Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity. - Test2 - elhamkhani - TriplyDB

Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity.

Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity.

http://www.wikidata.org/entity/Q30991292

about

1-Cys peroxiredoxin overexpression protects cells against phospholipid peroxidation-mediated membrane damage Central functions of the lumenal and peripheral thylakoid proteome of Arabidopsis determined by experimentation and genome-wide prediction Fish Peroxiredoxins and Their Role in Immunity Peroxiredoxin-null yeast cells are hypersensitive to oxidative stress and are genomically unstable.Mitochondrial and cytosolic expression of human peroxiredoxin 5 in Saccharomyces cerevisiae protect yeast cells from oxidative stress induced by paraquat Glutaredoxin-dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanism Mice with targeted mutation of peroxiredoxin 6 develop normally but are susceptible to oxidative stress Structural and biochemical characterization of a mitochondrial peroxiredoxin from Plasmodium falciparum Kinetics and redox-sensitive oligomerisation reveal negative subunit cooperativity in tryparedoxin peroxidase of Trypanosoma brucei brucei.Proteomic modeling for HIV-1 infected microglia-astrocyte crosstalk.Effects of the cyclophilin-type peptidylprolyl cis-trans isomerase from Pyropia yezoensis against hydrogen peroxide-induced oxidative stress in HepG2 cells.Comprehensive survey of proteins targeted by chloroplast thioredoxin.The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux.Comparative molecular modeling study of Arabidopsis NADPH-dependent thioredoxin reductase and its hybrid protein.Decarbonylated cyclophilin A Cpr1 protein protects Saccharomyces cerevisiae KNU5377Y when exposed to stress induced by menadione.Profilin-1 overexpression in MDA-MB-231 breast cancer cells is associated with alterations in proteomics biomarkers of cell proliferation, survival, and motility as revealed by global proteomics analyses.Of mice and men: comparative proteomics of bronchoalveolar fluid.Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein.Peroxiredoxins in plants and cyanobacteria.Cloning, expression and antioxidant activity of a thioredoxin peroxidase from Branchiostoma belcheri tsingtaunese.Peroxiredoxin 6 in human brain: molecular forms, cellular distribution and association with Alzheimer's disease pathology Reactive oxygen species and antioxidant mechanisms in human tissues and their relation to malignancies.The peroxiredoxin and glutathione peroxidase families in Chlamydomonas reinhardtii Dietary vitamin D deficiency in rats from middle to old age leads to elevated tyrosine nitration and proteomics changes in levels of key proteins in brain: implications for low vitamin D-dependent age-related cognitive decline.The consequences of mitochondrial amyloid beta-peptide in Alzheimer's disease.Peroxiredoxin 6: a bifunctional enzyme with glutathione peroxidase and phospholipase A₂ activities.Novel roles of peroxiredoxins in inflammation, cancer and innate immunity.The functional role of peroxiredoxin 3 in reactive oxygen species, apoptosis, and chemoresistance of cancer cells.Mitochondrial Thioredoxin System as a Modulator of Cyclophilin D Redox State.The Relevance of Mammalian Peroxiredoxins to the Gametogenesis, Embryogenesis, and Pregnancy Outcomes.Peroxiredoxin 6 in the repair of peroxidized cell membranes and cell signaling.Genome wide analysis of Cyclophilin gene family from rice and Arabidopsis and its comparison with yeast.Characterization of a bacterioferritin comigratory protein family 1-Cys peroxiredoxin from Candidatus Liberibacter asiaticus.Phorbol ester-dependent activation of peroxiredoxin I gene expression via a protein kinase C, Ras, p38 mitogen-activated protein kinase signaling pathway.The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex.Role of the cysteine residues in Arabidopsis thaliana cyclophilin CYP20-3 in peptidyl-prolyl cis-trans isomerase and redox-related functions.Cooperation of yeast peroxiredoxins Tsa1p and Tsa2p in the cellular defense against oxidative and nitrosative stress.Regulation of 1-cys peroxiredoxin expression in lung epithelial cells.Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis.Organic hydroperoxide resistance gene encodes a thiol-dependent peroxidase.

