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Titlebook: DJ-1/PARK7 Protein; Parkinson’s Disease, Hiroyoshi Ariga,Sanae‘M. M. Iguchi-Ariga Book 2017 Springer Nature Singapore Pte Ltd. 2017 DJ-1.Pa

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Protein Repair from Glycation by Glyoxals by the DJ-1 Family Maillard Deglycases, their major glycating agents. Glycation is a non-enzymatic covalent reaction discovered by Louis Camille Maillard in 1912, between reactive carbonyls (reducing sugars and glyoxals) and amino acids (cysteine, arginine and lysine), which inactivates proteins. By degrading Maillard adducts formed betw
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,DJ-1 as a Biomarker of Parkinson’s Disease,s been identified as a causative gene of a familial form of Parkinson’s disease, ., and plays a significant role in antioxidative defense, protecting cells from oxidative stress. A cysteine residue of DJ-1 at position 106 (Cys-106) is preferentially oxidized under oxidative stress. This reactive Cys
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DJ-1 as a Therapeutic Target Against Cancer,egulation, inflammatory and fibrogenic niche formation, and glycation damage prevention. Although a disease-associated genetic study within the past decade has demonstrated that the mutation of DJ-1 is associated with autosomal early-onset Parkinson’s disease, increasing evidence suggests that DJ-1
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P. Nisha,Manuel Thomas,T. K. Neelima thioredoxin and glutathione pathways, which in turn mediate an antioxidant protective function. Crosstalk between DJ-1 and both the thioredoxin and glutathione systems has also been identified. Thioredoxin reduces a cysteine residue on DJ-1 to modulate its activity, while glutaredoxin1 de-glutathio
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Aquatic Lectins: An Overview (A Paradigm). It also modulates autophagy through the ERK, Akt, or the JNK/Beclin1 pathways. In addition, DJ-1 regulates the transcription of genes essential for male reproductive function, such as spermatogenesis, by relaying nuclear receptor androgen receptor (AR) signaling. In this chapter, we summarize the
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