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Protein palmitoylation in cancer: molecular functions and therapeutic potential [PDF]

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   +3 more
doaj   +3 more sources

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

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, Leisi Zhang, Chun-Wei Chen
doaj   +4 more sources

Protein Palmitoylation Regulates Cell Survival by Modulating XBP1 Activity in Glioblastoma Multiforme [PDF]

open access: yesMolecular Therapy: Oncolytics, 2020
Glioblastoma multiforme (GBM) almost invariably acquires an invasive phenotype, resulting in limited therapeutic options. Protein palmitoylation markedly affects tumorigenesis and malignant progression in GBM.
Xueran Chen   +9 more
doaj   +4 more sources

Protein Palmitoylation Modification During Viral Infection and Detection Methods of Palmitoylated Proteins [PDF]

open access: yesFrontiers in Cellular and Infection Microbiology, 2022
Protein palmitoylation—a lipid modification in which one or more cysteine thiols on a substrate protein are modified to form a thioester with a palmitoyl group—is a significant post-translational biological process. This process regulates the trafficking,
Xiaoling Li   +5 more
doaj   +2 more sources

Protein palmitoylation: an emerging regulator of inflammatory signaling and diseases [PDF]

open access: yesFrontiers in Immunology
Protein palmitoylation is a reversible lipid modification in which palmitoyl esters are covalently attached to cysteine residues of proteins. It controls various cellular physiological processes and alters protein stability, conformation, localization ...
Rong Chen   +6 more
doaj   +2 more sources

Protein palmitoylation is involved in regulating mouse sperm motility via the signals of calcium, protein tyrosine phosphorylation and reactive oxygen species [PDF]

open access: yesBiological Research
Background Protein palmitoylation, a critical posttranslational modification, plays an indispensable role in various cellular processes, including the regulation of protein stability, mediation of membrane fusion, facilitation of intracellular protein ...
Yuping Xiong   +5 more
doaj   +2 more sources

Protein palmitoylation: biological functions, disease, and therapeutic targets [PDF]

open access: yesMedComm
Protein palmitoylation, a reversible post‐translational lipid modification, is catalyzed by the ZDHHC family of palmitoyltransferases and reversed by several acyl protein thioesterases, regulating protein localization, accumulation, secretion, and ...
Yan‐Ran Qian   +2 more
doaj   +2 more sources

Protein palmitoylation in hepatic diseases: Functional insights and therapeutic strategies [PDF]

open access: yesJournal of Advanced Research
Background: Liver pathologies represent a spectrum of conditions ranging from fatty liver to the aggressive hepatocellular carcinoma (HCC), as well as parasitic infections, which collectively pose substantial global health challenges.
Ying Wang   +12 more
doaj   +2 more sources

Protein S-palmitoylation modification: implications in tumor and tumor immune microenvironment

open access: yesFrontiers in Immunology
Protein S-palmitoylation is a reversible post-translational lipid modification that involves the addition of a 16-carbon palmitoyl group to a protein cysteine residue via a thioester linkage.
Yijiao Chen, Yongsheng Li, Lei Wu
doaj   +3 more sources

Cell Labeling with 15-YNE Is Useful for Tracking Protein Palmitoylation and Metabolic Lipid Flux in the Same Sample [PDF]

open access: yesMolecules
Protein S-palmitoylation is the process by which a palmitoyl fatty acid is attached to a cysteine residue of a protein via a thioester bond. A range of methodologies are available for the detection of protein S-palmitoylation.
Nadine Merz   +4 more
doaj   +2 more sources

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