Results 131 to 140 of about 21,089,371 (171)

Palmitoylation-dependent regulation of GPX4 suppresses ferroptosis

Nature Communications
S-palmitoylation is a reversible and widespread post-translational modification, but its role in the regulation of ferroptosis has been poorly understood. Here, we elucidate that GPX4, an essential regulator of ferroptosis, is reversibly palmitoylated on
Bin Huang, Hui Wang, Shuo Liu, Meng Hao, Dan Luo, Yi Zhou, Ying Huang, Yong Nian, Lei Zhang, Bo Chu, Chengqian Yin   +10 more
doaj   +1 more source

ZDHHC2‐Dependent Palmitoylation Dictates Ferroptosis and Castration Sensitivity in Prostate Cancer via Controlling ACSL4 Degradation and Lipid Peroxidation

Advanced Science
Ferroptosis represents a promising vulnerability to overcome therapeutic resistance in castration‐resistant prostate cancer (CRPC). While S‐palmitoylation of lipid peroxide‐scavenging proteins such as GPX4 and SLC7A11 has been shown to suppress ...
Shuai Shao, Wei Li, Yulong Hong, Ruijiang Zeng, Liang Zhu, Lu Yi, Yuan Li, Yinhuai Wang, Haojie Huang, Xuewen Jiang, Xin Jin   +10 more
doaj   +1 more source

Targeting Autopalmitoylation to Modulate Protein S-Palmitoylation

, 2015
Palmitoylation refers to the covalent attachment of fatty acids, such as palmitate, onto the cysteine residues of proteins. This process may subsequently alter their localization and function. Nearly all of the enzymes that catalyze palmitoylation, zDHHC
Hamel, Laura Dawn
core  

Palmitoylation, pathogens and their host

S-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 ...
Blanc, Mathieu, Blaskovic, Sanja, van der Goot, Gisou   +2 more
core   +1 more source

S-Palmitoylation of Tyrosinase at Cysteine⁵⁰⁰ Regulates Melanogenesis

S-Palmitoylation of Tyrosinase at Cysteine⁵⁰⁰ Regulates Melanogenesis
Palmitoylation is a lipid modification involving the attachment of palmitic acid to a cysteine residue, thereby affecting protein function. We investigated the effect of palmitoylation of tyrosinase, the rate-limiting enzyme in melanin synthesis, using a human three-dimensional skin model system and melanocyte culture.
openaire   +1 more source

Mapping and Analysis of S-Palmitoylation Sites on RPE65 Protein [PDF]

Biophysical Journal, 2018
Sheetal Uppal, Eugenia Poliakov, Susan Gentleman, T. Michael Redmond   +3 more
openaire   +1 more source

The Role of Lipid-Protein Dynamics in Diseases Development: Focus on S-Palmitoylation and Cancer

Protein lipidation, a crucial post-translational modification, plays a fundamental role in regulating protein function, localization, and stability. Among the different lipidation types, S-palmitoylation is one of the most extensively studied due to its ...
Temiloluwa Adelanwa
core  

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.
Caglar Gok, William Fuller
exaly   +7 more sources

What does S‐palmitoylation do to membrane proteins? [PDF]

FEBS Journal, 2013
S-Palmitoylation is post-translational modification, which consists in the addition of a C16 acyl chain to cytosolic cysteines and which is unique amongst lipid modifications in that it is reversible.
Gisou van der Goot
exaly   +3 more sources

Some of the next articles are maybe not open access.

Related searches:

Protein S-Palmitoylation and Lung Diseases

2021
S-palmitoylation of protein is a posttranslational, reversible lipid modification; it was catalyzed by a family of 23 mammalian palmitoyl acyltransferases in humans. S-palmitoylation can impact protein function by regulating protein sorting, secretion, trafficking, stability, and protein interaction.
Zeang, Wu, Rubin, Tan, Liping, Zhu, Ping, Yao, Qinghua, Hu   +4 more
openaire   +2 more sources