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 …
Fatty acyl recognition and transfer by an integral membrane S-acyltransferase
INTRODUCTION Hundreds of cellular proteins are modified by posttranslational S-acylation
of cysteines, commonly known as protein palmitoylation. Unlike other lipid attachments …
of cysteines, commonly known as protein palmitoylation. Unlike other lipid attachments …
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 …
Protein palmitoylation and its pathophysiological relevance
J Jin, X Zhi, X Wang, D Meng - Journal of cellular physiology, 2021 - Wiley Online Library
Protein palmitoylation, in which C16 fatty acid chains are attached to cysteine residues via a
reversible thioester linkage, is one of the most common lipid modifications and plays …
reversible thioester linkage, is one of the most common lipid modifications and plays …
[HTML][HTML] Protein lipidation by palmitoylation and myristoylation in cancer
CW Fhu, A Ali - Frontiers in Cell and Developmental Biology, 2021 - frontiersin.org
Posttranslational modification of proteins with lipid moieties is known as protein lipidation.
The attachment of a lipid molecule to proteins endows distinct properties, which affect their …
The attachment of a lipid molecule to proteins endows distinct properties, which affect their …
[HTML][HTML] Function of protein S-palmitoylation in immunity and immune-related diseases
Y Zhang, Z Qin, W Sun, F Chu, F Zhou - Frontiers in Immunology, 2021 - frontiersin.org
Protein S-palmitoylation is a covalent and reversible lipid modification that specifically
targets cysteine residues within many eukaryotic proteins. In mammalian cells, the …
targets cysteine residues within many eukaryotic proteins. In mammalian cells, the …
Structure and mechanism of DHHC protein acyltransferases
R Stix, CJ Lee, JD Faraldo-Gómez… - Journal of molecular …, 2020 - Elsevier
S-acylation, whereby a fatty acid chain is covalently linked to a cysteine residue by a
thioester linkage, is the most prevalent kind of lipid modification of proteins. Thousands of …
thioester linkage, is the most prevalent kind of lipid modification of proteins. Thousands of …
The molecular mechanism of DHHC protein acyltransferases
Protein S-acylation is a reversible lipidic posttranslational modification where a fatty acid
chain is covalently linked to cysteine residues by a thioester linkage. A family of integral …
chain is covalently linked to cysteine residues by a thioester linkage. A family of integral …
Protein palmitoylation: Palmitoyltransferases and their specificity
S Tabaczar, A Czogalla, J Podkalicka… - Experimental …, 2017 - journals.sagepub.com
A plethora of novel information has emerged over the past decade regarding protein
lipidation. The reversible attachment of palmitic acid to cysteine residues, termed S …
lipidation. The reversible attachment of palmitic acid to cysteine residues, termed S …