Biliverdin reductase: new features of an old enzyme and its potential therapeutic significance - Wikidata - wikimedia - TriplyDB

Biliverdin reductase: new features of an old enzyme and its potential therapeutic significance

Biliverdin reductase: new features of an old enzyme and its potential therapeutic significance

http://www.wikidata.org/entity/Q28268811

about

Rethinking the immune properties of bilirubin in viral hepatitis: from bench to bedside Organic Nitrate Therapy, Nitrate Tolerance, and Nitrate-Induced Endothelial Dysfunction: Emphasis on Redox Biology and Oxidative Stress Probing mechanisms of axonopathy. Part I: Protein targets of 1,2-diacetylbenzene, the neurotoxic metabolite of aromatic solvent 1,2-diethylbenzene Abnormal modulation of cell protective systems in response to ischemic/reperfusion injury is important in the development of mouse sickle cell hepatopathy.Heme oxygenase in the regulation of vascular biology: from molecular mechanisms to therapeutic opportunities.The coordinated increased expression of biliverdin reductase and heme oxygenase-2 promotes cardiomyocyte survival: a reductase-based peptide counters β-adrenergic receptor ligand-mediated cardiac dysfunction.Scalable production of biliverdin IXα by Escherichia coli.Biliverdin reductase A in the prevention of cellular senescence against oxidative stress.Expression of Biliverdin Reductase A in peripheral blood leukocytes is associated with treatment response in HCV-infected patients Pilot study on the effect of grounding on delayed-onset muscle soreness.The effects of grounding (earthing) on inflammation, the immune response, wound healing, and prevention and treatment of chronic inflammatory and autoimmune diseases Formation of ternary complex of human biliverdin reductase-protein kinase Cδ-ERK2 protein is essential for ERK2-mediated activation of Elk1 protein, nuclear factor-κB, and inducible nitric-oxidase synthase (iNOS).Proteomic profiling of posterior longitudinal ligament of cervical spine.Direct Antioxidant Properties of Bilirubin and Biliverdin. Is there a Role for Biliverdin Reductase?Effect of cerebral amyloid angiopathy on brain iron, copper, and zinc in Alzheimer's disease Mesobiliverdin IXα Enhances Rat Pancreatic Islet Yield and Function.Label-free quantitative protein profiling of vastus lateralis muscle during human aging.Role of heme oxygenase in inflammation, insulin-signalling, diabetes and obesity.Characterization of the human biliverdin reductase gene structure and regulatory elements: promoter activity is enhanced by hypoxia and suppressed by TNF-alpha-activated NF-kappaB.Proteomic analysis of acetaminophen-induced hepatotoxicity and identification of heme oxygenase 1 as a potential plasma biomarker of liver injury.Bilirubin Is Inversely Associated With Cardiovascular Disease Among HIV-Positive and HIV-Negative Individuals in VACS (Veterans Aging Cohort Study).The association between total bilirubin and serum triglyceride in both sexes in Chinese

P2860

Q26771481-66F625ED-8EE7-4EE1-88A4-51E602C02691 Q26799354-E683A46E-B1F8-4184-BDB6-E6ACB29D1538 Q33337705-90D48654-3E65-4ABA-BCD2-932F8B79EE83 Q33695612-E00F406D-B21B-42F9-B5D0-943C96292BA9 Q34334879-72876A76-E719-4ABF-8007-A7B9239DABD2 Q34421837-C15F2340-BBD2-458B-900A-32E07EBDB5A7 Q34486712-A81D4FC4-EE1A-48DA-BC48-E0C319B077C9 Q34587100-CD973DE6-6BB0-4631-9737-B1D3BE4AB3BE Q34638990-F39C970F-10C3-4487-95E2-AB2938AC9F02 Q35049567-8B7C51D0-A868-4EF1-B88A-C5CAF24AFBA0 Q35229060-8A4E6513-AB79-4D46-A22C-05851EE591F6 Q35668827-354A1A90-CBFE-43DD-B651-93CEC9246722 Q35791478-55487A4C-CAB1-404C-B310-14B4A62778CD Q35835328-AB2A5AE0-F8B6-4778-AE7F-2B4B11D649BF Q35866579-810D5FBD-C670-4149-8D84-02B52A72359C Q36786559-EECBD9DC-4AED-41D0-8031-178567907576 Q37428846-FD952816-3ADC-4982-A6ED-AB7BC0832BCB Q37761303-46AB21C1-E9D3-452C-BD6F-A7D4E3F57949 Q39615979-D36D63D9-9074-4F40-B0CC-217015855040 Q47098758-001EC175-42E8-4556-800E-1089A6B22059 Q55499286-1D61545A-2C9B-4C26-A6E7-0F94C1171CD2 Q58747198-51427B46-1894-428F-970F-2CB338F2BE4D

