Protein lipidation: occurrence, mechanisms, biological functions, and enabling technologies
Protein lipidation, including cysteine prenylation, N-terminal glycine myristoylation, cysteine
palmitoylation, and serine and lysine fatty acylation, occurs in many proteins in eukaryotic …
palmitoylation, and serine and lysine fatty acylation, occurs in many proteins in eukaryotic …
The Physiology of Protein S-acylation
LH Chamberlain, MJ Shipston - Physiological reviews, 2015 - journals.physiology.org
Protein S-acylation, the only fully reversible posttranslational lipid modification of proteins, is
emerging as a ubiquitous mechanism to control the properties and function of a diverse …
emerging as a ubiquitous mechanism to control the properties and function of a diverse …
Protein lipidation in cell signaling and diseases: function, regulation, and therapeutic opportunities
B Chen, Y Sun, J Niu, GK Jarugumilli, X Wu - Cell chemical biology, 2018 - cell.com
Protein lipidation is an important co-or posttranslational modification in which lipid moieties
are covalently attached to proteins. Lipidation markedly increases the hydrophobicity of …
are covalently attached to proteins. Lipidation markedly increases the hydrophobicity of …
The intracellular dynamic of protein palmitoylation
S-palmitoylation describes the reversible attachment of fatty acids (predominantly palmitate)
onto cysteine residues via a labile thioester bond. This posttranslational modification …
onto cysteine residues via a labile thioester bond. This posttranslational modification …
Protein S‐Palmitoylation: advances and challenges in studying a therapeutically important lipid modification
A Main, W Fuller - The FEBS Journal, 2022 - Wiley Online Library
The lipid post‐translational modification S‐palmitoylation is a vast developing field, with the
modification itself and the enzymes that catalyse the reversible reaction implicated in a …
modification itself and the enzymes that catalyse the reversible reaction implicated in a …
DHHC palmitoyl transferases: substrate interactions and (patho) physiology
J Greaves, LH Chamberlain - Trends in biochemical sciences, 2011 - cell.com
S-palmitoylation is a reversible post-translational modification that occurs on diverse cellular
proteins. Palmitoylation can affect proteins in many different ways, including regulating …
proteins. Palmitoylation can affect proteins in many different ways, including regulating …
What does S‐palmitoylation do to membrane proteins?
S Blaskovic, M Blanc, FG van der Goot - The FEBS journal, 2013 - Wiley Online Library
S‐palmitoylation is post‐translational modification, which consists in the addition of a C16
acyl chain to cytosolic cysteines and which is unique amongst lipid modifications in that it is …
acyl chain to cytosolic cysteines and which is unique amongst lipid modifications in that it is …
Substrate recruitment by zDHHC protein acyltransferases
MIP Malgapo, ME Linder - Open biology, 2021 - royalsocietypublishing.org
Protein palmitoylation is the post-translational attachment of fatty acids, most commonly
palmitate (C16: 0), onto a cysteine residue of a protein. This reaction is catalysed by a family …
palmitate (C16: 0), onto a cysteine residue of a protein. This reaction is catalysed by a family …
[HTML][HTML] Palmitoylation in Alzheimer⿿ s disease and other neurodegenerative diseases
Posttranslational modifications of proteins are important regulatory processes endowing the
proteins functional complexity. Over the last decade, numerous studies have shed light on …
proteins functional complexity. Over the last decade, numerous studies have shed light on …