An acetylation switch regulates SUMO-dependent protein interaction networks.
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A high-confidence interaction map identifies SIRT1 as a mediator of acetylation of USP22 and the SAGA coactivator complexStructural analysis of poly-SUMO chain recognition by the RNF4-SIMs domainTnaA, an SP-RING protein, interacts with Osa, a subunit of the chromatin remodeling complex BRAHMA and with the SUMOylation pathway in Drosophila melanogasterPromyelocytic leukemia (PML) protein plays important roles in regulating cell adhesion, morphology, proliferation and migrationC-terminal Src kinase (Csk)-mediated phosphorylation of eukaryotic elongation factor 2 (eEF2) promotes proteolytic cleavage and nuclear translocation of eEF2Neuronal SUMOylation: mechanisms, physiology, and roles in neuronal dysfunction.Contribution of the Major ND10 Proteins PML, hDaxx and Sp100 to the Regulation of Human Cytomegalovirus Latency and Lytic Replication in the Monocytic Cell Line THP-1.PML nuclear bodies: assembly and oxidative stress-sensitive sumoylation.Global SUMO Proteome Responses Guide Gene Regulation, mRNA Biogenesis, and Plant Stress Responses.A high throughput mutagenic analysis of yeast sumo structure and function.Post-translational modifications of PML: consequences and implications.SUMO: a multifaceted modifier of chromatin structure and function.Global analysis of SUMO chain function reveals multiple roles in chromatin regulation.p53 SUMOylation promotes its nuclear export by facilitating its release from the nuclear export receptor CRM1Acetylation within the First 17 Residues of Huntingtin Exon 1 Alters Aggregation and Lipid Binding.Anticancer effects of valproic acid on oral squamous cell carcinoma via SUMOylation in vivo and in vitro.Regulation of the tumor suppressor PML by sequential post-translational modifications.Starting and stopping SUMOylation. What regulates the regulator?The SUMO system: a master organizer of nuclear protein assemblies.SUMO and Parkinson's disease.SUMO rules: regulatory concepts and their implication in neurologic functions.PML tumour suppression and beyond: therapeutic implications.Sumoylation and the DNA damage responseUbiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism.Molecular Basis for Phosphorylation-dependent SUMO Recognition by the DNA Repair Protein RAP80.Class I HDAC inhibition stimulates cardiac protein SUMOylation through a post-translational mechanism.CBP-mediated SMN acetylation modulates Cajal body biogenesis and the cytoplasmic targeting of SMN.Multiple crosstalks between mRNA biogenesis and SUMO.Identification and Characterization of SUMO-SIM Interactions.Beyond Histones: New Substrate Proteins of Lysine Deacetylases in Arabidopsis Nuclei.PIAS1 protects against myocardial ischemia-reperfusion injury by stimulating PPARγ SUMOylationAn E2-ubiquitin thioester-driven approach to identify substrates modified with ubiquitin and ubiquitin-like molecules
P2860
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P2860
An acetylation switch regulates SUMO-dependent protein interaction networks.
description
2012 nî lūn-bûn
@nan
2012年の論文
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2012年学术文章
@wuu
2012年学术文章
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2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
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2012年學術文章
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2012年學術文章
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name
An acetylation switch regulates SUMO-dependent protein interaction networks.
@en
An acetylation switch regulates SUMO-dependent protein interaction networks.
@nl
type
label
An acetylation switch regulates SUMO-dependent protein interaction networks.
@en
An acetylation switch regulates SUMO-dependent protein interaction networks.
@nl
prefLabel
An acetylation switch regulates SUMO-dependent protein interaction networks.
@en
An acetylation switch regulates SUMO-dependent protein interaction networks.
@nl
P2093
P2860
P1433
P1476
An acetylation switch regulates SUMO-dependent protein interaction networks
@en
P2093
Christopher D Chien
Maria Laura Avantaggiati
Rebecca Ullmann
P2860
P304
P356
10.1016/J.MOLCEL.2012.04.006
P577
2012-05-10T00:00:00Z