Results 41 to 50 of about 21,089,371 (171)

Palmitoylation and depalmitoylation defects [PDF]

open access: yes, 2021
Palmitoylation describes the enzymatic attachment of a 16-carbon atom fatty acid to a target protein. Such lipidation events occur in all eukaryotes and can be of reversible (S-palmitoylation) or irreversible (N-palmitoylation) nature.
Hornemann, Thorsten
core  

Emerging roles for protein S-palmitoylation in Toxoplasma biology

open access: yesInternational Journal for Parasitology, 2014
Post-translational modifications are refined, rapidly responsive and powerful ways to modulate protein function. Among post-translational modifications, acylation is now emerging as a widespread modification exploited by eukaryotes, bacteria and viruses to control biological processes.
Frenal, Karine   +2 more
openaire   +5 more sources

Differential S-palmitoylation of the human and rodent β3-adrenergic receptors [PDF]

open access: yesJournal of Biological Chemistry, 2019
With few reported exceptions, G protein-coupled receptors (GPCRs) are modified by Cys palmitoylation (S-palmitoylation). In multiple GPCRs, S-palmitoylation targets a canonical site within the C-terminal cytoplasmic tail adjacent to the C terminus of the seventh transmembrane domain, but modification of additional sites is exemplified by the β ...
Naoko Adachi   +5 more
openaire   +2 more sources

The Roles of Protein S-Palmitoylation in Cancers: From Dynamic Modulation to Therapeutic Potential

open access: yesCancer Communications
Protein S-palmitoylation is a highly conserved posttranslational lipid modification that occurs on cysteine residues and critically influences protein maturation, subcellular localization, trafficking, and stability. Owing to its unique reversibility and
Haonan Zheng   +7 more
doaj   +1 more source

S-palmitoylation regulates AMPA receptors trafficking and function: a novel insight into synaptic regulation and therapeutics

open access: yesActa Pharmaceutica Sinica B, 2015
Glutamate acting on AMPA-type ionotropic glutamate receptor (AMPAR) mediates the majority of fast excitatory synaptic transmission in the mammalian central nervous system.
Jun Han   +3 more
doaj   +1 more source

Evolutionarily Established Palmitoylation-Dependent Regulatory Mechanisms of the Vertebrate Glutamatergic Synapse and Diseases Caused by Their Disruption

open access: yesFrontiers in Molecular Neuroscience, 2021
Glutamate is the major excitatory neurotransmitter in the vertebrate brain and various modifications have been established in the glutamatergic synapses.
Takashi Hayashi
doaj   +1 more source

The Unconventional Role of ABHD17A in Increasing the S-Palmitoylation and Antiviral Activity of IFITM1 by Downregulating ABHD16A

open access: yesBiomolecules
The broad-spectrum antiviral functions of interferon-inducible transmembrane 1 (IFITM1) rely on S-palmitoylation post-translational modification.
Xuemeng Shi   +11 more
doaj   +1 more source

Targeted Degradation of STING by a Neutrophil Membrane‐Coated Nanoplatform Suppresses Microglial Pyroptosis After Subarachnoid Hemorrhage

open access: yesAdvanced Science, EarlyView.
MG1@NM‐Px serves as a microglia‐targeted STING‐degrading nanoplatform for subarachnoid hemorrhage. Following systemic administration, it crosses the blood–brain barrier and accumulates in activated microglia. STP1‐mediated STING ubiquitination and degradation suppress MAPK/inflammasome signaling, GSDME‐mediated pyroptosis, and IL‐1β release, revealing ...
Ruotian Zhang   +13 more
wiley   +1 more source

Glycosylation and S-palmitoylation regulate SARS-CoV-2 spike protein intracellular trafficking

open access: yesiScience, 2022
Summary: Post-translational modifications (PTMs), such as glycosylation and palmitoylation, are critical to protein folding, stability, intracellular trafficking, and function.
Chih-Feng Tien   +13 more
doaj   +1 more source

Membrane‐Active Peptide Protects Against Inflammation by Targeting NLRP3 Activation at the Trans‐Golgi Network

open access: yesAdvanced Science, EarlyView.
The membrane‐active peptide Pep19‐2.5 reduces harmful inflammation by blocking activation of the NLRP3 inflammasome at trans‐Golgi network membranes. By targeting key membrane interactions, Pep19‐2.5 suppresses inflammatory IL‐1β production and alleviates allergic airway inflammation in mice, leading to reduced immune cell infiltration and improved ...
Jonas Engelhardt   +16 more
wiley   +1 more source

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