mark J.   +8 more
core   +1 more source

Unbiased identification of substrates for the Epac1-inducible E3 ubiquitin ligase component SOCS-3 [PDF]

open access: yes, 2012
The anti-inflammatory effects of the prototypical second messenger cAMP have been extensively documented in multiple cell types. One mechanism by which these effects are achieved is via Epac1 (exchange protein directly activated by cAMP 1)-dependent ...
Williams, Jamie J.L., Palmer, Timothy M.
core   +1 more source

MAGE-A cancer/testis antigens inhibit MDM2 ubiquitylation function and promote increased levels of MDM4 [PDF]

open access: yes, 2015
Melanoma antigen A (MAGE-A) proteins comprise a structurally and biochemically similar sub-family of Cancer/Testis antigens that are expressed in many cancer types and are thought to contribute actively to malignancy.
Susan E. Bray (264528)   +41 more
core   +1 more source

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