Results 51 to 60 of about 327,531 (416)

RBR E3 ubiquitin ligases: new structures, new insights, new questions [PDF]

open access: yes, 2014
The RBR (RING-BetweenRING-RING) or TRIAD [two RING fingers and a DRIL (double RING finger linked)] E3 ubiquitin ligases comprise a group of 12 complex multidomain enzymes.
Shaw, Gary S.   +2 more
core   +1 more source

The E3 ligase HOIL-1 catalyses ester bond formation between ubiquitin and components of the Myddosome in mammalian cells

open access: yesProceedings of the National Academy of Sciences of the United States of America, 2019
Significance The formation of isopeptide bonds between the C-terminal carboxylate of ubiquitin and ε-amino groups of lysine residues on another protein is a major mechanism for regulating protein function. Ubiquitin can also form peptide bonds with the N-
Ian R. Kelsall   +4 more
semanticscholar   +1 more source

SUMO-targeted ubiquitin ligases

open access: yesBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2014
Covalent posttranslational modification with SUMO (small ubiquitin-related modifier) modulates functions of a wide range of proteins in eukaryotic cells. Sumoylation affects the activity, interaction properties, subcellular localization and the stability of its substrate proteins.
Sriramachandran, Annie M.   +1 more
openaire   +3 more sources

Linear ubiquitin chains: enzymes, mechanisms and biology [PDF]

open access: yesOpen Biology, 2017
Ubiquitination is a versatile post-translational modification that regulates a multitude of cellular processes. Its versatility is based on the ability of ubiquitin to form multiple types of polyubiquitin chains, which are recognized by specific ...
Katrin Rittinger, Fumiyo Ikeda
doaj   +1 more source

RMND5 from Xenopus laevis is an E3 ubiquitin-ligase and functions in early embryonic forebrain development. [PDF]

open access: yesPLoS ONE, 2015
In Saccharomyces cerevisiae the Gid-complex functions as an ubiquitin-ligase complex that regulates the metabolic switch between glycolysis and gluconeogenesis.
Thorsten Pfirrmann   +5 more
doaj   +1 more source

A yeast cell cycle pulse generator model shows consistency with multiple oscillatory and checkpoint mutant datasets [PDF]

open access: yesarXiv, 2023
The regulatory mechanisms driving progression of the yeast cell cycle appears to be comprised of an interacting network of transcription factors (TFs), cyclin-dependent kinases (CDK) and ubiquitin ligases. From a systems perspective the controlling regulatory network must produce robust periodic behavior during proliferative phases, but have the ...
arxiv  

The E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by promoting proteasomal degradation of NLRP3

open access: yesNature Communications, 2016
The NLRP3 inflammasome has a fundamental role in host defence against microbial pathogens and its deregulation may cause diverse inflammatory diseases. NLRP3 protein expression is a rate-limiting step for inflammasome activation, thus its expression must
Hui Song   +10 more
semanticscholar   +1 more source

Mechanical unfolding and refolding pathways of ubiquitin [PDF]

open access: yesPhys. Rev. Lett. 100, 158104 (2008), 2008
Mechanical unfolding and refolding of ubiquitin are studied by Monte Carlo simulations of a Go model with binary variables. The exponential dependence of the time constants on the force is verified, and folding and unfolding lengths are computed, with good agreement with experimental results. Furthermore, the model exhibits intermediate kinetic states,
arxiv   +1 more source

Differential regulation of RNF8-mediated Lys48- and Lys63-based poly-ubiquitylation [PDF]

open access: yes, 2012
Pairing of a given E3 ubiquitin ligase with different E2s allows synthesis of ubiquitin conjugates of different topologies. While this phenomenon contributes to functional diversity, it remains largely unknown how a single E3 ubiquitin ligase recognizes ...
Ching, YP   +6 more
core   +1 more source

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

open access: yesNature Communications, 2017
The ubiquitination mediated by ubiquitin activating enzyme (E1), ubiquitin conjugating enzyme (E2), and ubiquitin ligase (E3) cascade is crucial to protein degradation, transcription regulation, and cell signaling in eukaryotic cells.
Yang Li   +12 more
semanticscholar   +1 more source

Home - About - Disclaimer - Privacy