Results 21 to 30 of about 2,794 (185)

Protein S-Palmitoylation as Potential Therapeutic Target for Dermatoses [PDF]

Biomolecules
Protein S-palmitoylation is a pivotal yet poorly integrated research field in dermatology. This reversible post-translational lipid modification primarily occurs on cysteine residues and is principally catalyzed by zinc finger and Asp-His-His-Cys DHHC ...
Yanhai Feng, Jianxin Wu, Hui Tang, Shunying Liu, Honglin Jia, Yi Liang, Zhenglin Li, Lingbo Li, Lingfei Li, Xia Lei   +9 more
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Dual Regulation of Sprouty 4 Palmitoylation by ZDHHC7 and Palmitoyl-Protein Thioesterase 1: A Potential Therapeutic Strategy for Cisplatin-Resistant Osteosarcoma [PDF]

Research
Background: Osteosarcoma (OS) is a primary malignant bone tumor predominantly affecting adolescents. Chemotherapeutic agents, such as cisplatin, are commonly used in OS treatment; however, drug resistance markedly undermines treatment efficacy and ...
Tianlong Huang, Yifan Chen, Qiangqiang Zhao, Xin Wu, Hongxing Li, Xin Luo, Yang Su, Shengqun Zhang, Pan Liu, Ning Tang   +9 more
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Engineered depalmitoylases enable selective manipulation of protein localization and function [PDF]

Nature Communications
S-Palmitoylation is a reversible post-translational modification that tunes the localization, stability, and function of an impressive array of proteins including ion channels, G-proteins, and synaptic proteins.
Srinidhi Jayaraman, Audrey Kochiss, Thy-Lan Alcalay, Pedro J. del Rivero Morfin, Manu Ben-Johny   +4 more
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The Unconventional Role of ABHD17A in Increasing the S-Palmitoylation and Antiviral Activity of IFITM1 by Downregulating ABHD16A [PDF]

Biomolecules
The broad-spectrum antiviral functions of interferon-inducible transmembrane 1 (IFITM1) rely on S-palmitoylation post-translational modification.
Xuemeng Shi, Shuaiwu Chen, Mingyang Liu, Yali Fan, Xin Wen, Jingyi Wang, Xiaoling Li, Huimin Liu, Lin Mao, Li Yu, Yuxin Hu, Jun Xu   +11 more
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Nanobody-thioesterase chimeras to specifically target protein palmitoylation [PDF]

Nature Communications
The complexity of the cellular proteome is massively expanded by a repertoire of chemically distinct reversible post-translational modifications (PTMs) that control protein localisation, interactions, and function.
Chien-Wen Kuo, Caglar Gök, Hannah Fulton, Eleanor Dickson-Murray, Samuel Adu, Emily K. Gallen, Sheon Mary, Alan D. Robertson, Fiona Jordan, Emma Dunning, William Mullen, Godfrey L. Smith, William Fuller   +12 more
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Insights into the molecular basis of the palmitoylation and depalmitoylation of NCX1 [PDF]

Cell Calcium, 2021
Catalyzed by zDHHC-PAT enzymes and reversed by thioesterases, protein palmitoylation is the only post-translational modification recognized to regulate the sodium/calcium exchanger NCX1. NCX1 palmitoylation occurs at a single site at position 739 in its large regulatory intracellular loop.
Caglar Gök, Alice Main, Xing Gao, Zsombor Kerekes, Fiona Plain, Chien-Wen Kuo, Alan D. Robertson, Niall J. Fraser, William Fuller   +8 more
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Trypanosoma brucei Acyl-Protein Thioesterase-like (TbAPT-L) Is a Lipase with Esterase Activity for Short and Medium-Chain Fatty Acids but Has No Depalmitoylation Activity

Pathogens, 2022
Dynamic post-translational modifications allow the rapid, specific, and tunable regulation of protein functions in eukaryotic cells. S-acylation is the only reversible lipid modification of proteins, in which a fatty acid, usually palmitate, is ...
Robert W. B. Brown, Aabha I. Sharma, Miguel Rey Villanueva, Xiaomo Li, Ouma Onguka, Leeor Zilbermintz, Helen Nguyen, Ben A. Falk, Cheryl L. Olson, Joann M. Taylor, Conrad L. Epting, Rahul S. Kathayat, Neri Amara, Bryan C. Dickinson, Matthew Bogyo, David M. Engman   +15 more
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Protein Lipidation by Palmitoylation and Myristoylation in Cancer

Frontiers in Cell and Developmental Biology, 2021
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 hydrophobicity, structural stability, localization, trafficking ...
Chee Wai Fhu, Azhar Ali
doaj   +1 more source

Dynamic but discordant alterations in zDHHC5 expression and palmitoylation of its substrates in cardiac pathologies

Frontiers in Physiology, 2022
S-palmitoylation is an essential lipid modification catalysed by zDHHC-palmitoyl acyltransferases that regulates the localisation and activity of substrates in every class of protein and tissue investigated to date.
Alice Main, Andri Boguslavskyi, Jacqueline Howie, Chien-Wen Kuo, Aileen Rankin, Francis L. Burton, Godfrey L. Smith, Roger Hajjar, George S. Baillie, Kenneth S. Campbell, Michael J. Shattock, William Fuller   +11 more
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Palmitoylation and depalmitoylation dynamics at a glance [PDF]

Journal of Cell Science, 2010
Protein palmitoylation, the thioester linkage of fatty acyl moieties (typically, saturated 16C palmitate) to cysteine, is a lipid modification that serves both to tether proteins to membranes and to direct their localization to membrane microdomains.
Elizabeth, Conibear, Nicholas G, Davis
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