Results 161 to 170 of about 17,841 (206)
Palmitoylation of the human cytomegalovirus tegument protein pp28 facilitates virus release. [PDF]
PLoS PathogLee JB, Koo N, Park JM, Seo JY.
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Journal of Cellular Physiology, 2023
AbstractPalmitoylation, a critical lipid modification of proteins, is involved in various physiological processes such as altering protein localization, transport, and stability, which perform essential roles in protein function. Palmitoyltransferases are specific enzymes involved in the palmitoylation modification of substrates.
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AbstractPalmitoylation, a critical lipid modification of proteins, is involved in various physiological processes such as altering protein localization, transport, and stability, which perform essential roles in protein function. Palmitoyltransferases are specific enzymes involved in the palmitoylation modification of substrates.
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Regulation of NCX1 by palmitoylation [PDF]
Cell 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
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Protein palmitoylation and cancer [PDF]
EMBO 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 Dixon
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Assays of protein palmitoylation
Methods, 2006Protein palmitoylation plays an important role in the structure and function of a wide array of proteins. Unlike other lipid modifications, protein palmitoylation is highly dynamic and cycles of palmitoylation and depalmitoylation can regulate protein function and localization.
Renaldo C Drisdel
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Biochemical and Biophysical Research Communications, 1997
Tubulin is a very water soluble protein, yet a significant portion is firmly associated with cell membranes. Because recent work has shown that palmitoylation is a dynamic process that can alter the targeting of proteins to membranes, we tested whether or not tubulin could be palmitoylated to account for its membrane location.
A M, Zambito, J, Wolff
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Tubulin is a very water soluble protein, yet a significant portion is firmly associated with cell membranes. Because recent work has shown that palmitoylation is a dynamic process that can alter the targeting of proteins to membranes, we tested whether or not tubulin could be palmitoylated to account for its membrane location.
A M, Zambito, J, Wolff
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On the mechanism of protein palmitoylation [PDF]
EMBO 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 Dietrich, Christian Ungermann
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Palmitoylation and palmitoyl-transferases in Plasmodium parasites
Biochemical Society Transactions, 2015Protein post-translational modifications (PTM) are commonly used to regulate biological processes. Protein S-acylation is an enzymatically regulated reversible modification that has been shown to modulate protein localization, activity and membrane binding.
Nicola, Hodson +3 more
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Palmitoylation as a Signal for Delivery
2020The ligands and receptors in immune checkpoint signaling are typically transmembrane proteins, which may be regulated by palmitoylation as a reversible lipid modification. Our recent work demonstrated that palmitoylation reduces the lysosomal degradation of PD-L1 trafficking and may present a new therapeutic target.
Yiting, Wang +3 more
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Palmitoylation, pathogens and their host
Biochemical Society Transactions, 2013S-Palmitoylation, the only reversible post-translational lipid modification, confers unique biochemical and functional properties to proteins. Although it has long been known that viral proteins are palmitoylated, recent studies reveal that this modification plays a critical role for pathogens of all kinds and at multiple steps of their life cycle. The
Blanc Mathieu +2 more
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