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Endothelial cell palmitoylproteomic identifies novel lipid-modified targets and potential substrates for protein acyl transferases
scientific journal article
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scholarly article
1 reference
stated in
PubMed
PubMed ID
22496122
retrieved
4 January 2017
title
Endothelial cell palmitoylproteomic identifies novel lipid-modified targets and potential substrates for protein acyl transferases
(English)
1 reference
stated in
PubMed
PubMed ID
22496122
retrieved
4 January 2017
main subject
endothelium
0 references
superoxide dismutase 1
1 reference
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GOA release 2020-03-11
author
Alberto Davalos
series ordinal
4
object named as
Alberto Davalos
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stated in
PubMed
PubMed ID
22496122
retrieved
4 January 2017
William C. Sessa
series ordinal
5
object named as
William C. Sessa
1 reference
stated in
PubMed
PubMed ID
22496122
retrieved
4 January 2017
author name string
Ethan P. Marin
series ordinal
1
1 reference
stated in
PubMed
PubMed ID
22496122
retrieved
4 January 2017
Behrad Derakhshan
series ordinal
2
1 reference
stated in
PubMed
PubMed ID
22496122
retrieved
4 January 2017
TuKiet T. Lam
series ordinal
3
1 reference
stated in
PubMed
PubMed ID
22496122
retrieved
4 January 2017
language of work or name
English
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based on heuristic
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publication date
11 May 2012
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PubMed
PubMed ID
22496122
retrieved
4 January 2017
published in
Circulation Research
1 reference
stated in
PubMed
PubMed ID
22496122
retrieved
4 January 2017
volume
110
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stated in
PubMed
PubMed ID
22496122
retrieved
4 January 2017
issue
10
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stated in
PubMed
PubMed ID
22496122
retrieved
4 January 2017
page(s)
1336–1344
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stated in
PubMed
PubMed ID
22496122
retrieved
4 January 2017
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Palmitoylome profiling reveals S-palmitoylation-dependent antiviral activity of IFITM3
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DHHC5 protein palmitoylates flotillin-2 and is rapidly degraded on induction of neuronal differentiation in cultured cells
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Proteomic profiling of S-acylated macrophage proteins identifies a role for palmitoylation in mitochondrial targeting of phospholipid scramblase 3.
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Proteomic analysis of fatty-acylated proteins in mammalian cells with chemical reporters reveals S-acylation of histone H3 variants
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Site-specific analysis of protein S-acylation by resin-assisted capture
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Identification and regulation of reticulon 4B (Nogo-B) in renal tubular epithelial cells
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Palmitoylation of ketogenic enzyme HMGCS2 enhances its interaction with PPARalpha and transcription at the Hmgcs2 PPRE.
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29 September 2017
Attenuation of retinal vascular development and neovascularization in PECAM-1-deficient mice
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Evolving functions of endothelial cells in inflammation
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Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1.
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29 September 2017
Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALS
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Palmitoylation of ligands, receptors, and intracellular signaling molecules
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Identification of Golgi-localized acyl transferases that palmitoylate and regulate endothelial nitric oxide synthase
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29 September 2017
Palmitoylation of the Rous sarcoma virus transmembrane glycoprotein is required for protein stability and virus infectivity
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Palmitoylation-dependent control of degradation, life span, and membrane expression of the CCR5 receptor.
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Palmitoylation of the recombinant human A1 adenosine receptor: enhanced proteolysis of palmitoylation-deficient mutant receptors
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PECAM-1 is required for transendothelial migration of leukocytes
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29 September 2017
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27 November 2018
Palmitoylation at Cys595 is essential for PECAM-1 localisation into membrane microdomains and for efficient PECAM-1-mediated cytoprotection.
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27 November 2018
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27 November 2018
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27 November 2018
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Inhibition of antigen-receptor signaling by Platelet Endothelial Cell Adhesion Molecule-1 (CD31) requires functional ITIMs, SHP-2, and p56(lck).
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Dicer dependent microRNAs regulate gene expression and functions in human endothelial cells
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A novel two-base mutation in the Cu/Zn superoxide dismutase gene associated with familial amyotrophic lateral sclerosis in Japan
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Copper activation of superoxide dismutase 1 (SOD1) in vivo. Role for protein-protein interactions with the copper chaperone for SOD1
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https://pubmed.ncbi.nlm.nih.gov/22496122
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12 December 2020
based on heuristic
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Identifiers
DOI
10.1161/CIRCRESAHA.112.269514
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3391155
OpenCitations bibliographic resource ID
3391155
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3391155
PMCID
3428238
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3391155
PubMed ID
22496122
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3391155
ResearchGate publication ID
223977395
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