Saccharomyces cerevisiae expresses three phospholipid hydroperoxide glutathione peroxidases.
about
Stress induction and mitochondrial localization of Oxr1 proteins in yeast and humansMicrobial 2-Cys Peroxiredoxins: Insights into Their Complex Physiological RolesThe yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms.Role of yeast glutaredoxins as glutathione S-transferases.Peroxiredoxin Tsa1 is the key peroxidase suppressing genome instability and protecting against cell death in Saccharomyces cerevisiaeThe thioredoxin system protects ribosomes against stress-induced aggregationThe yeast homolog of heme oxygenase-1 affords cellular antioxidant protection via the transcriptional regulation of known antioxidant genesCytosolic thioredoxin peroxidase I and II are important defenses of yeast against organic hydroperoxide insult: catalases and peroxiredoxins cooperate in the decomposition of H2O2 by yeast.Cross-stress resistance in Saccharomyces cerevisiae yeast--new insight into an old phenomenonOxidative folding in the mitochondrial intermembrane space: A regulated process important for cell physiology and diseaseThe Incomplete Glutathione Puzzle: Just Guessing at Numbers and Figures?Phylogenetic diversity of stress signalling pathways in fungi.Multiple means to the same end: the genetic basis of acquired stress resistance in yeast.Thiol peroxidase deficiency leads to increased mutational load and decreased fitness in Saccharomyces cerevisiae.Thiol peroxidases mediate specific genome-wide regulation of gene expression in response to hydrogen peroxide.Genome-wide amplifications caused by chromosomal rearrangements play a major role in the adaptive evolution of natural yeast.Regulation of the transcriptional response to oxidative stress in fungi: similarities and differences.Function of glutathione peroxidases in legume root nodulesRegulation of redox homeostasis in the yeast Saccharomyces cerevisiae.The response to heat shock and oxidative stress in Saccharomyces cerevisiaeAcclimation to singlet oxygen stress in Chlamydomonas reinhardtii.Oxidative stress and programmed cell death in yeast.Genome-wide expression and location analyses of the Candida albicans Tac1p regulon.Purification, crystallization and preliminary X-ray analysis of glutathione peroxidase Gpx3 from Saccharomyces cerevisiae.Involvement of GDH3-encoded NADP+-dependent glutamate dehydrogenase in yeast cell resistance to stress-induced apoptosis in stationary phase cellsSeleno-independent glutathione peroxidases. More than simple antioxidant scavengers.The peroxiredoxin and glutathione peroxidase families in Chlamydomonas reinhardtiiThriving within the host: Candida spp. interactions with phagocytic cells.Cellular redox homeostasis, reactive oxygen species and replicative ageing in Saccharomyces cerevisiae.The impact of thiol peroxidases on redox regulation.High resistance to oxidative stress in the fungal pathogen Candida glabrata is mediated by a single catalase, Cta1p, and is controlled by the transcription factors Yap1p, Skn7p, Msn2p, and Msn4p.Global translational responses to oxidative stress impact upon multiple levels of protein synthesis.Chemical Composition and Antioxidant Properties of Juniper Berry (Juniperus communis L.) Essential Oil. Action of the Essential Oil on the Antioxidant Protection of Saccharomyces cerevisiae Model Organism.Roles of vacuolar H+-ATPase in the oxidative stress response of Candida glabrata.YBP1 and its homologue YBP2/YBH1 influence oxidative-stress tolerance by nonidentical mechanisms in Saccharomyces cerevisiae.Roles of thioredoxin reductase during the aerobic life of Lactococcus lactis.The importance of Arabidopsis glutathione peroxidase 8 for protecting Arabidopsis plant and E. coli cells against oxidative stress.Characterizing roles for the glutathione reductase, thioredoxin reductase and thioredoxin peroxidase-encoding genes of Magnaporthe oryzae during rice blast disease.Absolute transcript levels of thioredoxin- and glutathione-dependent redox systems in Saccharomyces cerevisiae: response to stress and modulation with growth.The role of cytoplasmic catalase in dehydration tolerance of Saccharomyces cerevisiae.
