SUMOylation of tissue transglutaminase as link between oxidative stress and inflammation. - Wikidata - wikimedia - TriplyDB

SUMOylation of tissue transglutaminase as link between oxidative stress and inflammation.

SUMOylation of tissue transglutaminase as link between oxidative stress and inflammation.

http://www.wikidata.org/entity/Q39821994

about

Manipulating proteostasis to repair the F508del-CFTR defect in cystic fibrosis The redox state of transglutaminase 2 controls arterial remodeling Transglutaminase 2 has opposing roles in the regulation of cellular functions as well as cell growth and death Protein transamidation by transglutaminase 2 in cells: a disputed Ca2+-dependent action of a multifunctional protein Cellular functions of tissue transglutaminase Physiological, pathological, and structural implications of non-enzymatic protein-protein interactions of the multifunctional human transglutaminase 2 The emerging potential of autophagy-based therapies in the treatment of cystic fibrosis lung infections Targeting vascular NADPH oxidase 1 blocks tumor angiogenesis through a PPARα mediated mechanism Genomic variants reveal differential evolutionary constraints on human transglutaminases and point towards unrecognized significance of transglutaminase 2.ROS-PIASγ cross talk channelizes ATM signaling from resistance to apoptosis during chemosensitization of resistant tumors.Transglutaminase regulation of cell function.Butyrate attenuates lipopolysaccharide-induced inflammation in intestinal cells and Crohn's mucosa through modulation of antioxidant defense machinery.Xanthine oxidoreductase promotes the inflammatory state of mononuclear phagocytes through effects on chemokine expression, peroxisome proliferator-activated receptor-{gamma} sumoylation, and HIF-1{alpha}Autophagy: a core cellular process with emerging links to pulmonary disease.Transglutaminase 2: a molecular Swiss army knife.Aberrant sumoylation signaling evoked by reactive oxygen species impairs protective function of Prdx6 by destabilization and repression of its transcription.Restoration of CFTR function in patients with cystic fibrosis carrying the F508del-CFTR mutation Targeting autophagy as a novel strategy for facilitating the therapeutic action of potentiators on ΔF508 cystic fibrosis transmembrane conductance regulator.Targeting the Intracellular Environment in Cystic Fibrosis: Restoring Autophagy as a Novel Strategy to Circumvent the CFTR Defect.Disease-relevant proteostasis regulation of cystic fibrosis transmembrane conductance regulator.Reduced caveolin-1 promotes hyperinflammation due to abnormal heme oxygenase-1 localization in lipopolysaccharide-challenged macrophages with dysfunctional cystic fibrosis transmembrane conductance regulator.Variations in both TG1 and TG2 isozyme-specific in situ activities and protein expressions during mouse embryonic development Salen Mn complexes mitigate radiation injury in normal tissues.Cysteamine re-establishes the clearance of Pseudomonas aeruginosa by macrophages bearing the cystic fibrosis-relevant F508del-CFTR mutation.How Förster resonance energy transfer imaging improves the understanding of protein interaction networks in cancer biology.Monitoring of transglutaminase 2 under different oxidative stress conditions.Autophagy: a primer for the gastroenterologist/hepatologist.miR-19-Mediated Inhibition of Transglutaminase-2 Leads to Enhanced Invasion and Metastasis in Colorectal Cancer.Nebulized hyaluronan ameliorates lung inflammation in cystic fibrosis mice.Computational analyses of the effect of novel amino acid clusters of human transglutaminase 2 on its structure and function.SUMO E3 Ligase PIASy Mediates High Glucose-Induced Activation of NF-κB Inflammatory Signaling in Rat Mesangial Cells.SUMO1 negatively regulates reactive oxygen species production from NADPH oxidases.Strategies for the etiological therapy of cystic fibrosis.SUMO1/UBC9‑decreased Nox1 activity inhibits reactive oxygen species generation and apoptosis in diabetic retinopathy.The kiwi fruit peptide kissper displays anti-inflammatory and anti-oxidant effects in in-vitro and ex-vivo human intestinal models.New Insights into Transglutaminase 2 and Links to Neurodegenerative Diseases.Isozyme-specific comprehensive characterization of transglutaminase-crosslinked substrates in kidney fibrosis.Sumoylation-deficient Prdx6 repairs aberrant Sumoylation-mediated Sp1 dysregulation-dependent Prdx6 repression and cell injury in aging and oxidative stress

