SwePub
Sök i SwePub databas

  Utökad sökning

Träfflista för sökning "L773:1523 0864 OR L773:1557 7716 srt2:(2005-2009)"

Sökning: L773:1523 0864 OR L773:1557 7716 > (2005-2009)

  • Resultat 11-20 av 20
Sortera/gruppera träfflistan
   
NumreringReferensOmslagsbildHitta
11.
  •  
12.
  •  
13.
  •  
14.
  •  
15.
  •  
16.
  •  
17.
  • Rouhier, Nicolas, et al. (författare)
  • Identification of plant glutaredoxin targets
  • 2005
  • Ingår i: Antioxidants and Redox Signaling. - Larchmont, NY : Mary Ann Liebert. - 1523-0864 .- 1557-7716. ; 7:7-8, s. 919-929
  • Tidskriftsartikel (refereegranskat)abstract
    • Glutaredoxins (Grxs) are small ubiquitous proteins of the thioredoxin (Trx) family, which catalyze dithiol–disulfide exchange reactions or reduce protein-mixed glutathione disulfides. In plants, several Trx-interacting proteins have been isolated from different compartments, whereas very few Grx-interacting proteins are known. We describe here the determination of Grx target proteins using a mutated poplar Grx, various tissular and subcellular plant extracts, and liquid chromatography coupled to tandem mass spectrometry detection. We have identified 94 putative targets, involved in many processes, including oxidative stress response [peroxiredoxins (Prxs), ascorbate peroxidase, catalase], nitrogen, sulfur, and carbon metabolisms (methionine synthase, alanine aminotransferase, phosphoglycerate kinase), translation (elongation factors E and Tu), or protein folding (heat shock protein 70). Some of these proteins were previously found to interact with Trx or to be glutathiolated in other organisms, but others could be more specific partners of Grx. To substantiate further these data, Grx was shown to support catalysis of the stroma β-type carbonic anhydrase and Prx IIF of Arabidopsis thaliana, but not of poplar 2-Cys Prx. Overall, these data suggest that the interaction could occur randomly either with exposed cysteinyl disulfide bonds formed within or between target proteins or with mixed disulfides between a protein thiol and glutathione.
  •  
18.
  • Terman, Alexei, 1957-, et al. (författare)
  • Oxidative stress, accumulation of biological 'garbage', and aging
  • 2006
  • Ingår i: Antioxidants and Redox Signaling. - : Mary Ann Liebert Inc. - 1523-0864 .- 1557-7716. ; 8:1-2, s. 197-204
  • Tidskriftsartikel (refereegranskat)abstract
    • Normal metabolism is associated with unavoidable mild oxidative stress resulting in biomolecular damage that cannot be totally repaired or removed by cellular degradative systems, including lysosomes, proteasomes, and cytosolic and mitochondrial proteases. Consequently, irreversibly damaged and functionally defective structures (biological 'garbage') accumulate within long-lived postmitotic cells, such as cardiac myocytes and neurons, leading to progressive loss of adaptability and increased probability of death and characterizing a process called aging, or senescence. Intralysosomal 'garbage' is represented by lipofuscin (age pigment), an undegradable autophagocytosed material, while extralysosomal 'garbage' involves oxidatively modified cytosolic proteins, altered biomembranes, defective mitochondria and other organelles. In aged postmitotic cells, heavily lipofuscin-loaded lysosomes perform poorly, resulting in the enhanced accumulation of defective mitochondria, which in turn produce more reactive oxygen species causing additional damage (the mitochondrial- lysosomal axis theory). Potential anti-aging strategies may involve not only overall reduction of oxidative stress, but also the use of intralysosomal iron chelators hampering Fenton-type chemistry as well as the stimulation of cellular degradative systems. © Mary Ann Liebert, Inc.
  •  
19.
  •  
20.
  •  
Skapa referenser, mejla, bekava och länka
  • Resultat 11-20 av 20

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Stäng

Kopiera och spara länken för att återkomma till aktuell vy