Elafin prevents lipopolysaccharide-induced AP-1 and NF-kappaB activation via an effect on the ubiquitin-proteasome pathway. - Wikidata - awgldk - TriplyDB

Elafin prevents lipopolysaccharide-induced AP-1 and NF-kappaB activation via an effect on the ubiquitin-proteasome pathway.

Elafin prevents lipopolysaccharide-induced AP-1 and NF-kappaB activation via an effect on the ubiquitin-proteasome pathway.

http://www.wikidata.org/entity/Q53598924

about

Functional domains of the human epididymal protease inhibitor, eppin The Role of Serine Proteases and Antiproteases in the Cystic Fibrosis Lung A comparative proteomic analysis of the soluble immune factor environment of rectal and oral mucosa.Inflammation and immunity in the pathogenesis of pulmonary arterial hypertension Trappin-2/elafin modulate innate immune responses of human endometrial epithelial cells to PolyI:C Anti-HIV-1 activity of elafin depends on its nuclear localization and altered innate immune activation in female genital epithelial cells.Inhibiting lung elastase activity enables lung growth in mechanically ventilated newborn mice.Activated microglia/macrophage whey acidic protein (AMWAP) inhibits NFκB signaling and induces a neuroprotective phenotype in microglia.A functional variant of elafin with improved anti-inflammatory activity for pulmonary inflammation.Elafin Reverses Pulmonary Hypertension via Caveolin-1-Dependent Bone Morphogenetic Protein Signaling.Anti-HIV-1 activity of elafin is more potent than its precursor's, trappin-2, in genital epithelial cells Functional study of elafin cleaved by Pseudomonas aeruginosa metalloproteinases.Neonatal mice genetically modified to express the elastase inhibitor elafin are protected against the adverse effects of mechanical ventilation on lung growth Elafin, an elastase-specific inhibitor, is cleaved by its cognate enzyme neutrophil elastase in sputum from individuals with cystic fibrosis Antiviral activity of trappin-2 and elafin in vitro and in vivo against genital herpes.Trappin-2 promotes early clearance of Pseudomonas aeruginosa through CD14-dependent macrophage activation and neutrophil recruitment Proteases and antiproteases in chronic neutrophilic lung disease - relevance to drug discovery.The antimicrobial molecule trappin-2/elafin has anti-parasitic properties and is protective in vivo in a murine model of cerebral malaria.Diverse macrophage populations mediate acute lung inflammation and resolution.Secretory leukocyte protease inhibitor and elafin/trappin-2: versatile mucosal antimicrobials and regulators of immunity.WAP domain proteins as modulators of mucosal immunity.War and peace between WAP and HIV: role of SLPI, trappin-2, elafin and ps20 in susceptibility to HIV infection.SLPI and elafin: multifunctional antiproteases of the WFDC family.SLPI and trappin-2 as therapeutic agents to target airway serine proteases in inflammatory lung diseases: current and future directions.Therapeutic potential of human elafin.The role of serpin and cystatin antiproteases in mucosal innate immunity and their defense against HIV.Lactic acid bacteria as mucosal delivery vehicles: a realistic therapeutic option.Elafin (SKALP/Trappin-2/proteinase inhibitor-3) is produced by the cervix in pregnancy and cervicovaginal levels are diminished in bacterial vaginosis.MG-132 inhibits telomerase activity, induces apoptosis and G(1) arrest associated with upregulated p27kip1 expression and downregulated survivin expression in gastric carcinoma cells.A role for whey acidic protein four-disulfide-core 12 (WFDC12) in the regulation of the inflammatory response in the lung.Protease inhibitors derived from elafin and SLPI and engineered to have enhanced specificity towards neutrophil serine proteases.Serine protease inhibitors protect better than IL-10 and TGF-β anti-inflammatory cytokines against mouse colitis when delivered by recombinant lactococci.Differential effects of periopathogens on host protease inhibitors SLPI, elafin, SCCA1, and SCCA2.

