Results 171 to 180 of about 2,794 (185)

Enzymatic protein depalmitoylation by acyl protein thioesterases

Biochemical Society Transactions, 2015
Protein palmitoylation is a dynamic post-translational modification, where the 16-carbon fatty acid, palmitate, is added to cysteines of proteins to modulate protein sorting, targeting and signalling. Palmitate removal from proteins is mediated by acyl protein thioesterases (APTs).
David T S, Lin, Elizabeth, Conibear
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Targeting the Ras palmitoylation/depalmitoylation cycle in cancer

Biochemical Society Transactions, 2017
The Ras proteins are well-known drivers of many cancers and thus represent attractive targets for the development of anticancer therapeutics. Inhibitors that disrupt the association of the Ras proteins with membranes by blocking the addition of the farnesyl lipid moiety to the Ras C-terminus failed in clinical trials.
David Tse Shen, Lin, Nicholas G, Davis, Elizabeth, Conibear   +2 more
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Amphiphile-Mediated Depalmitoylation of Proteins in Living Cells

Journal of the American Chemical Society, 2018
Post-translational S-palmitoylation plays a central role in protein localization, trafficking, stability, aggregation, and cell signaling. Dysregulation of palmitoylation pathways in cells can alter protein function and is the cause of several diseases.
Andrew K. Rudd, Roberto J. Brea, Neal K. Devaraj   +2 more
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Activation and depalmitoylation of Gsα

Cell, 1994
[3H]palmitate attached to mutationally activated alpha s (alpha s-R201C) turns over rapidly, compared with palmitate linked to normal alpha s (t1/2 approximately 2 min versus 90 min); although alpha s-R201C (unlike normal alpha s) is predominantly found in the cytosol, [3H]palmitate is linked only to the membrane-bound pool of alpha s, normal or mutant.
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Depalmitoylation and cell physiology: APT1 as a mediator of metabolic signals

American Journal of Physiology-Cell Physiology
More than half of the global population is obese or overweight, especially in Western countries, and this excess adiposity disrupts normal physiology to cause chronic diseases. Diabetes, an adiposity-associated epidemic disease, affects >500 million people, and cases are projected to exceed 1 billion before 2050.
Sarah L. Speck, Xiaochao Wei, Clay F. Semenkovich   +2 more
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Activation and depalmitoylation of Gs alpha.

Cell, 1994
[3H]palmitate attached to mutationally activated alpha s (alpha s-R201C) turns over rapidly, compared with palmitate linked to normal alpha s (t1/2 approximately 2 min versus 90 min); although alpha s-R201C (unlike normal alpha s) is predominantly found in the cytosol, [3H]palmitate is linked only to the membrane-bound pool of alpha s, normal or mutant.
P B, Wedegaertner, H R, Bourne
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Identifying the Potential Substrates of the Depalmitoylation Enzyme Acyl-protein Thioesterase 1

Current Molecular Medicine, 2019
Background:The homeostasis of palmitoylation and depalmitoylation is involved in various cellular processes, the disruption of which induces severe physiological consequences. Acyl-protein thioesterase (APT) and palmitoyl-protein thioesterases (PPT) catalyze the depalmitoylation process.
Huicong, Liu, Peipei, Yan, Junyan, Ren, Can, Wu, Wei, Yuan, Muding, Rao, Zhongjian, Zhang, Eryan, Kong   +7 more
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Role of palmitoylation/depalmitoylation reactions in G-protein-coupled receptor function

Pharmacology & Therapeutics, 2003
G-protein-coupled receptors (GPCRs) constitute one of the largest protein families in the human genome. They are subject to numerous post-translational modifications, including palmitoylation. This review highlights the dynamic nature of palmitoylation and its role in GPCR expression and function.
Riad, Qanbar, Michel, Bouvier
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In vitro depalmitoylation of neurospecific peptides: Implication for infantile neuronal ceroid lipofuscinosis

Journal of Neuroscience Research, 2000
Palmitoyl protein thioesterase 1 (PPT1) removes palmitate from specific cysteine residues in peptides and proteins. We have previously shown that a palmitoylated myelin glycoprotein. Po octapeptide (IRYCWLRR) can be specifically depalmitoylated by PPT1 in vitro (Cho and Dawson [1998] J. Neurochem. 171 ;323-329).
S, Cho, P E, Dawson, G, Dawson
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A palmitoylation–depalmitoylation relay spatiotemporally controls GSDMD activation in pyroptosis

Nature Cell Biology
Gasdermin D (GSDMD) is the executor of pyroptosis, which is important for host defence against pathogen infection. Following activation, caspase-mediated cleavage of GSDMD releases an amino-terminal fragment (GSDMD-NT), which oligomerizes and forms pores in the plasma membrane, leading to cell death and release of proinflammatory cytokines. The spatial
Na Zhang, Jian Zhang, Yuanxin Yang, Hengyue Shan, Shouqiao Hou, Hongwen Fang, Min Ma, Zhongwen Chen, Li Tan, Daichao Xu   +9 more
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