Results 31 to 40 of about 23,719 (175)
Multiple UBX proteins reduce the ubiquitin threshold of the mammalian p97-UFD1-NPL4 unfoldase
eLife, 2022 The p97/Cdc48 ATPase and its ubiquitin receptors Ufd1-Npl4 are essential to unfold ubiquitylated proteins in many areas of eukaryotic cell biology.
Ryo Fujisawa +2 more
doaj +1 more source
Ubiquitylation of DNA polymerase λ
FEBS Letters, 2011 DNA polymerase (pol) λ, one of the 15 cellular pols, belongs to the X family. It is a small 575 amino‐acid protein containing a polymerase, a dRP‐lyase, a proline/serine rich and a BRCT domain. Pol λ shows various enzymatic activities including DNA polymerization, terminal transferase and dRP‐lyase.
Markkanen Enni +3 more
openaire +3 more sources
Determination of VPS34/PIK3C3 Activity in vitro Utilising 32P-γATP
Bio-Protocol, 2016 VPS34 is the only class III phosphatidylinositol-3-kinase (PI3K) in mammalian cells and produces the vast majority of cellular phosphatidylinositol-3-phosphate [PI(3)P].
Michael Munson, Ian Ganley
doaj +1 more source
Disorders of ubiquitylation: unchained inflammation
Nature Reviews Rheumatology, 2022 Ubiquitylation is an essential post-translational modification that regulates intracellular signalling networks by triggering proteasomal substrate degradation, changing the activity of substrates or mediating changes in proteins that interact with substrates.
David B. Beck +3 more
openaire +2 more sources
Nature Communications, 2023 Ubiquitin widely modifies proteins, thereby regulating most cellular functions. The complexity of ubiquitin signalling necessitates unbiased methods enabling global detection of dynamic protein ubiquitylation.
Camilla S. Colding-Christensen +9 more
doaj +1 more source
Neddylation is essential for β-catenin degradation in Wnt signaling pathway
Cell Reports, 2022 Summary: β-Catenin is a central component in the Wnt signaling pathway; its degradation has been tightly connected to ubiquitylation, but it is rarely examined by loss-of-function assays.
Bojun Wang +9 more
doaj +1 more source
Studying Protein Ubiquitylation in Yeast [PDF]
, 2016 Ubiquitylation is a reversible posttranslational modification that is critical for most, if not all, cellular processes and essential for viability. Ubiquitin conjugates to substrate proteins either as a single moiety (monoubiquitylation) or as polymers composed of ubiquitin molecules linked to each other with various topologies and structures ...
Hovsepian, Junie +4 more
openaire +3 more sources
PLoS Genetics, 2017 Apoptosis is an evolutionary conserved cell death mechanism, which requires activation of initiator and effector caspases. The Drosophila initiator caspase Dronc, the ortholog of mammalian Caspase-2 and Caspase-9, has an N-terminal CARD domain that ...
Hatem Elif Kamber Kaya +3 more
doaj +1 more source
Cell wall target fragment discovery using a low‐cost, minimal fragment library
FEBS Letters, EarlyView.LoCoFrag100 is a fragment library made up of 100 different compounds. Similarity between the fragments is minimized and 10 different fragments are mixed into a single cocktail, which is soaked to protein crystals. These crystals are analysed by X‐ray crystallography, revealing the binding modes of the bound fragment ligands.
Kaizhou Yan +5 more
wiley +1 more source
Macromolecular juggling by ubiquitylation enzymes [PDF]
BMC Biology, 2013 Abstract The posttranslational modification of target proteins with ubiquitin and ubiquitin-like proteins is accomplished by the sequential action of E1, E2, and E3 enzymes. Members of the E1 and E3 enzyme families can undergo particularly large conformational changes during their catalytic cycles, involving the remodeling of domain ...
Lorenz, Sonja +3 more
openaire +5 more sources