SUMO2/3 conjugation is an endogenous neuroprotective mechanism. - Wikidata - awgldk - TriplyDB

SUMO2/3 conjugation is an endogenous neuroprotective mechanism.

SUMO2/3 conjugation is an endogenous neuroprotective mechanism.

http://www.wikidata.org/entity/Q35534157

about

Detecting endogenous SUMO targets in mammalian cells and tissues.Interaction of ARC and Daxx: A Novel Endogenous Target to Preserve Motor Function and Cell Loss after Focal Brain Ischemia in Mice Patterns of ubiquitylation and SUMOylation associated with exposure to anoxia in embryos of the annual killifish Austrofundulus limnaeus Tomosyn interacts with the SUMO E3 ligase PIASγ.SUMO3 modification accelerates the aggregation of ALS-linked SOD1 mutants.Elevated global SUMOylation in Ubc9 transgenic mice protects their brains against focal cerebral ischemic damage.Neuronal SUMOylation: mechanisms, physiology, and roles in neuronal dysfunction.Global SUMOylation is a molecular mechanism underlying hypothermia-induced ischemic tolerance Selective antegrade cerebral perfusion reduces brain injury following deep hypothermic circulatory arrest in the piglets' model by decreasing the levels of protein SUMO2/3-ylation.SUMO2/3 is associated with ubiquitinated protein aggregates in the mouse neocortex after middle cerebral artery occlusion Histone acetylation and CREB binding protein are required for neuronal resistance against ischemic injury.SUMO proteomics to decipher the SUMO-modified proteome regulated by various diseases.SUMOylation occurs in acute kidney injury and plays a cytoprotective role Reperfusion rather than ischemia drives the formation of ubiquitin aggregates after middle cerebral artery occlusion Inhibition of histone methyltransferases SUV39H1 and G9a leads to neuroprotection in an in vitro model of cerebral ischemia.Moderate hypothermia induces marked increase in levels and nuclear accumulation of SUMO2/3-conjugated proteins in neurons.A Proteomic Approach to Identify Alterations in the Small Ubiquitin-like Modifier (SUMO) Network during Controlled Mechanical Ventilation in Rat Diaphragm Muscle.O-linked β-N-acetylglucosamine modification of proteins is activated in post-ischemic brains of young but not aged mice: Implications for impaired functional recovery from ischemic stress Analysis of oxygen/glucose-deprivation-induced changes in SUMO3 conjugation using SILAC-based quantitative proteomics.Global SUMOylation facilitates the multimodal neuroprotection afforded by quercetin against the deleterious effects of oxygen/glucose deprivation and the restoration of oxygen/glucose.PIAS1 Regulates Mutant Huntingtin Accumulation and Huntington's Disease-Associated Phenotypes In Vivo SUMO-2 and PIAS1 modulate insoluble mutant huntingtin protein accumulation.SUMO-specific protease 1 protects neurons from apoptotic death during transient brain ischemia/reperfusion.SUMOylation of NaV1.2 channels mediates the early response to acute hypoxia in central neurons.Protein SUMOylation, an emerging pathway in amyotrophic lateral sclerosis.SUMO and ischemic tolerance.Molecular targets underlying SUMO-mediated neuroprotection in brain ischemia.Receptor trafficking and the regulation of synaptic plasticity by SUMO.SUMO rules: regulatory concepts and their implication in neurologic functions.RNA metabolism in ALS: when normal processes become pathological.Small ubiquitin-like modifier 3-modified proteome regulated by brain ischemia in novel small ubiquitin-like modifier transgenic mice: putative protective proteins/pathways.SUMO-regulated transcription: challenging the dogma.Neuron-specific SUMO knockdown suppresses global gene expression response and worsens functional outcome after transient forebrain ischemia in mice.Ubiquitin-dependent and independent roles of SUMO in proteostasis.SENP3-mediated deSUMOylation of dynamin-related protein 1 promotes cell death following ischaemia.The activity of the glucocorticoid receptor is regulated by SUMO conjugation to FKBP51.DJ-1 protects the heart against ischemia-reperfusion injury by regulating mitochondrial fission.Sumoylation as an Integral Mechanism in Bacterial Infection and Disease Progression.ICAM1 depletion reduces spinal metastasis formation in vivo and improves neurological outcome.Targeting the SUMO pathway for neuroprotection in brain ischaemia.