P2860

Q24309156-855EADA1-1D6D-459A-9BF1-067346885F4E Q26799771-818B3F51-B98E-4443-A243-A8D0C8466AB0 Q33825756-2BA3FD69-7B54-43FE-AE2D-5B5A839C4A97 Q33898213-71BCD0C9-062E-4A64-A761-05E24EBFC5CE Q34251265-C09E30B7-8E4E-4ECD-815A-5ACA028C7822 Q34541093-06D6B916-05C4-4D49-B0C4-652F9141B861 Q35219764-A8C0FE40-2311-4E91-A584-A9BC03BC76BC Q35562493-542CA049-3039-4393-A2FF-CF14CDF15114 Q35591399-C4E740D2-9D26-417A-BD43-2C018D752CB9 Q35766693-0FEF68E9-7DA1-46EE-BABB-A959BDE6D067 Q35868058-7EBBDA97-B3E1-4A2F-BB1C-908449748F5A Q36093198-8BD5F1BB-B58B-4957-87EB-D022ED376FF1 Q36178195-035C9B8A-90BA-4FBC-8641-7C0D0E9DA112 Q36973716-4AC366B4-DF64-42B7-B5BB-0417A1913777 Q36978882-D0337A64-1122-4218-8B8A-267F5A6D9F25 Q37164539-63E8A7E9-A2EF-464B-81B4-2C805DCAD2AE Q37447482-9C32272C-C41F-47AC-93C8-EC009CC25DD5 Q37633868-1140CCC1-21E6-4F6D-AD23-7260CBA2E5C1 Q37707609-90A4E16B-DAB7-4555-98B7-D1A8B67B6F2C Q37731798-998C4D74-C8E7-4A13-862F-C1639776EBF5 Q37936531-EB9EAA03-4CC7-4DFD-895D-80AAA6FAE555 Q37936538-E36D2954-9F85-43A4-8043-9999F9D240AC Q37936541-C9CD1BA9-4E55-48DC-A800-8A60B3F298D3 Q37936542-BE6E79E9-7971-496F-AC09-596D5F14CC09 Q37936546-D20693C6-AE5A-4CF9-9524-2F481CECD1C7 Q38170193-796776E5-4E77-42A7-89FF-1D869C0A2B0A Q38827869-911C01C8-CF9B-4D27-8066-3EFAE7CBACBF Q39805118-3CCA7684-0921-4654-95C1-417C8A974F9F Q39903879-55623CDC-9E4A-425D-8B2A-9C4A259866CA Q41431968-C3978A8F-6B75-47B1-BBA1-349B342B58CA Q41818079-921C5714-8782-4E17-A3C5-1CB2332647BF Q41981077-5FE3C841-BCD6-40CC-A649-E66FD0BD98A7 Q42723859-CFD8D038-3664-4F6C-B655-6859FEB88F13

P2860

Elafin prevents lipopolysaccharide-induced AP-1 and NF-kappaB activation via an effect on the ubiquitin-proteasome pathway.

http://www.wikidata.org/entity/Q53598924

description

2006 nî lūn-bûn

@nan

2006年の論文

@ja

2006年学术文章

@wuu

2006年学术文章

@zh-cn

2006年学术文章

@zh-hans

2006年学术文章

@zh-my

2006年学术文章

@zh-sg

2006年學術文章

@yue

2006年學術文章

@zh

2006年學術文章

@zh-hant

name

Elafin prevents lipopolysaccha ...... ubiquitin-proteasome pathway.

@en

Elafin prevents lipopolysaccha ...... ubiquitin-proteasome pathway.

@nl

type

label

Elafin prevents lipopolysaccha ...... ubiquitin-proteasome pathway.

@en

Elafin prevents lipopolysaccha ...... ubiquitin-proteasome pathway.

@nl

prefLabel

Elafin prevents lipopolysaccha ...... ubiquitin-proteasome pathway.

