Results 31 to 40 of about 129,362 (255)

Genome-Wide Identification and Expression of Xenopus F-Box Family of Proteins. [PDF]

open access: yesPLoS ONE, 2015
Protein degradation via the multistep ubiquitin/26S proteasome pathway is a rapid way to alter the protein profile and drive cell processes and developmental changes.
Banu Saritas-Yildirim   +3 more
doaj   +1 more source

Genome-wide analysis of HECT E3 ubiquitin ligase gene family in Solanum lycopersicum

open access: yesScientific Reports, 2021
The E3 ubiquitin ligases have been known to intrigue many researchers to date, due to their heterogenicity and substrate mediation for ubiquitin transfer to the protein.
Bhaskar Sharma   +2 more
doaj   +1 more source

Tau affects P53 function and cell fate during the DNA damage response [PDF]

open access: yesCommunications Biology 3, 245 (2020), 2020
Cells are constantly exposed to DNA damaging insults. To protect the organism, cells developed a complex molecular response coordinated by P53, the master regulator of DNA repair, cell division and cell fate. DNA damage accumulation and abnormal cell fate decision may represent a pathomechanism shared by aging-associated disorders such as cancer and ...
arxiv   +1 more source

Exploring PROTAC cooperativity with coarse-grained alchemical methods [PDF]

open access: yes, 2022
Proteolysis targeting chimera (PROTAC) is a novel drug modality that facilitates the degradation of a target protein by inducing proximity with an E3 ligase. In this work, we present a new computational framework to model the cooperativity between PROTAC-E3 binding and PROTAC-target binding principally through protein-protein interactions (PPIs ...
arxiv   +1 more source

Peroxisomal Ubiquitin-Protein Ligases Peroxin2 and Peroxin10 Have Distinct But Synergistic Roles in Matrix Protein Import and Peroxin5 Retrotranslocation in Arabidopsis1[W][OPEN]

open access: yesPlant Physiology, 2014
Two Arabidopsis membrane peroxins contribute to peroxisomal matrix protein import via distinct roles in recycling and degrading a matrix receptor protein.
Sarah E. Burkhart   +2 more
semanticscholar   +1 more source

RNF125 is a Ubiquitin-Protein Ligase that Promotes p53 Degradation [PDF]

open access: yesCellular Physiology and Biochemistry, 2015
Background/Aims: Although early studies show that Mdm2 is the primary E3 ubiquitin ligase for the p53 tumor suppressor, an increasing amount of data suggests that p53 ubiquitination and degradation are more complex than once thought. Here, we investigated the role of RNF125, a non-Mdm2 ubiquitin-protein ligase, in the regulation of p53.
Zhanhui Miao   +6 more
openaire   +4 more sources

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

Runaway Transition in Irreversible Polymer Condensation with Cyclisation [PDF]

open access: yes, 2022
The process of polymer condensation, i.e. the formation of bonds between reactive end-groups, is ubiquitous in both industry and biology. Here we study generic systems undergoing polymer condensation in competition with cyclisation. Using a generalised Smoluchowski theory, molecular dynamics simulations and experiments using DNA and T4 ligase, we find ...
arxiv   +1 more source

Bacterial pseudokinase catalyzes protein polyglutamylation to inhibit the SidE-family ubiquitin ligases

open access: yesScience, 2019
Divergent protein kinase SidJ is a protein produced by Legionella pneumophila that orchestrates this intracellular pathogen's establishment within the host cell.
M. Black   +6 more
semanticscholar   +1 more source

Ubiquitination, Biotech Startups, and the Future of TRIM Family Proteins: A TRIM-Endous Opportunity

open access: yesCells, 2021
Ubiquitination is a post-translational modification that has pivotal roles in protein degradation and diversified cellular processes, and for more than two decades it has been a subject of interest in the biotech or biopharmaceutical industry. Tripartite
Utsa Bhaduri, Giuseppe Merla
doaj   +1 more source

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