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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.
F Gisou Van Der Goot
exaly   +2 more sources

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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

Protein S-palmitoylation and cancer

Biochimica et Biophysica Acta (BBA) - Reviews on Cancer, 2015
Protein S-palmitoylation is a reversible posttranslational modification of proteins with fatty acids, an enzymatic process driven by a recently discovered family of protein acyltransferases (PATs) that are defined by a conserved catalytic domain characterized by a DHHC sequence motif.
Marc, Yeste-Velasco, Maurine E, Linder, Yong-Jie, Lu   +2 more
openaire   +2 more sources

Dynamic Radiolabeling of S-Palmitoylated Proteins

2019
Proteins can be radiolabeled either during synthesis, typically using 35S-cysteine/methionine (35S-Cys/Met), or after synthesis, by adding a radiolabeled posttranslational modification. Here we describe how protein S-palmitoylation, and its dynamics, can be monitored by 3H-palmitate labeling and how the importance of S-palmitoylation in protein ...
Abrami L, Denhardt-Eriksson RA, Hatzimanikatis V, van der Goot FG   +3 more
openaire   +3 more sources

SwissPalm 2: Protein S-Palmitoylation Database

2019
Protein S-palmitoylation is increasingly recognized as an important posttranslational modification, present in all eukaryotic organisms, involved in the regulation of many biological processes. The SwissPalm database centralizes the large and increasing number of published palmitoyl-proteome datasets, provides tools to compare them, and includes ...
Blanc M, David FPA, van der Goot FG
openaire   +3 more sources

S-palmitoylation: An oily modification guardinggenome stability

DNA Repair
S-palmitoylation is a dynamic post-translational lipid modification that regulates key cellular processes. It is mediated by aspartate-histidine-histidine-cysteine-family palmitoyltransferases (PATs) and reversed by acyl-protein thioesterases (APTs).
Xiyuan, Zheng, Xinying, Wu, Lei, Wang, Haohong, Ouyang, Yeltokova, Damira, Bin, Peng, Xingzhi, Xu   +6 more
openaire   +2 more sources

S-palmitoylation modulates human estrogen receptor-α functions

Biochemical and Biophysical Research Communications, 2004
17beta-Estradiol (E2)-induced rapid functions (from seconds to minutes) can be attributed to a fraction of nuclear estrogen receptor-alpha (ERalpha) localized at the plasma membrane. As a potential mechanism, we postulated that S-palmitoylation of the Cys447 residue may explain the ability of ERalpha to associate to plasma membrane making possible E2 ...
ACCONCIA, FILIPPO, ASCENZI P., FABOZZI G., VISCA, PAOLO, MARINO, Maria   +4 more
openaire   +4 more sources

Enrichment of S-Palmitoylated Proteins for Mass Spectrometry Analysis

2019
As the 10-year anniversary of their first introduction approaches, alkynyl fatty acids have revolutionized the analysis of S-palmitoylation dynamics, acting as functional mimics incorporated into native modification sites in cultured cells. The alkyne functional group provides a robust handle for bioorthogonal Cu(I)-catalyzed azide-alkyne cycloaddition
Melanie, Cheung See Kit, Brent R, Martin
openaire   +2 more sources

NODs require S-palmitoylation to signal

Science, 2019
Innate Immunity The compartmentalization of proteins within the cell is essential for their function. The addition of lipid molecules redistributes proteins to the cell surface or to membrane-bound organelles. Working in transgenic mice and in tissue cultured cells, Lu et al. found that nucleotide oligomerization domain–like receptors 1 and 2 (NOD1 and
openaire   +1 more source

S-palmitoylation modulates estrogen receptor α localization and functions

Steroids, 2006
17beta-Estradiol (E2) acts as a chemical messenger in target tissues inducing both slow nuclear and rapid extra-nuclear responses. E2 binds to its cognate nuclear receptors (ER) resulting in the activation of target gene transcription in the nucleus.
MARINO, Maria, ASCENZI P, ACCONCIA, FILIPPO   +2 more
openaire   +5 more sources