Nitric oxide destabilizes Pias3 and regulates sumoylation - sprookjes - yvandenbroek - TriplyDB

Nitric oxide destabilizes Pias3 and regulates sumoylation

Nitric oxide destabilizes Pias3 and regulates sumoylation

http://www.wikidata.org/entity/Q27302404

about

Calpain 3 is a rapid-action, unidirectional proteolytic switch central to muscle remodeling TRIM family proteins and their emerging roles in innate immunity Loss of protein inhibitors of activated STAT-3 expression in glioblastoma multiforme tumors: implications for STAT-3 activation and gene expression The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition.Sumoylation regulates nuclear localization of lipin-1alpha in neuronal cells.Lipin proteins form homo- and hetero-oligomers Silencing of the JNK pathway maintains progesterone receptor activity in decidualizing human endometrial stromal cells exposed to oxidative stress signals.Comprehensively surveying structure and function of RING domains from Drosophila melanogaster Emerging roles of SUMO modification in arthritis.Xanthine oxidoreductase promotes the inflammatory state of mononuclear phagocytes through effects on chemokine expression, peroxisome proliferator-activated receptor-{gamma} sumoylation, and HIF-1{alpha}SUMOylation occurs in acute kidney injury and plays a cytoprotective role The role of small ubiquitin-like modifier-interacting motif in the assembly and regulation of metal-responsive transcription factor 1.Regulation by S-nitrosylation of protein post-translational modification.Lipopolysaccharides Promote S-Nitrosylation and Proteasomal Degradation of Liver Kinase B1 (LKB1) in Macrophages in Vivo SNOs Differ: Methodological and Biological Implications.Quantitative proteomic analysis of S-nitrosated proteins in diabetic mouse liver with ICAT switch method.Protein Inhibitor of Activated STAT3 (PIAS3) Is Down-Regulated in Eutopic Endometrium of Women with Endometriosis.Repression of classical nuclear export by S-nitrosylation of CRM1.Protein Inhibitor of Activated STAT3 Suppresses Oxidized LDL-induced Cell Responses during Atherosclerosis in Apolipoprotein E-deficient Mice.SUMO rules: regulatory concepts and their implication in neurologic functions.Ubiquitin-Conjugating Enzyme 9 Phosphorylation as a Novel Mechanism for Potentiation of the Inflammatory Response.Gating neural development and aging via nuclear pores.Nuclear Smad6 promotes gliomagenesis by negatively regulating PIAS3-mediated STAT3 inhibition.

P2860

Q24294688-CDA57E8E-8894-4FCD-A85B-DBBCF357D936 Q24607229-C18F3147-98B8-4A5F-89A6-8D82F6E8178F Q24619748-6EA1D9F5-F38F-46D4-8E63-E0CBAB423088 Q27865256-CD8A8623-2014-44F6-9734-844235280B3B Q28587748-E2A28778-343C-4715-9A6C-31CC02326284 Q30431845-D1B8600D-A24F-45CE-8359-0A7D15654FFB Q33803307-6E76C6A9-BB99-47A9-813C-89A9C5194D6C Q34017765-AB07467A-8360-4A2C-9BFB-6F9DCF28A534 Q34108064-35B1C49B-5707-4B73-9312-E2EFF6352A61 Q34489192-13CD0ED9-1CF6-4053-8AD8-4EEE18A48BD4 Q35275798-3E48255A-C2A5-4F67-8E65-B401A867E3A9 Q35604640-92F9CFBD-4DDA-49D0-A7CE-F91254A8FB79 Q35763044-274E912D-E475-4600-8906-404A16D7C300 Q35905322-AE49FE73-5506-404D-AC80-529F8302678B Q36232644-B10B3A1E-D161-4D52-8516-BF4DC75BA0B9 Q36922808-4C37C782-95BB-41CB-8DFB-5D967A34B889 Q37268557-8D6B4FCD-CDE4-4150-8ADE-269193FF0B6B Q37379750-FDE9DE51-50BA-4596-86CC-2DD84B0F669B Q37414017-07ECFD1A-30AB-4290-B90C-FBB35AE25993 Q38132691-DC60DEE3-4976-48DD-BFA8-8309642F1AA5 Q41022416-91D3CDCC-DCFA-40F0-B93B-C48E0E40A989 Q42260512-9B292A2B-7214-42BC-B6CA-FCCCC59DE794 Q55363685-2D8A33C5-624C-4CE2-808C-4C08DB3A7D6A

