Results 11 to 20 of about 349,913 (393)
Self‐regulating ubiquitin ligases [PDF]
The EMBO Journal, 2017 Occasional auto‐modification of ubiquitin ligases typically leads to their proteasomal destruction, but new findings published in The EMBO Journal now show that in the case of Rsp5/Nedd4, auto‐ubiquitylation instead triggers oligomerization and concomitant reduction of ligase activity. This novel mechanism therefore creates silenced ligases that remain
Spencer Hill, Gary Kleiger
openalex +3 more sources
HERC Ubiquitin Ligases in Cancer [PDF]
Cancers, 2020 HERC proteins are ubiquitin E3 ligases of the HECT family. The HERC subfamily is composed of six members classified by size into large (HERC1 and HERC2) and small (HERC3–HERC6). HERC family ubiquitin ligases regulate important cellular processes, such as neurodevelopment, DNA damage response, cell proliferation, cell migration, and immune responses ...
Joan Sala-Gaston +7 more
openaire +4 more sources
Ubiquitin-protein ligases [PDF]
Journal of Cell Science, 2004 Post-translational covalent tagging of proteins with the 76-residue protein ubiquitin (Ub) serves many functions. Polyubiquitylated proteins are directed to the large multi-component, multi-catalytic protease the 26S proteasome.
P A, Robinson, H C, Ardley
openaire +2 more sources
Ubiquitin ligases and beyond [PDF]
BMC Biology, 2012 In a review published in 2004 [1] and that still repays reading today, Cecile Pickart traced the evolution of research on ubiquitination from its origins in the proteasomal degradation of proteins through the revelation that it has a central role in cell cycle regulation and the recognition of regulatory roles for ubiquitin in intracellular membrane ...
Đikić, Ivan, Robertson, Miranda
openaire +5 more sources
Biomolecules, 2021 Cellular homeostasis depends on robust protein quality control (PQC) pathways that discern misfolded proteins from functional ones in the cell. One major branch of PQC involves the controlled degradation of misfolded proteins by the ubiquitin-proteasome ...
Rebeca Ibarra +4 more
doaj +1 more source
The ZSWIM8 ubiquitin ligase mediates target-directed microRNA degradation
Science, 2020 Turning the tables on microRNA decay MicroRNAs help to regulate many genes in animal cells. Each microRNA associates with an Argonaute (AGO) protein, forming a complex in which the microRNA pairs with a messenger RNA (mRNA) target and AGO recruits ...
Charlie Y. Shi +5 more
semanticscholar +1 more source
Ubiquitin ligase activity inhibits Cdk5 to control axon termination.
PLoS Genetics, 2022 The Cdk5 kinase plays prominent roles in nervous system development, plasticity, behavior and disease. It also has important, non-neuronal functions in cancer, the immune system and insulin secretion.
Muriel Desbois +5 more
doaj +1 more source
Plants, 2023 Plant U-box E3 ubiquitin ligases (PUBs) play an important role in growth, development, and stress responses in many species. However, the characteristics of U-box E3 ubiquitin ligase genes in cabbage (Brassica oleracea var.
Peiwen Wang +7 more
doaj +1 more source
A ubiquitin ligase mediates target-directed microRNA decay independently of tailing and trimming
Science, 2020 Turning the tables on microRNA decay MicroRNAs help to regulate many genes in animal cells. Each microRNA associates with an Argonaute (AGO) protein, forming a complex in which the microRNA pairs with a messenger RNA (mRNA) target and AGO recruits ...
Jaeil Han +5 more
semanticscholar +1 more source
Ubiquitylation in immune disorders and cancer: from molecular mechanisms to therapeutic implications [PDF]
, 2012 Conjugation of ubiquitin to proteins (ubiquitylation) has emerged to be one of the most crucial post-translational modifications controlling virtually all cellular processes.
Fulda, Simone +2 more
core +2 more sources