P2860

Biliverdin reductase: new features of an old enzyme and its potential therapeutic significance

http://www.wikidata.org/entity/Q28268811

description

2008 nî lūn-bûn

@nan

2008 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Biliverdin reductase: new feat ...... ntial therapeutic significance

@ast

Biliverdin reductase: new feat ...... ntial therapeutic significance

@en

Biliverdin reductase: new feat ...... ntial therapeutic significance

@nl

type

label

Biliverdin reductase: new feat ...... ntial therapeutic significance

@ast

Biliverdin reductase: new feat ...... ntial therapeutic significance

@en

Biliverdin reductase: new feat ...... ntial therapeutic significance

@nl

prefLabel

Biliverdin reductase: new feat ...... ntial therapeutic significance

@ast

Biliverdin reductase: new feat ...... ntial therapeutic significance

@en

Biliverdin reductase: new feat ...... ntial therapeutic significance

@nl

P1433

Q28268811-395529C4-DE6F-4C2F-8CE6-D447ECC6BB6B

P1476

Q28268811-09EB3B09-C9E6-4C9B-8274-1B715BEFDBB3

P2093

Q28268811-2F629712-E760-4E8D-B92F-811F855501BD

Q28268811-35B989BE-9E79-4E54-A34B-6495D86D8E1F

Q28268811-D79B5914-AE2B-4DB0-B44A-42A68F4EFCF6

P2860

Q28268811-068C5BC3-0BB2-4F43-91C2-2F5B99ADA5D4

Q28268811-13FBE4DC-0FB1-41C2-8EC8-3D0FD594428F

Q28268811-160D2251-A032-41A9-B62A-100DCB0ACB1E

Q28268811-17596962-58BD-40B7-91FD-C19AEB1F5068

Q28268811-1D83401B-CF7F-43DD-B8F5-76838B4569B4

Q28268811-21261953-0BB5-4B90-AEFB-961445B36DB8

Q28268811-22F914C9-5F67-4F11-905D-B0B64CF39526

Q28268811-24B052ED-5801-4AED-8823-3A3F11CA770D

Q28268811-269D49F3-B93F-439A-A32A-8CB925D37A83

Q28268811-2D143335-0525-421E-8148-25AB6E499BCF

P304

Q28268811-5AB7C3DF-E811-4764-BD93-55637F4D862E

P31

Q28268811-3D582497-3243-4BA8-9647-D15FA63AF2D9

P407

Q28268811-4C347F51-6265-44A7-8BBE-C474A6F8BF6C

P433

Q28268811-F4851FA6-9516-45EA-8226-89BE8843CCE4

P478

Q28268811-61102B5F-C731-4B05-8A0B-659F60866FE8

P50

Q28268811-1A7FD0FD-EB22-47E2-A669-40184F911CF4

P577

Q28268811-6CFDD377-C8CE-4F9E-B409-520ACCE551A1

P698

Q28268811-B8829A70-40F0-4D91-BAAB-5EF6F198B796

P932

Q28268811-2E5F02BE-DAB7-4E44-A46E-14E541ADA317

P1433

Pharmacological Reports

P1476

Biliverdin reductase: new feat ...... ntial therapeutic significance

@en

P2093

Alicja Jozkowicz

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

Jozef Dulak

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

Urszula M Florczyk

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

P2860

Bifunctional role for VEGF-induced heme oxygenase-1 in vivo: induction of angiogenesis and inhibition of leukocytic infiltration

Biliverdin-IX alpha reductase and biliverdin-IX beta reductase from human liver. Purification and characterization

Biliverdin reductase: a major physiologic cytoprotectant

Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex

The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins

Human biliverdin reductase is a leucine zipper-like DNA-binding protein and functions in transcriptional activation of heme oxygenase-1 by oxidative stress

Biliverdin reductase, a novel regulator for induction of activating transcription factor-2 and heme oxygenase-1

Ferritin: a cytoprotective antioxidant strategem of endothelium

Scissors-grip model for DNA recognition by a family of leucine zipper proteins

Human biliverdin IXalpha reductase is a zinc-metalloprotein. Characterization of purified and Escherichia coli expressed enzymes

P304

38-48

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

P31

scholarly article

P407

P433

1

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

P478

60

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

P50

Alicja Józkowicz

P577

2008-01-01T00:00:00Z

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

P698

18276984

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

P932

5536200

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