LPS-induced formation of immunoproteasomes: TNF-α and nitric oxide production are regulated by altered composition of proteasome-active sites. - Wikidata - awgldk - TriplyDB

LPS-induced formation of immunoproteasomes: TNF-α and nitric oxide production are regulated by altered composition of proteasome-active sites.

LPS-induced formation of immunoproteasomes: TNF-α and nitric oxide production are regulated by altered composition of proteasome-active sites.

http://www.wikidata.org/entity/Q39566694

about

Immunoproteasome deficiency modifies the alternative pathway of NFκB signaling New Insights into the Function of the Immunoproteasome in Immune and Nonimmune Cells Mechanisms of HIV protein degradation into epitopes: implications for vaccine design Co-operation of TLR4 and raft proteins in LPS-induced pro-inflammatory signaling Suppression of nitric oxide induction and pro-inflammatory cytokines by novel proteasome inhibitors in various experimental models The immunoproteasomes regulate LPS-induced TRIF/TRAM signaling pathway in murine macrophages.Inhibition of nitric oxide and inflammatory cytokines in LPS-stimulated murine macrophages by resveratrol, a potent proteasome inhibitor Proteasome protease mediated regulation of cytokine induction and inflammation.Nutritional Supplement-5 with a Combination of Proteasome Inhibitors (Resveratrol, Quercetin, δ-Tocotrienol) Modulate Age-Associated Biomarkers and Cardiovascular Lipid Parameters in Human Subjects.Quantitative proteomic analysis of hepatocyte-secreted extracellular vesicles reveals candidate markers for liver toxicity Immunoproteasome dysfunction augments alternative polarization of alveolar macrophages.Long-lasting effect of infant rats endotoxemia on heat shock protein 60 in the pancreatic acinar cells: involvement of toll-like receptor 4 Of Mice and Men: Proteasome's Role in LPS-Induced Inflammation and Tolerance.Pluripotent Stem Cell Model of Nakajo-Nishimura Syndrome Untangles Proinflammatory Pathways Mediated by Oxidative Stress.Dingchuan tang essential oil inhibits the production of inflammatory mediators via suppressing the IRAK/NF-κB, IRAK/AP-1, and TBK1/IRF3 pathways in lipopolysaccharide-stimulated RAW264.7 cells

P2860

Q21133685-98257C90-B1F7-4DE4-B504-7197AD978783 Q26774372-532BA435-8B5C-4F04-9442-CA108E202745 Q26866505-401540B7-A0EB-412A-9A34-F8BDDB201FFA Q26866939-2C23BABD-952D-48A3-AB3D-D321D7E823F8 Q35505150-4BBF4F82-4092-44C0-B0FF-49F7DD761FEF Q35539348-1F7D7625-985D-4B5A-B546-C7BF1D949E3E Q36086859-EE9D910A-AB57-4734-8548-CCD576840BC9 Q36301130-519E437C-89F9-4902-B4E2-F869191F1CB0 Q37364057-EC73CC11-6E0A-4A40-B1F5-112F51F665B1 Q37428949-70D5C74A-C36C-4DF5-96B2-A18BE41230D1 Q41727507-DD973F8F-09AC-4AE3-AB27-ACFB8DED778B Q42128315-340F784E-9A5A-48C0-8B12-4CAF31F5E8CF Q53720678-331BD524-3511-44EB-989B-D28851B3031B Q54957638-7D7A0F3A-E15E-452B-97F5-3C5871F6C310 Q58764997-D417FA2D-6267-4754-96A7-2A175E399896

P2860

LPS-induced formation of immunoproteasomes: TNF-α and nitric oxide production are regulated by altered composition of proteasome-active sites.

http://www.wikidata.org/entity/Q39566694

description

2011 nî lūn-bûn

@nan

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

2011年论文

@zh

2011年论文

@zh-cn

name

LPS-induced formation of immun ...... on of proteasome-active sites.

@en

LPS-induced formation of immun ...... on of proteasome-active sites.

@nl

type

label

LPS-induced formation of immun ...... on of proteasome-active sites.

@en

LPS-induced formation of immun ...... on of proteasome-active sites.

@nl

prefLabel

LPS-induced formation of immun ...... on of proteasome-active sites.

@en

LPS-induced formation of immun ...... on of proteasome-active sites.

