Results 1 to 10 of about 24,596 (118)

Identification of E3 ligase substrates and PROTAC-induced ubiquitylation sites using proximity-based identification of ubiquitin sites (PrIUS) [PDF]

open access: yesCommunications Biology
The ubiquitin system regulates virtually all cellular processes, yet the vast majority of ubiquitylation sites identified in the human proteome cannot be attributed to specific E3 ligases.
Tanner M. Tessier   +9 more
doaj   +2 more sources

Aging and diet alter the protein ubiquitylation landscape in the mouse brain

open access: yesNature Communications
Post-translational modifications (PTMs) regulate protein homeostasis, but how aging impacts PTMs remains unclear. Here, we used mass spectrometry to reveal changes in hundreds of protein ubiquitylation, acetylation, and phosphorylation sites in the mouse
Antonio Marino   +7 more
doaj   +2 more sources

Pacritinib abrogates the lupus phenotype in ABIN1[D485N] mice

open access: yesLupus Science and Medicine, 2023
Objective The aim of the study was to investigate whether the IRAK1/JAK2/Flt3 inhibitor pacritinib prevents disease development in the lupus-prone ABIN1[D485N] knock-in mouse.Methods ABIN1[D485N] knock-in mice aged 8 weeks were fed for 10 weeks on a diet
Philip Cohen   +4 more
doaj   +1 more source

IL-15 and PIM kinases direct the metabolic programming of intestinal intraepithelial lymphocytes

open access: yesNature Communications, 2021
Intraepithelial lymphocytes (IEL) respond to IL-15 complexed with IL-15Ra but how this intrinsically affects IEL is unclear. Here the authors use proteomics analyses of the main mouse IEL subsets and identify PIM kinases as essential for IEL ...
Olivia J. James   +7 more
doaj   +1 more source

Pathogenic FAM83G palmoplantar keratoderma mutations inhibit the PAWS1:CK1α association and attenuate Wnt signalling. [version 2; peer review: 2 approved]

open access: yesWellcome Open Research, 2020
Background: Two recessive mutations in the FAM83G gene, causing A34E and R52P amino acid substitutions in the DUF1669 domain of the PAWS1 protein, are associated with palmoplantar keratoderma (PPK) in humans and dogs respectively.
Kevin Z.L. Wu   +9 more
doaj   +1 more source

A novel RLIM/RNF12 variant disrupts protein stability and function to cause severe Tonne–Kalscheuer syndrome

open access: yesScientific Reports, 2021
Tonne–Kalscheuer syndrome (TOKAS) is an X-linked intellectual disability syndrome associated with variable clinical features including craniofacial abnormalities, hypogenitalism and diaphragmatic hernia.
Francisco Bustos   +8 more
doaj   +1 more source

CMG helicase disassembly is controlled by replication fork DNA, replisome components and a ubiquitin threshold

open access: yeseLife, 2020
The eukaryotic replisome assembles around the CMG helicase, which stably associates with DNA replication forks throughout elongation. When replication terminates, CMG is ubiquitylated on its Mcm7 subunit and disassembled by the Cdc48/p97 ATPase.
Tom D Deegan   +4 more
doaj   +1 more source

Pathogenic FAM83G palmoplantar keratoderma mutations inhibit the PAWS1:CK1α association and attenuate Wnt signalling. [version 1; peer review: 2 approved]

open access: yesWellcome Open Research, 2019
Background: Two recessive mutations in the FAM83G gene, causing A34E and R52P amino acid substitutions in the DUF1669 domain of the PAWS1 protein, are associated with palmoplantar keratoderma (PPK) in humans and dogs respectively.
Kevin Z.L. Wu   +9 more
doaj   +1 more source

Mapping of a N-terminal α-helix domain required for human PINK1 stabilization, Serine228 autophosphorylation and activation in cells

open access: yesOpen Biology, 2022
Autosomal recessive mutations in the PINK1 gene are causal for Parkinson's disease (PD). PINK1 encodes a mitochondrial localized protein kinase that is a master-regulator of mitochondrial quality control pathways.
Poonam Kakade   +14 more
doaj   +1 more source

Remodeling Membrane Binding by Mono-Ubiquitylation

open access: yesBiomolecules, 2019
Ubiquitin (Ub) receptors respond to ubiquitylation signals. They bind ubiquitylated substrates and exert their activity in situ. Intriguingly, Ub receptors themselves undergo rapid ubiquitylation and deubiquitylation.
Neta Tanner   +3 more
doaj   +1 more source

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