P2860

Q27865266-4EFAF726-38C9-4C73-9FC5-5FE2BC8145FD Q28595484-6A08AC1F-3B99-4B33-8491-2426B42D1DD3 Q30356816-D4D6155B-429E-43BA-AC56-14138011D93B Q31153788-32192F50-CB8D-435B-B756-BCFBA7626664 Q33817594-91055FBB-7EB3-4568-9B40-E2FCB36C2B00 Q34053347-39CBA0BF-AB22-4C08-ADA1-80C7E4F78CC6 Q34295237-934360B0-5832-4550-AD57-5773F370D209 Q34630903-C5205A22-95C7-49D1-8D82-651AFCB1C6D8 Q34770195-F34030E2-364A-44B4-95C3-F1D95F812AF4 Q34957573-B9AB30FA-33F0-4257-91BC-941CFC38BE51 Q35153024-6A61DD15-8622-4342-8E08-A07745CD17F6 Q35245641-BF1746B1-C3B0-47FE-9E22-0DFE5DC65492 Q35275798-D9096A55-DAEA-4927-B9F8-D460033D12EB Q36113521-37990736-7350-4BF7-8244-56ECFED52A1A Q36267373-90DEE7D4-A267-42F5-A9BA-1980A0885DA5 Q36303526-1919DC18-49F4-428A-BD79-52ADC1AFE1F4 Q36333305-9BB2AC5E-6DC5-40AB-AE01-F1D8754FA672 Q36595831-C6365F7A-9ACE-417C-B034-6FA9B7832742 Q36773146-BD8C8197-6453-4FA1-9A7F-DB2C645F8E37 Q37026526-7F3C5759-272F-42E0-A860-DE31E29032BB Q37088539-3171C0C5-247D-408E-A5F4-E7E288CA3EF9 Q37596830-2DE5C259-7611-468C-82A2-87B2C39DD9F8 Q37603287-9D3286E7-F2B3-4F43-B08F-15B9814D8279 Q37616739-A64FCC46-0328-4949-8D1B-558345A327E0 Q38071685-FD3C5815-4EF0-425D-A689-92A052110323 Q38115253-FBDF9BF9-6B2C-4BDF-986B-E183CD17EF4B Q38115818-3C790AD1-7590-4C96-BE36-280906150CDD Q38128213-54F36471-932E-4744-838C-D3BB5D70F64C Q38132691-09C36B73-0B91-4A71-971C-3474D160982A Q38189807-04DD20E9-8FB6-4580-BABB-5AC1D47FB3D9 Q38531850-35D49308-2597-4F36-AF80-EEAB0196E08D Q38583743-66704FD3-7EBF-4681-A005-54F5D43D948F Q38786900-6F4851FE-6C07-490F-83F2-352B96D25A26 Q38874015-79787A58-72CC-43A0-A333-8F3F7932E0AD Q39176491-607042CB-EF71-4F7B-B109-40D01B0D815C Q39768470-BD09132F-9E99-46F3-893F-5287749B5921 Q39827142-DE0CB77C-D05A-46DF-BDC4-01FA6008DF94 Q40332990-7C6F4E24-E1DD-4B5D-A237-E16FD2AB5C02 Q41466240-4D2211E7-5369-49B1-88C6-0A9D0286A7C2 Q41678635-BC4BA77D-AD7F-4FD0-A227-51CB0A8D36B3

P2860

SUMO2/3 conjugation is an endogenous neuroprotective mechanism.

http://www.wikidata.org/entity/Q35534157

description

2011 nî lūn-bûn

@nan

2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

SUMO2/3 conjugation is an endogenous neuroprotective mechanism.

@ast

SUMO2/3 conjugation is an endogenous neuroprotective mechanism.

@en

type

label

SUMO2/3 conjugation is an endogenous neuroprotective mechanism.

@ast

SUMO2/3 conjugation is an endogenous neuroprotective mechanism.

@en

prefLabel

SUMO2/3 conjugation is an endogenous neuroprotective mechanism.

@ast

SUMO2/3 conjugation is an endogenous neuroprotective mechanism.