P2860
4dc5653f7c1d8d4f48cc8613918bbe2aa9aed4b9550469ee1068dcdd467d73f18abc8678e1d23c8d714dbc4628dcb3da4148536acc57075e99e22f0b7c7f0e6e402ff4cdababe5bc17742cd88465ca268c107572cfb36d0d5b2b4339b3ecc467d6dcd73fa6bc67a876aafd7f0f8db0871544e8d7730b9997be95901951f89a1b6a2ce2c9e20cbb9f1fc65b55deffe9012b05a2ee8c2f6f2a89dc58d4838a4b3deb97c021ada350de724aae425fe31a8fbbc53324f1fa986fb2c5d9f58d4a0c6aa576b3c734ab0ec9
P248
Q24602344-2E852006-27D4-478B-818E-E68DE79CE0B9Q26774297-E31D050D-B842-4C5E-9EEE-76275F63C9F4Q27931000-5AE0824B-DAB9-4A2F-AAF3-2119EFFB1B51Q27931430-3693336A-E8CE-4991-AD6B-66D15538390FQ27931969-D83F334A-1102-4CCA-A63F-E50B4F6FA840Q27935088-8FDE0AF2-30A4-4406-BD27-0B051CE0CA3BQ27935661-43E24BF8-F4F3-4F47-BC66-D4CBE5A7D3D3Q27937410-5A824ADF-69E8-4636-854A-6DD051214637Q28073348-37A9E637-21B8-43F9-AE4A-84E865E9D0B3Q28076268-C0889FC1-D159-48D1-AEB9-5D73CC05EA7FQ33365461-40127CBE-FAC9-4D18-9BA1-FD789E0BB2F8Q33411072-621591AC-91F4-46BE-ACE7-933D7AEF7185Q34079179-6DBC7C44-AB53-429D-A369-60A8688721A5Q34471700-0589F4FC-E99A-46EF-83A9-8926F1825168Q34582837-1AA70DD1-D5A9-4BF6-9D3D-FEF626177AD8Q34619448-BDD53C59-76DC-4186-B91A-B096157E4596Q35149524-81A4AC25-A171-491E-90F0-054E26285B51Q35580295-ED95C667-F072-4272-A753-56B1E63D9CA8Q35699713-1780BB74-4CD5-43E1-B5F2-55C92FB339C9Q35863026-E621BC14-4FBD-47D3-A651-5B502287E955Q35948274-8A14C960-46AB-4C61-A25B-9CEEEC355139Q36049724-264342B3-0BDA-470A-AAA9-C1DBCAAB7A25Q36314156-1C07E2B1-639C-4BF1-98CB-25E8BB6610FEQ36459721-9FDFC705-BAC9-4D18-A59B-6E98764E4A2DQ36492783-CE416A00-A7C1-43C9-AFA6-D5AD8C4D4F89Q36785888-E7A92A87-91FB-4CE4-909B-BD12E8283640Q37168901-0D4A0B4C-8221-4BD1-A784-3EDF589535A8Q38077110-C279E3DF-F4E0-4B47-81BE-1DF12A23E011Q38155951-BC95C729-EF0A-4A7E-888D-2D8C55092A03Q38570138-61353383-930D-4377-A8A9-0E323A09BE40Q38608198-D4954F6C-CFDA-4D59-9429-68F204DF9064Q39348564-FC9C5F5D-5FA6-40B5-A4BC-526957E21847Q40089297-7A674224-0CAA-4CB3-B3E3-7ECA8DE247D0Q40628108-C6525B7E-3FFC-4E6D-8129-FC7CCC4001B1Q40763026-9DA42D83-A8EE-4DBE-A881-8C92EDAB85A3Q40875415-77A08F81-5037-4BB8-B37C-4890F1314A4BQ41155494-5CA7FC24-AEC2-4BD5-9F10-FC3CEA2E9A5AQ41770277-4587A3BC-DDA9-439B-9841-B038BF0E171DQ41818181-63F59298-0D01-43D8-A36D-51F5FE370B11Q42123253-89AB5714-CA40-4078-8A40-403F83BE91D8
P2860
Saccharomyces cerevisiae expresses three phospholipid hydroperoxide glutathione peroxidases.
description
2001 nî lūn-bûn
@nan
2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Saccharomyces cerevisiae expre ...... oxide glutathione peroxidases.
@ast
Saccharomyces cerevisiae expre ...... oxide glutathione peroxidases.
@en
Saccharomyces cerevisiae expre ...... oxide glutathione peroxidases.
@nl
type
label
Saccharomyces cerevisiae expre ...... oxide glutathione peroxidases.
@ast
Saccharomyces cerevisiae expre ...... oxide glutathione peroxidases.
@en
Saccharomyces cerevisiae expre ...... oxide glutathione peroxidases.
@nl
prefLabel
Saccharomyces cerevisiae expre ...... oxide glutathione peroxidases.
@ast
Saccharomyces cerevisiae expre ...... oxide glutathione peroxidases.
@en
Saccharomyces cerevisiae expre ...... oxide glutathione peroxidases.
@nl
P2860
P356
P1476
Saccharomyces cerevisiae expre ...... oxide glutathione peroxidases.
@en
P2093
P2860
P304
P356
10.1074/JBC.M105672200
P407
P577
2001-09-07T00:00:00Z