Results 11 to 20 of about 20,725 (233)

Regulation of NCX1 by palmitoylation [PDF]

open access: yesCell Calcium, 2020
Palmitoylation (S-acylation) is the reversible conjugation of a fatty acid (usually C16 palmitate) to intracellular cysteine residues of proteins via a thioester linkage. Palmitoylation anchors intracellular regions of proteins to membranes because the palmitoylated cysteine is recruited to the lipid bilayer.
Caglar Gok, William Fuller
exaly   +7 more sources

Protein palmitoylation in cancer: molecular functions and therapeutic potential

open access: yesMolecular Oncology, 2023
Protein S‐palmitoylation (hereinafter referred to as protein palmitoylation) is a reversible lipid posttranslational modification catalyzed by the zinc finger DHHC‐type containing (ZDHHC) protein family.
Binhui Zhou   +2 more
exaly   +3 more sources

Palmitoylation in Renal Physiology and Pathology. [PDF]

open access: yesBiomolecules
Palmitoylation is a critical post-translational modification that involves the covalent binding of palmitic acid to cysteine residues within proteins.
Ma J   +9 more
europepmc   +2 more sources

The Roles of Protein <i>S</i>-Palmitoylation in Cancers: From Dynamic Modulation to Therapeutic Potential. [PDF]

open access: yesCancer Commun (Lond)
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
Zheng H   +7 more
europepmc   +2 more sources

Diverse Roles of Protein Palmitoylation in Cancer Progression, Immunity, Stemness, and Beyond

open access: yesCells, 2023
Protein S-palmitoylation, a type of post-translational modification, refers to the reversible process of attachment of a fatty acyl chain—a 16-carbon palmitate acid—to the specific cysteine residues on target proteins.
Mingli Li, Chun-Wei Chen, Li Mingli
exaly   +3 more sources

Palmitoylation landscapes across human cancers reveal a role of palmitoylation in tumorigenesis

open access: yesJournal of Translational Medicine, 2023
Background Protein palmitoylation, which is catalyzed by palmitoyl-transferase and de-palmitoyl-transferase, plays a crucial role in various biological processes. However, the landscape and dynamics of protein palmitoylation in human cancers are not well
Yue Kong   +8 more
doaj   +3 more sources

Palmitoylation and depalmitoylation defects [PDF]

open access: yesJournal of Inherited Metabolic Disease, 2014
AbstractPalmitoylation 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. In particular S‐palmitoylation is dynamically regulated by two opposing types of enzymes which add (palmitoyl ...
Hornemann, Thorsten, Thorsten Hornemann
openaire   +5 more sources

Protein palmitoylation and cancer [PDF]

open access: yesEMBO Reports, 2018
Protein S-palmitoylation is a reversible post-translational modification that alters the localization, stability, and function of hundreds of proteins in the cell. S-palmitoylation is essential for the function of both oncogenes (e.g., NRAS and EGFR) and tumor suppressors (e.g., SCRIB, melanocortin 1 receptor).
Scott J Dixon
exaly   +3 more sources

Insulin regulates lymphatic endothelial integrity via palmitoylation

open access: yesJournal of Lipid Research
Lipid metabolism plays a critical role in lymphatic endothelial cell (LEC) development and vessel maintenance. Altered lipid metabolism is associated with loss of lymphatic vessel integrity, which compromises organ function, protective immunity, and ...
Silvia Gonzalez-Nieves   +10 more
doaj   +2 more sources

On the mechanism of protein palmitoylation [PDF]

open access: yesEMBO Reports, 2004
Protein palmitoylation or, more specifically, S-acylation is a reversible post-translational lipid modification. Despite the identification of several proteins that are altered in this way, our understanding of the enzymology of this process has been hampered by the lack of well-characterized acyltransferases.
Lars E P Dietrich, Christian Ungermann
exaly   +3 more sources

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