@en

P1433

Q35534157-82A8184B-E153-4A0D-B323-2E3D9C7DA332

P1476

Q35534157-2AEE9FB2-36DF-46F0-96C3-63C7C96815F4

P2093

Q35534157-032112C2-05C4-4F22-AB77-3AFFCADBF317

Q35534157-63978AE6-5FBF-4271-A861-FB21D8A92E02

Q35534157-C9489307-D938-44DF-8CBE-C25AD365A90C

Q35534157-D2AE3221-21C4-4541-BC3F-F723FCBB6CFF

Q35534157-F55C0C67-DCB8-4526-847A-DAA163BBC4F4

P2860

Q35534157-0659FBD3-A30B-4474-8E2B-F18C7D7072F6

Q35534157-08A327D5-7A0B-4B70-9527-42987E26C8FE

Q35534157-2B6EC939-6CEE-4982-A6E8-669EB08D21BC

Q35534157-40930B7F-4E85-4692-8121-52EF7168E557

Q35534157-4E6007AA-5B47-4EA6-90DF-3D12C2680847

Q35534157-4FDC4862-48B1-48B6-963F-79F344CE3CF0

Q35534157-6D66EBF6-BDFC-4736-AB71-E6BE43B7F86D

Q35534157-771F289B-13DD-41C0-8F21-FD4C8D7801C2

Q35534157-77451D79-F919-40B9-B0EC-5BB6FF5D3B64

Q35534157-8F17C4D7-4212-48C2-8597-D2ED21974171

P304

Q35534157-F7DBFCEC-2D86-4A3A-B745-CFCD319101DF

P31

Q35534157-9B9C3652-5B46-41CC-97C9-882C584B9A39

P356

Q35534157-91101CEE-44C6-405C-97BF-A80363EDCDA7

P433

Q35534157-EA85159E-FAF1-42E9-B406-069CCC4872FE

P478

Q35534157-74731CD7-E65F-4476-B7E6-786E49C148E3

P50

Q35534157-4CA4403E-1E14-4652-B357-4A94CB437512

Q35534157-7D3364BA-B974-498B-A22F-1CBCA1E1CE0A

Q35534157-A4DEE271-7B77-4761-8372-D2A73BAF35FC

Q35534157-B2190082-0F8A-4134-A2D7-9C318E5AC87B

P577

Q35534157-D93D7F93-EB13-4F8B-A01C-DBC832D9C9F9

P5875

Q35534157-6970FA66-64C4-4BF7-A169-AD2AE6666649

P698

Q35534157-CE75DB99-338C-4FE0-AEF3-51571DCE1C56

P932

Q35534157-0BD245ED-A38C-47A7-BB61-095AF2178D92

P356

P1433

Journal of Cerebral Blood Flow & Metabolism

P1476

SUMO2/3 conjugation is an endogenous neuroprotective mechanism.

@en

P2093

Anna Lena Datwyler

http://www.w3.org/2001/XMLSchema#string

Matthias Endres

http://www.w3.org/2001/XMLSchema#string

Sabrina Lin Lin Lee

http://www.w3.org/2001/XMLSchema#string

Wei Yang

http://www.w3.org/2001/XMLSchema#string

Wulf Paschen

http://www.w3.org/2001/XMLSchema#string

P2860

System-wide changes to SUMO modifications in response to heat shock.

The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition.

A proteomic study of SUMO-2 target proteins

Phosphatidylinositol 3-Akt-kinase-dependent phosphorylation of p21(Waf1/Cip1) as a novel mechanism of neuroprotection by glucocorticoids

Fas/CD95 regulatory protein Faim2 is neuroprotective after transient brain ischemia

Lentivirus-based genetic manipulations of cortical neurons and their optical and electrophysiological monitoring in vivo.

Therapeutic hypothermia for acute ischemic stroke: ready to start large randomized trials?

Protein SUMOylation modulates calcium influx and glutamate release from presynaptic terminals

Protein SUMOylation is massively increased in hibernation torpor and is critical for the cytoprotection provided by ischemic preconditioning and hypothermia in SHSY5Y cells.

Emerging extranuclear roles of protein SUMOylation in neuronal function and dysfunction

P304

2152-2159

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1038/JCBFM.2011.112

http://www.w3.org/2001/XMLSchema#string

P433

11

http://www.w3.org/2001/XMLSchema#string

P478

31

http://www.w3.org/2001/XMLSchema#string

P50

Christoph Harms

Gisela Tünnemann

Anna Lena Datwyler

P577

2011-08-24T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

51591644

http://www.w3.org/2001/XMLSchema#string

P698

21863037

http://www.w3.org/2001/XMLSchema#string

P932

3210338

http://www.w3.org/2001/XMLSchema#string