Protein S-palmitoylation and cancer
M Yeste-Velasco, ME Linder, YJ Lu - … et Biophysica Acta (BBA)-Reviews on …, 2015 - Elsevier
Protein S-palmitoylation is a reversible posttranslational modification of proteins with fatty
acids, an enzymatic process driven by a recently discovered family of protein …
acids, an enzymatic process driven by a recently discovered family of protein …
Emerging roles of DHHC-mediated protein S-palmitoylation in physiological and pathophysiological context
I De, S Sadhukhan - European journal of cell biology, 2018 - Elsevier
Protein S-palmitoylation refers to a post-translational modification (PTM) wherein palmitic
acid, a 16-carbon long saturated fatty acid gets covalently attached to Cys sidechain of a …
acid, a 16-carbon long saturated fatty acid gets covalently attached to Cys sidechain of a …
Mechanism and function of DHHC S-acyltransferases
ME Linder, BC Jennings - 2013 - portlandpress.com
Protein S-palmitoylation is a reversible post-translational modification of proteins with fatty
acids. In the last 5 years, improved proteomic methods have increased the number of …
acids. In the last 5 years, improved proteomic methods have increased the number of …
Understanding protein palmitoylation: Biological significance and enzymology
XM Guan, CA Fierke - Science China Chemistry, 2011 - Springer
Protein palmitoylation is a widespread lipid modification in which one or more cysteine thiols
on a substrate protein are modified to form a thioester with a palmitoyl group. This lipid …
on a substrate protein are modified to form a thioester with a palmitoyl group. This lipid …
Protein palmitoylation in cancer: molecular functions and therapeutic potential
B Zhou, Q Hao, Y Liang, E Kong - Molecular oncology, 2023 - Wiley Online Library
Protein S‐palmitoylation (hereinafter referred to as protein palmitoylation) is a reversible
lipid posttranslational modification catalyzed by the zinc finger DHHC‐type containing …
lipid posttranslational modification catalyzed by the zinc finger DHHC‐type containing …
2-Bromopalmitate analogues as activity-based probes to explore palmitoyl acyltransferases
B Zheng, M DeRan, X Li, X Liao… - Journal of the American …, 2013 - ACS Publications
Reversible S-palmitoylation is an important post-translational modification that regulates the
trafficking, localization, and activity of proteins. Cysteine-rich Asp-His-His-Cys (DHHC) …
trafficking, localization, and activity of proteins. Cysteine-rich Asp-His-His-Cys (DHHC) …
Protein palmitoylation and its pathophysiological relevance
J Jin, X Zhi, X Wang, D Meng - Journal of cellular physiology, 2021 - Wiley Online Library
Protein palmitoylation, in which C16 fatty acid chains are attached to cysteine residues via a
reversible thioester linkage, is one of the most common lipid modifications and plays …
reversible thioester linkage, is one of the most common lipid modifications and plays …
Therapeutic targeting of protein S-acylation for the treatment of disease
NJ Fraser, J Howie, KJ Wypijewski… - Biochemical Society …, 2020 - portlandpress.com
The post-translational modification protein S-acylation (commonly known as palmitoylation)
plays a critical role in regulating a wide range of biological processes including cell growth …
plays a critical role in regulating a wide range of biological processes including cell growth …
Identification of CKAP4/p63 as a major substrate of the palmitoyl acyltransferase DHHC2, a putative tumor suppressor, using a novel proteomics method
Protein palmitoylation is the post-translational addition of the 16-carbon fatty acid palmitate
to specific cysteine residues by a labile thioester linkage. Palmitoylation is mediated by a …
to specific cysteine residues by a labile thioester linkage. Palmitoylation is mediated by a …