@nl

P1433

Q39566694-0744DC20-911C-4982-8E39-E0A7B8F233A1

P1476

Q39566694-75F28876-4690-4389-8F4C-7DADAF26CDAF

P2093

Q39566694-1CF20696-3D25-49BC-8ED1-E32AC8B7F770

Q39566694-4D3B75E5-4A5F-4837-A048-D923516F2A2E

Q39566694-5E54C319-797E-464B-9AF7-2C62637816BE

Q39566694-6141F696-BCEE-4D0A-82AC-8785692A0C35

Q39566694-61A3EAA2-7470-4F61-ADA9-746D24D8EB30

Q39566694-7A62D43B-5449-42C5-B792-5911432560AF

Q39566694-8D2F9631-C227-4A6C-962D-CC561C22096D

Q39566694-8D64557F-4573-4AD7-AA3E-F6F20CBCA621

Q39566694-D85D1EF7-400C-4FD3-9061-C5D4E7E9CA3B

P2860

Q39566694-00B3B99D-764A-45A3-8954-6A1CF0901B0E

Q39566694-052E5FB6-18DF-40A2-B1B1-29542B0427EE

Q39566694-0FC6A8E6-3774-4BC4-81A2-E3A59B1FC9F1

Q39566694-20513906-B886-4705-9673-C1345F9E5A9C

Q39566694-3432CD1C-46EE-4172-BE42-F60E92DFE0C2

Q39566694-435BB9CD-CBCF-4C2D-8FC4-34390E9365C0

Q39566694-47C141F8-45A6-4C7E-AA80-EEA9642D39AA

Q39566694-513F5AC3-459F-418D-AF87-E3A6C1980A8D

Q39566694-55121154-1CCD-4BC0-9763-5BB094CB0D0D

Q39566694-6E022E70-028A-4BF6-8BEF-BA7B84FE140F

P2888

Q39566694-EABE9605-9DA8-47B2-8839-2CB7E3D3283D

P304

Q39566694-0E9274E3-AECD-4D24-BE06-F7215EE09D76

P31

Q39566694-BF07C417-4BE2-43B1-92B9-5B8E4A07CFF4

P356

Q39566694-34D9E82B-8B4E-42F5-B20C-A922D6865753

P433

Q39566694-0DA6CF7D-29D1-48E2-A9F3-70642223D92D

P478

Q39566694-0633056B-7E04-431A-8758-E650A7CAB513

P577

Q39566694-CEED9F17-1483-451D-923B-F7CEC67EC49A

P5875

Q39566694-47ED7111-7F12-4905-8B78-E5B3E41F0F76

P698

Q39566694-D634E47E-D7F7-4B2D-8258-66F80E8BDD42

P921

Q39566694-907CB2ED-6153-40C0-9DF8-54AED5B96441

P932

Q39566694-00881A0F-0D70-4358-BBCD-C6E8E268B27E

P356

S12013-011-9182-8

P1433

Cell Biochemistry and Biophysics

P1476

LPS-induced formation of immun ...... on of proteasome-active sites.

@en

P2093

Alexei F Kisselev

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

Asaf A Qureshi

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

Charles W Van Way

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

Christopher J Papasian

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

David C Morrison

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

Julia Reis

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

Nilofer Qureshi

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

Stefanie N Vogel

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

Xiu Qin Guan

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

P2860

The complete primary structure of mouse 20S proteasomes

Role of adaptor TRIF in the MyD88-independent toll-like receptor signaling pathway

The proteasome as a lipopolysaccharide-binding protein in macrophages: differential effects of proteasome inhibition on lipopolysaccharide-induced signaling events

Regulation of tumor necrosis factor alpha transcription in macrophages: involvement of four kappa B-like motifs and of constitutive and inducible forms of NF-kappa B

Rapid colorimetric assay for cell growth and survival. Modifications to the tetrazolium dye procedure giving improved sensitivity and reliability

The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B

Abnormally high expression of proteasomes in human leukemic cells.

The proteasome activator 11 S REG (PA28) and class I antigen presentation

Intracellular targeting of the proteasome.

The proteasome regulates bacterial CpG DNA-induced signaling pathways in murine macrophages

P2888

s12013-011-9182-8

P304

77-88

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

P31

scholarly article

P356

10.1007/S12013-011-9182-8

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

P433

1-2

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

P478

60

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

P577

2011-06-01T00:00:00Z

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

P5875

50940855

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

P698

21455682

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

P921

P932

3119080

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