@en

Elafin prevents lipopolysaccha ...... ubiquitin-proteasome pathway.

@nl

P1433

Q53598924-00ADCE94-5767-4FBB-B9D3-66DF62752807

P1476

Q53598924-EE9C9768-7B21-4E98-8A4D-BB6312782A93

P2093

Q53598924-57C2C1F6-BE10-414E-8456-2B36B06DF4A6

Q53598924-73D58FB9-233E-40BE-946D-32C32582A9AE

Q53598924-CEEAFDAF-9FC1-44D8-9FC3-BFE145949DBE

Q53598924-D8FBC513-9BD9-4819-A13D-82004F305F2B

P2860

Q53598924-02981958-783C-4DAF-832E-C998867320C3

Q53598924-052351EF-9AF7-42F2-95E7-6C8EAE16B16D

Q53598924-0F5322ED-7BC5-44DF-8C2C-CA781420C68E

Q53598924-156D2AE6-5B75-4DA3-B5DD-889209A96D3D

Q53598924-2A1DE2EC-43E6-4B07-805A-5704B6FFFA09

Q53598924-2D313E7C-E662-4A2A-8140-5B845F5295E4

Q53598924-37CE83BD-A415-4CE6-9F17-6532DD091B3E

Q53598924-3D944499-C449-4456-B983-738D4718CBB5

Q53598924-42369678-06C5-4F55-B504-3AEF3824A2C6

Q53598924-49291086-0995-4BD2-80E7-47004D842807

P304

Q53598924-5BD86BB1-FB9A-41BD-824A-8C5B768FB369

P31

Q53598924-05DC64D2-85E3-4937-833A-89148352323F

P356

Q53598924-074ED837-BBAC-4420-B7FC-2BA79BFDCEFA

P407

Q53598924-1D17CC2F-1541-4D09-8992-C4139EEEA4A1

P433

Q53598924-13FF5FD7-683F-459B-9661-6E91FB5B217B

P478

Q53598924-BFCEAA7E-D8B1-4AB7-8462-26975933EC17

P50

Q53598924-6D8D34DC-3DCB-432C-9C04-EC85C653DD51

Q53598924-FE8A6B53-438C-4F16-B70C-4F5B93FB1E3F

P577

Q53598924-83421E6B-8F09-4BDC-B5EE-9DA9C9700AB2

P698

Q53598924-A7FEF36F-6067-4BB8-8D8B-ECB08E8EC912

P921

Q53598924-98393BFD-1EEB-409F-A0C0-737979895A6A

P356

P1433

Journal of Biological Chemistry

P1476

Elafin prevents lipopolysaccha ...... e ubiquitin-proteasome pathway

@en

P2093

Ian Robertson

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

Marcus W Butler

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

Noel G McElvaney

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

Shane J O'Neill

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

P2860

The trappin gene family: proteins defined by an N-terminal transglutaminase substrate domain and a C-terminal four-disulphide core

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Signal transduction by the JNK group of MAP kinases

Signal transduction by the lipopolysaccharide receptor, Toll-like receptor-4

TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40, and LPS signaling

Impaired monocyte migration and reduced type 1 (Th1) cytokine responses in C-C chemokine receptor 2 knockout mice

Severe reduction in leukocyte adhesion and monocyte extravasation in mice deficient in CC chemokine receptor 2.

Targeted disruption of the MyD88 gene results in loss of IL-1- and IL-18-mediated function

LPS induction of gene expression in human monocytes.

Defects in macrophage recruitment and host defense in mice lacking the CCR2 chemokine receptor

P304

34730-34735

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

P31

scholarly article

P356

10.1074/JBC.M604844200

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

P407

P433

46

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

P478

281

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

P50

Catherine M Greene

Clifford C Taggart

P577

2006-09-15T00:00:00Z

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

P698

16980310

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

P921

lipopolysaccharide