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. Author manuscript; available in PMC: 2012 Feb 15.
Published in final edited form as: Free Radic Biol Med. 2010 Nov 25;50(4):487–494. doi: 10.1016/j.freeradbiomed.2010.11.021

Table 1.

Functional Categorization of Oxidatively Proteins Identified in AD.

Protein Function Carbonylationa HNE-boundb Nitrationc
Energy Dysfunction Creatine kinase, α -enolase, triose phosphate isomerase, phosphoglyerate mutase 1 α-enolase, α-enolase, γ-enolase, lactate dehydrogenase, glyceraldehydes-3-phosphate dehydrogenase, triose phosphate isomerase
Mitochondrial dysfunction ATP synthase Manganese superoxide dismutase ATP synthase, Voltage dependent anion channel protein 1
Antioxidant defense/detoxification dysfunction peroxiredoxin VI, Manganese superoxide dismutase
Cell cycle; Aβ production; Tau phosphorylation Pin 1
Lipid abnormalities and cholinergic dysfunction Neuropolypeptide h3
Neuritic abnormalities and structural dysfunction DRP2, β-actin, gamma-SNAP DRP2, Alpha tubulin DRP2, β-actin
Excitotoxicity Excitatory amino acid transporter, Glutamine synthetase Glutamine synthetase
pH dysfunction Carbonic anhydrase II Carbonic anhydrase II
Protein degradation UCHL 1, heat shock protein
a

For Carbonylated proteins identified in AD please see reference [36–37, 42].

b

For these HNE-bound proteins identified in AD please see reference [35].

c

For these nitrated proteins identified in AD please see reference [10, 17].

d

For these glutathionylated proteins identified in AD please see reference [44].

Protein in bold is a common targets of the different oxidative modifications examined.