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. 2016 Feb;11(2):232-3.
doi: 10.4103/1673-5374.177722.

ERp57 in neurodegeneration and regeneration

Affiliations

ERp57 in neurodegeneration and regeneration

Leslie Bargsted et al. Neural Regen Res. 2016 Feb.
No abstract available

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Figures

Figure 1
Figure 1
ERp57 and protein disulfide isomerase (PDI) in neurodegeneration. (A) Primary structure of ERp57 and PDIA1 (indicated as PDI) indicating the catalytic domains (a and a’ in yellow and orange, respectively) and non catalytic domains (b and b’ in blue and green, respectively). (B) Function of ERp57 and PDIA1 in disulfide bond formation. Both proteins participate in the formation (reduction), oxidation and isomerization (rearrangement) of disulfide bonds of folded proteins at the endoplasmic reticulum (ER). (C) Possible involvement of PDIs in neurodegeneration. Alterations and upregulation of ERp57 and PDIA1 is detected in PMDs. PDIs can be inactivated in oxidative conditions through S-nitrosylation in PDIA1, which may trigger chronic ER stress. Upregulation of PDIs may decrease the accumulation of toxic misfolded proteins, it could promote the synthesis of synaptic proteins (like SV2), decrease ER stress levels and improve axonal regeneration.

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