P2860

Q24535582-CA701B22-095E-46BD-A0C8-093310A5F470 Q24551036-F0278696-6A3E-49F1-A198-A7C81A9C1F08 Q26774985-3D28FB58-3E8C-4DB0-BEC7-0DBB4B4102E9 Q27939536-7675E09F-0D57-446D-BA50-33E380CFBC96 Q28208184-BF88AF09-1A82-4EBC-8624-E45A2BF94FC5 Q28217838-35CF24A5-B6B4-4835-9146-73ACA66C0D19 Q28587822-A2ACAF7A-74FD-4530-8AF2-39B958A7F178 Q30042256-816F2D05-1501-4CAD-8CEC-4256E47D4711 Q30932104-0356331F-15AE-4381-B29C-39D0836E4226 Q33346280-033FA6A4-3972-4D08-ABD3-80896F516297 Q33702398-73FB4430-DF2E-4347-9CF6-258E75B88CF0 Q33944400-77C1B3CB-5097-426E-83E3-73938394C85C Q34026318-F2312B1F-8012-45CE-A775-94B894C980DF Q34431019-4AC8AF81-2602-4D17-BC4D-3500CB03F941 Q34505918-F04C67CA-3FB9-4CA3-BD12-6C8BA0E7D55E Q34617881-223633FA-A3FF-49FF-A07E-2B2D72007679 Q34626421-24871393-E8FB-47A5-BD37-F9FBD671B739 Q34790896-633313A1-FDC3-4B82-84EC-37E70E5F5A4C Q35101766-4FFF67E0-B942-4402-A5F9-B4F2C147B00A Q36338080-F633D391-C9B6-47CE-8728-6087CB197815 Q36660813-5A7CE4BE-0719-46E3-B29A-82185BFC09EA Q36734074-6524BCF3-86E5-47AF-BA6B-AED8FB547467 Q37168901-55A566F9-CF6A-425F-A635-6F5B03E2EC0F Q37384973-F8F227D0-C7F1-4F40-BFD3-F50E01D78256 Q37696521-F87F28B7-AC7D-4C43-9BAB-547D3BD8CC1E Q37797498-4DD32D49-3D36-479F-9169-A0517BDFC6B9 Q37997003-7144B864-4284-47F6-873C-141223462FE0 Q38421684-9EA3596B-7EB0-4323-9498-8B8210D538D3 Q38786513-ECB18EC3-5B99-48B8-A8E1-C9B222B00AA1 Q38953521-7AA0149D-0435-4E56-9B98-3C983CA1D2FB Q39033606-B2E85441-2EEA-4E24-A757-986356A29AE0 Q39535256-ADB4B253-2D6C-4F4D-9314-4C9E1E3DEFE6 Q40420302-AA9C6AB2-E2E5-4A67-9031-83BE9813EA46 Q40636850-FF14163F-1EA4-4210-B737-AC20F76D4C4C Q40659678-04841847-022F-4693-9867-A236FED7B43B Q41084059-A4718C83-B4D9-40D4-892B-672CF8354F37 Q42514053-FE2B5571-9A24-4B75-BED9-59F0455374C8 Q44084970-0588D143-543B-41A5-981D-7C9E65365B5E Q44279349-F313CBBA-FF42-469D-982D-9F5BF61912C6 Q44286549-2F002E49-619A-4491-BB13-30137ADC467C

P2860

Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity.

http://www.wikidata.org/entity/Q30991292

description

2001 nî lūn-bûn

@nan

2001 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2001年の論文

@ja

2001年学术文章

@wuu

2001年学术文章

@zh-cn

2001年学术文章

@zh-hans

2001年学术文章

@zh-my

2001年学术文章

@zh-sg

2001年學術文章

@yue

name

Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity.

@ast

Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity.

@en

type

label

Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity.

@ast

Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity.

@en

prefLabel

Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity.

@ast

Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity.

@en

P1433

Q30991292-4A0B9CAB-662C-46EE-8FBB-D268646B0725

P1476

Q30991292-7CE72DF7-C40E-4419-8606-42451C3E3E68

P2093

Q30991292-2A918C6B-5721-4FE8-A238-56DBC2D85F7D

Q30991292-2AEF87E0-ACF8-4AD3-A1D1-7B2C7781D13C

Q30991292-48BB799E-BC30-4D22-98BD-E03C6B3C7DDB

Q30991292-5B7B433B-6F64-413E-9B5B-F3296959C299

Q30991292-7427B883-A074-41F8-94C1-44CD408ED18E

Q30991292-952E10E8-370C-4CB9-8843-5ED934159CBB

Q30991292-CDB472AA-E901-4027-9755-73E4A6614D84

P2860

Q30991292-00737C94-8E71-4CB7-A453-DDDB8B1DBA62

Q30991292-00A118F3-5EF7-4433-8C60-B82AE6E8CC2D

Q30991292-078990F2-2D5B-4EB8-835B-D5606E65F1AE

Q30991292-0A87EE45-6E3B-49C1-AB68-D20A45D431D5

Q30991292-1085ED93-6906-400A-BBB5-440FCAB53AA6

Q30991292-196AD27A-A622-406A-9732-B9B96EDB1796

Q30991292-21FB15BB-0AA4-40EB-886B-CCB4B913BD09

Q30991292-39611DEB-98DA-4FFE-812C-5CA2744454AD

Q30991292-4128C17F-5F2A-4EC8-8B62-318956241970

Q30991292-412F111A-007E-48B0-A084-C4B4621EA99E

P304

Q30991292-8B17543C-C415-434B-A7B5-A9F4E969F875

P31

Q30991292-09FF1853-A81A-4BCE-8BEE-1228E5296719

P356

Q30991292-6D56F98B-9084-4B48-A655-716B242E3FE5

P407

Q30991292-8331FD4C-41E3-4130-B1B2-2EF2E8E84B4C

P433

Q30991292-52341A29-9E0A-4D4C-B8DF-69EFC1A54BE4

P478

Q30991292-9ACA85A5-AE9F-4B18-8DBE-1CE40777A57C

P577

Q30991292-74A84B96-B6B1-41DB-BF8E-3316A3E7EA88

P5875

Q30991292-890F8D07-8709-4839-B0D0-1C8BCDE044B1

P698

Q30991292-06FB62BC-F2EE-4E7B-9749-94391EBA304B

P356

P1433

Journal of Biological Chemistry

P1476

Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity.

@en

P2093

Chae HZ

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

Hwang YS

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

Kim HJ

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

Kim K

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

Kim YJ

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

Kwon KS

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

Lee SP

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

P2860

Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate

1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities

Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation

Characterization of a mammalian peroxiredoxin that contains one conserved cysteine

Cloning, expression, and purification of human cyclophilin in Escherichia coli and assessment of the catalytic role of cysteines by site-directed mutagenesis

Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes

The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity

The mutant Escherichia coli F112W cyclophilin binds cyclosporin A in nearly identical conformation as human cyclophilin

Purification and characterization of a second type thioredoxin peroxidase (type II TPx) from Saccharomyces cerevisiae.

Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis

P304

29826-29832

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

P31

scholarly article

P356

10.1074/JBC.M101822200

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

P407

P433

32

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

P478

276

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

P577

2001-06-04T00:00:00Z

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

P5875

232315636

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

P698

11390385

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