Results 11 to 20 of about 15,826,951 (219)

Role of S-palmitoylation in digestive system diseases [PDF]

open access: yesCell Death Discovery
Digestive system diseases, including liver diseases, gastrointestinal cancers, and inflammatory bowel diseases, pose major health challenges worldwide.
Hanqing Li   +4 more
doaj   +4 more sources

Role of S-palmitoylation on IFITM5 for the interaction with FKBP11 in osteoblast cells. [PDF]

open access: yesPLoS ONE, 2013
Recently, one of the interferon-induced transmembrane (IFITM) family proteins, IFITM3, has become an important target for the activity against influenza A (H1N1) virus infection.
Takashi Tsukamoto   +6 more
doaj   +7 more sources

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

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   +4 more sources

Protein S-palmitoylation in cellular differentiation [PDF]

open access: yesBiochemical Society Transactions, 2017
Reversible protein S-palmitoylation confers spatiotemporal control of protein function by modulating protein stability, trafficking and activity, as well as protein–protein and membrane–protein associations. Enabled by technological advances, global studies revealed S-palmitoylation to be an important and pervasive posttranslational modification in ...
Zhang, Mingzi M., Hang, Howard C.
openaire   +3 more sources

Inhibiting S-palmitoylation arrests metastasis by relocating Rap2b from plasma membrane in colorectal cancer [PDF]

open access: yesCell Death and Disease
Rap2b, a proto-oncogene upregulated in colorectal cancer (CRC), undergoes protein S-palmitoylation at specific C-terminus sites (C176/C177). These palmitoylation sites are crucial for Rap2b localization on the plasma membrane (PM), as mutation of C176 or
Jiangli Zhu   +15 more
doaj   +3 more sources

PRDX6: A protein bridging S-palmitoylation and diabetic neuropathy

open access: yesFrontiers in Endocrinology, 2022
Diabetic neuropathy is regarded as one of the most debilitating outcomes of diabetes. It can affect both the peripheral and central nervous systems, leading to pain, decreased motility, cognitive decline, and dementia.
Yan Cao   +3 more
doaj   +3 more sources

The Roles of Protein S-Palmitoylation in Cancers: From Dynamic Modulation to Therapeutic Potential [PDF]

open access: yesCancer Communications
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
Haonan Zheng   +7 more
doaj   +2 more sources

S-palmitoylation-related genes in Crohn's disease: Bioinformatic identification and validation [PDF]

open access: yesBiomolecules & Biomedicine
Crohn's disease (CD) is a complex chronic inflammatory bowel disorder characterized by the absence of reliable biomarkers and effective targeted treatments.
Yuyan Zhou, Yuxuan Zhao
doaj   +2 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   +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

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