Results 51 to 60 of about 56,029 (251)

Synthesis and properties of lipoamino acid/fatty acid mixtures. Influence of the amphiphilic structure. [PDF]

open access: yes, 2009
The acylation of amino acids by acid chlorides with from 8 to 12 carbon atoms, in alkaline aqueous medium following Shotten-Baumann reaction, results in sodium salts of Nα-acylamino acids and fatty acids mixture. These lastest are present in proportion
Alric, Isabelle   +4 more
core   +2 more sources

Putative DHHC-cysteine-rich domain S-acyltransferase in plants. [PDF]

open access: yesPLoS ONE, 2013
Protein S-acyltransferases (PATs) containing Asp-His-His-Cys within a Cys-rich domain (DHHC-CRD) are polytopic transmembrane proteins that are found in eukaryotic cells and mediate the S-acylation of target proteins. S-acylation is an important secondary
Xiaowei Yuan   +5 more
doaj   +1 more source

GCP16 stabilizes the DHHC9 subfamily of protein acyltransferases through a conserved C-terminal cysteine motif

open access: yesFrontiers in Physiology, 2023
Protein S-acylation is a reversible lipid post-translational modification that allows dynamic regulation of processes such as protein stability, membrane association, and localization.
Phillip L. Nguyen   +3 more
doaj   +1 more source

Plasma membrane association by N-acylation governs PKG function in Toxoplasma gondii [PDF]

open access: yes, 2017
Cyclic GMP (cGMP)-dependent protein kinase (protein kinase G [PKG]) is essential for microneme secretion, motility, invasion, and egress in apicomplexan parasites, However, the separate roles of two isoforms of the kinase that are expressed by some ...
Brown, Kevin M   +2 more
core   +2 more sources

Therapeutic targeting of protein S-acylation for the treatment of disease [PDF]

open access: yesBiochemical Society Transactions, 2019
The post-translational modification protein S-acylation (commonly known as palmitoylation) plays a critical role in regulating a wide range of biological processes including cell growth, cardiac contractility, synaptic plasticity, endocytosis, vesicle trafficking, membrane transport and biased-receptor signalling.
Niall J. Fraser   +3 more
openaire   +3 more sources

A Receptor Component of the Chloroplast Protein Translocation Machinery [PDF]

open access: yes, 1994
The chloroplast outer envelope protein OEP86 functions as a receptor in precursor protein translocation into chloroplasts. Sequence analysis suggests that the precursor of OEP86 is directed to the chloroplast outer envelope by a cleavable, negatively ...
Heemeyer, Frank   +4 more
core   +1 more source

Development of an Acrylamide-Based Inhibitor of Protein S-Acylation [PDF]

open access: yes, 2021
Protein S-acylation is a dynamic lipid post-translational modification that can modulate the localization and activity of target proteins. In humans, the installation of the lipid onto target proteins is catalyzed by a family of 23 Asp-His-His-Cys domain-containing protein acyltransferases (DHHC-PATs).
Saara-Anne Azizi   +4 more
openaire   +1 more source

An engineered Tetrahymena tRNA(Gln) for in vivo incorporation of unnatural amino acids into proteins by nonsense suppression [PDF]

open access: yes, 1996
A new tRNA, THG73, has been designed and evaluated as a vehicle for incorporating unnatural amino acids site-specifically into proteins expressed in vivo using the stop codon suppression technique.
Abelson, John N.   +7 more
core   +1 more source

Identification of a novel sequence motif recognised by the ankyrin-repeat domain of zDHHC17/13 S-acyl-transferases [PDF]

open access: yes, 2015
S-acylation is a major post-translational modification affecting several cellular processes and being particularly important for neuronal functions. This modification is catalysed by a family of transmembrane S-acyl-transferases that contain a conserved ...
Chamberlain, Luke H.   +2 more
core   +1 more source

Pseudo-enzymatic S-acylation of a myristoylated Yes protein tyrosine kinase peptide in vitro may reflect non-enzymatic S-acylation in vivo [PDF]

open access: yesBiochemical Journal, 1998
Covalent attachment of a variety of lipid groups to proteins is now recognized as a major group of post-translational modifications. S-acylation of proteins at cysteine residues is the only modification considered dynamic and thus has the potential for regulating protein function and/or localization.
M C, Bañó, C S, Jackson, A I, Magee
openaire   +2 more sources

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