Results 31 to 40 of about 3,365,420 (200)

S-Palmitoylation of Synaptic Proteins in Neuronal Plasticity in Normal and Pathological Brains

open access: yesCells, 2023
Protein lipidation is a common post-translational modification of proteins that plays an important role in human physiology and pathology. One form of protein lipidation, S-palmitoylation, involves the addition of a 16-carbon fatty acid (palmitate) onto ...
Anna Buszka   +4 more
doaj   +1 more source

Protein S -palmitoylation in immunity [PDF]

open access: yesOpen Biology, 2021
S -palmitoylation is a reversible posttranslational lipid modification of proteins. It controls protein activity, stability, trafficking and protein–protein interactions. Recent global profiling of immune cells and targeted analysis have identified many S -palmitoylated ...
Tandrila Das   +2 more
openaire   +3 more sources

Palmitoylation-induced aggregation of cysteine-string protein mutants that cause neuronal ceroid lipofuscinosis [PDF]

open access: yes, 2012
Recently, mutations in the DNAJC5 gene encoding cysteine-string protein alpha (CSPα) were identified to cause the neurodegenerative disorder adult-onset neuronal ceroid lipofuscinosis.
Greaves, J.   +11 more
core   +1 more source

Proteomic identification of palmitoylated proteins [PDF]

open access: yesMethods, 2006
A proteomic method that purifies and identifies palmitoylated proteins from complex protein extracts is described. Using the fatty acid exchange labeling chemistry (described in the preceding report), palmitoyl modifications are exchanged for biotinylated compounds, allowing the subset of palmitoyl-proteins to be affinity-purified and then identified ...
Amy F, Roth   +4 more
openaire   +2 more sources

PPT1 regulation of HSP90α depalmitoylation participates in the pathogenesis of hyperandrogenism

open access: yesiScience, 2023
Summary: Ovarian granulosa cells (GCs) in the follicle are the important mediator of steroidogenesis and foster oocyte maturation. Evidences suggested that the function of GCs could be regulated by S-palmitoylation.
Tongmin Xue   +13 more
doaj   +1 more source

Biochemical Characterization of a Palmitoyl Acyltransferase Activity That Palmitoylates Myristoylated Proteins [PDF]

open access: yesJournal of Biological Chemistry, 1995
Dynamic regulation of signal transduction by reversible palmitoylation-depalmitoylation cycles has been recently described. However, further understanding of fatty acylation reactions has been hampered by our lack of knowledge about the specific transferases and thioesterases involved.
L, Berthiaume, M D, Resh
openaire   +2 more sources

Function of Protein S-Palmitoylation in Immunity and Immune-Related Diseases

open access: yesFrontiers in Immunology, 2021
Protein S-palmitoylation is a covalent and reversible lipid modification that specifically targets cysteine residues within many eukaryotic proteins. In mammalian cells, the ubiquitous palmitoyltransferases (PATs) and serine hydrolases, including acyl ...
Yuqi Zhang   +4 more
doaj   +1 more source

Palmitoylation of virus proteins [PDF]

open access: yesBiology of the Cell, 2012
AbstractThe article summarises the results of more than 30 years of research on palmitoylation (S‐acylation) of viral proteins, the post‐translational attachment of fatty acids to cysteine residues of integral and peripheral membrane proteins. Analysing viral proteins is not only important to characterise the cellular pathogens but also instrumental to
openaire   +2 more sources

Palmitoylated proteins: purification and identification [PDF]

open access: yesNature Protocols, 2007
This proteomic protocol purifies and identifies palmitoylated proteins (i.e., S-acylated proteins) from complex protein extracts. The method relies on an acyl-biotinyl exchange chemistry in which biotin moieties are substituted for the thioester-linked protein acyl-modifications through a sequence of three in vitro chemical steps: (i) blockade of free ...
Junmei, Wan   +3 more
openaire   +2 more sources

Post-translational palmitoylation of metabolic proteins

open access: yesFrontiers in Physiology, 2023
Numerous cellular proteins are post-translationally modified by addition of a lipid group to their structure, which dynamically influences the proteome by increasing hydrophobicity of proteins often impacting protein conformation, localization, stability,
Kaitlyn M. J. H. Dennis, Lisa C. Heather
doaj   +1 more source

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