P2860

Q26765794-0A3ED717-6293-4362-AEE5-43517D545BF4 Q27325795-8E3BBDF9-0C35-4B99-97CE-A326463AA667 Q28069852-36337E52-A1F6-45D2-A243-50B5CABA3DC3 Q28247511-E66F9F7F-57CE-4C05-AF08-10739B343E98 Q28260600-446D7201-0857-45C7-99A7-2120DDF0A620 Q28261578-674C844B-C9DF-4DD9-AF5C-50F4AF5B6389 Q28540241-D9764741-DB84-467F-8E88-AB2853317C06 Q28743072-EA4BEAB3-D09C-43EC-BCDD-3954C2EF3250 Q30399258-284AE4CC-DED9-4C79-B27D-A56677DD6FED Q33695127-DC0F18E2-CA1E-4D51-8567-23269278CE77 Q33707936-171C783A-F21D-488B-9426-F8276B400EF6 Q34193433-40A1A479-7853-4BFF-9F75-3A462D77BE8B Q34489192-D39B2890-CCE7-46DA-B35B-4D828F39D990 Q35683041-24BBD601-2280-4915-998D-E36A353575EB Q35693361-E0F7795A-43F6-4B5C-90CC-324E431F6E8F Q35760146-66E008FE-B53D-4992-A635-3C8227E27A27 Q35852856-4A04B02A-ECCF-4A27-98DE-9DEDD623E676 Q36388443-14906805-60F5-4AAF-8582-5C09091DFEA4 Q36547077-65F739CE-42B0-4B52-A47E-F0FCDE039A00 Q36994792-E1340E79-FD34-4BFC-812B-062C0ED6C2CB Q37011814-E8645B45-3F67-4478-A23D-FAFF38FC85C2 Q37255857-1575BAE2-BEF2-406F-B4C4-21D2B9A82A0F Q37270688-E9A7E290-5A6D-4F81-9E3C-F785EAE4CC21 Q37744944-21B26E92-0C8D-49E4-B444-F76C62D6301B Q37843988-96E51854-0F62-4D3F-8E0A-079430B4FDA9 Q37909103-D248C236-CAA7-4274-97BF-ECA45C73B707 Q37969122-639F74E3-D6EC-477E-AFF8-82B1F2912D4B Q38879949-13A19C7B-78C3-434E-A9B7-95F282FA56BD Q39309260-1D985686-91C0-4B95-9E3E-9CB2255F1149 Q39390772-DA21B216-9E3C-4DE0-A5F4-5FB4924CFAB0 Q42361148-19F767DA-4BBF-4CCD-A934-338FB09A7B82 Q42529820-4D569719-0464-46A9-BD6E-6E41EB736786 Q42650380-71CB28BB-53AE-4918-B0CC-16E4B7BF0408 Q46261257-DE426FE6-515B-471C-9ABC-C7E7F133692F Q46977539-AD1D3489-B81E-48E5-A067-9F8799DB6B55 Q47350887-9D857667-8C07-478B-9260-31A522034DEF Q55356191-2AAFD6D6-9484-48A6-B319-777A8D506C30 Q58744776-C85C617F-79A6-456F-A0EC-1C0243F07492

P2860

SUMOylation of tissue transglutaminase as link between oxidative stress and inflammation.

http://www.wikidata.org/entity/Q39821994

description

2009 nî lūn-bûn

@nan

2009年の論文

@ja

2009年学术文章

@wuu

2009年学术文章

@zh-cn

2009年学术文章

@zh-hans

2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

@yue

2009年學術文章

@zh

2009年學術文章

@zh-hant

name

SUMOylation of tissue transglutaminase as link between oxidative stress and inflammation.

@en

SUMOylation of tissue transglutaminase as link between oxidative stress and inflammation.

@nl

type

label

SUMOylation of tissue transglutaminase as link between oxidative stress and inflammation.

@en

SUMOylation of tissue transglutaminase as link between oxidative stress and inflammation.

@nl

prefLabel

SUMOylation of tissue transglutaminase as link between oxidative stress and inflammation.

@en

SUMOylation of tissue transglutaminase as link between oxidative stress and inflammation.

@nl

P1433

Q39821994-AAB924AB-6357-4EF5-87F4-49AC27FA661E

P1476

Q39821994-E9EDE127-1F0E-4B6B-8D80-45BA6F0087B6

P2093

Q39821994-00828722-2E81-4B05-8775-DC8E3BD14302

Q39821994-6109431F-9B76-463E-9E80-5A2EB22E0B52

Q39821994-76645F5A-1B45-497F-84EE-BF4F6EBE6A43

Q39821994-8F8AC950-CF42-4052-8D1F-88087B7881FC

Q39821994-91C15680-5C29-4FAB-928F-9393A23AA418

Q39821994-C1663A91-F062-4DF5-978F-6F12413662DC

Q39821994-E6002016-50A3-4072-8370-03AC6C8DC876

Q39821994-F0804096-2434-46C1-9B80-532C18F6C3FB

P304

Q39821994-FC874CB6-BA2A-4442-A398-7677001B83FA

P31

Q39821994-819D578A-3521-4700-8315-B6746478EB71

P356

Q39821994-78BE8073-7A35-48DC-96FE-B9888FD1A986

P407

Q39821994-679E2926-EDC8-464C-8ADC-9BAE7A9A9E1F

P433

Q39821994-02FA8E12-688E-4646-A54F-1FE9EC18825E

P478

Q39821994-56487FDD-3740-45F0-A56E-243F542E18C7

P50

Q39821994-8E5B6830-05FF-45D6-B9DA-0F025764716C

Q39821994-980750D8-AE35-468B-A1D7-9988824C7C75

Q39821994-E9174DD7-9BBC-4A58-9D57-4B0F355E5E40

P577

Q39821994-4285098D-6B4C-4C6D-AB39-F67FA6A086D3

P5875

Q39821994-A509EE2E-64C5-4D99-BD24-4E92C05344B4

P698

Q39821994-6C380D9B-1321-42EC-94B3-6C45550BD40F

P921

Q39821994-41C454BA-E85C-4F6D-BBA1-221CA56818E7

P356

JIMMUNOL.0900993

P1433

Journal of Immunology

P1476

SUMOylation of tissue transglutaminase as link between oxidative stress and inflammation

@en

P2093

Alessandro Luciani

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

Ida Giardino

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

Luigi Maiuri

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

Maria D'Apolito

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

Sonia Quaratino

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

Teresinha Leal

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

Valeria Rachela Villella

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

Valeria Raia

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

P304

2775-2784

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

P31

scholarly article

P356

10.4049/JIMMUNOL.0900993

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

P407

P433

4

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

P478

183

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

P50

Angela Vasaturo

M Pettoello-Mantovani

P577

2009-07-22T00:00:00Z

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

P5875

26689099

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

P698

19625650

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

P921