P2860

Nitric oxide destabilizes Pias3 and regulates sumoylation

http://www.wikidata.org/entity/Q27302404

description

2007 nî lūn-bûn

@nan

2007 թուականին հրատարակուած գիտական յօդուած

@hyw

2007 թվականին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

Nitric oxide destabilizes Pias3 and regulates sumoylation

@ast

Nitric oxide destabilizes Pias3 and regulates sumoylation

@en

Nitric oxide destabilizes Pias3 and regulates sumoylation

@nl

type

label

Nitric oxide destabilizes Pias3 and regulates sumoylation

@ast

Nitric oxide destabilizes Pias3 and regulates sumoylation

@en

Nitric oxide destabilizes Pias3 and regulates sumoylation

@nl

prefLabel

Nitric oxide destabilizes Pias3 and regulates sumoylation

@ast

Nitric oxide destabilizes Pias3 and regulates sumoylation

@en

Nitric oxide destabilizes Pias3 and regulates sumoylation

@nl

P1433

Q27302404-0CD16BE5-1869-439C-8A9D-2A63DD57A061

P1476

Q27302404-D5171E06-FBCB-4AB8-9277-560DD03AEEDF

P2093

Q27302404-516FC6B6-4426-49CA-92A0-CA87FB44BCF1

Q27302404-80919DFA-CAEA-419D-AA77-30346213D1E5

Q27302404-A49D65EC-C843-4E70-8601-DC4AA28260B8

Q27302404-A89324BB-AA4E-4F5E-BC42-37CA0DABC4D0

Q27302404-CA603AAB-1115-479C-8F6A-7712A3A780B7

Q27302404-D114E074-09E7-48B6-9C9D-692E953D3A56

Q27302404-D4772AA0-44BC-402C-AEEC-99E2F1CD749D

Q27302404-E85D2693-BC28-46AD-A588-BD44FDE84BB6

P2860

Q27302404-06E61498-00D3-4408-8208-33C0C7EDE4DA

Q27302404-1C1C142E-5C31-49A8-B281-D511F550F877

Q27302404-308DB5C4-4843-43DC-8E65-1A305EEE39D0

Q27302404-31463DF8-57A8-4E57-8A50-1B55A8F1B5AA

Q27302404-412A4C3A-E63E-4FC5-B63D-48176CB09435

Q27302404-45B475D4-73F3-4AD0-8641-44094B087077

Q27302404-488CAA14-E3B6-4627-A771-80CB1D6F508E

Q27302404-4B05838C-88EB-40B2-A3C7-31C9B8C9615B

Q27302404-4EC05261-35EF-438E-BB91-010A1AA8BF4D

Q27302404-689FBC7B-9C80-43C7-9876-1B5B2A7AD31B

P304

Q27302404-7B258995-0E13-4EA8-B47F-A80B4F7DD389

P31

Q27302404-E89C4AE0-AABA-4EB1-991D-56D49E52AAB4

P3181

Q27302404-555E87DD-7A44-40A4-A23A-50C2E777E7BE

P356

Q27302404-4B99A1DC-740E-44F0-9CA2-9219C83519A5

P407

Q27302404-857ECE98-A66B-48B9-B4B9-2AF79805556E

P433

Q27302404-3D734C50-0D33-4AEE-81CB-8C9B71455C0A

P478

Q27302404-4A17EB38-AA8C-4FFF-B775-F5134E0A81FD

P577

Q27302404-50F58CE4-498B-4E4D-86A3-590FA2B4BB5B

P5875

Q27302404-8D940596-A235-4881-8FFF-41633CE69E81

P698

Q27302404-8BF5D097-EAC3-415B-B716-9F40EFBF3D66

P932

Q27302404-40BF67D8-920E-4A53-A3BF-137AE613D9F6

P3181

P356

JOURNAL.PONE.0001085

P1433

P1476

Nitric oxide destabilizes Pias3 and regulates sumoylation

@en

P2093

Chang Chen

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

Guang-Hui Liu

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

Jiangmei Li

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

Jing Qu

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

Kaiyuan Wu

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

Peiwei Han

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

Peng Wang

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

Xu Zhang

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

P2860

Association of the human SUMO-1 protease SENP2 with the nuclear pore

PIAS3 suppresses NF-kappaB-mediated transcription by interacting with the p65/RelA subunit

The interaction of Piasy with Trim32, an E3-ubiquitin ligase mutated in limb-girdle muscular dystrophy type 2H, promotes Piasy degradation and regulates UVB-induced keratinocyte apoptosis through NFkappaB

Regulation of MBD1-mediated transcriptional repression by SUMO and PIAS proteins

PIAS3 interacts with ATF1 and regulates the human ferritin H gene through an antioxidant-responsive element

Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9.

The nucleoporin RanBP2 has SUMO1 E3 ligase activity

The polycomb protein Pc2 is a SUMO E3

Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1.

S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration

P304

e1085

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

P31

scholarly article

P3181

2565931

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

P356

10.1371/JOURNAL.PONE.0001085

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

P407

P433

10

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

P478

2

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

P577

2007-01-01T00:00:00Z

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

P5875

5859888

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

P698

17987106

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

P932

2064872

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