Amyloid fibril proteomics of AD brains reveals modifiers of aggregation and toxicity

Table 2 Newly discovered proteins found associated with purified Aβ fibrils

Protein name	Gene / Protein	Source
Acetyl-CoA acetyltransferase, mitochondrial	ACAT1	T, D, N
ADP-ribosylation factor 5	ARF3, ARF5	H, T, D
Cytochrome c oxidase subunit 6A1, mitochondrial	COX6A1	M, D, F
Nidogen-1	NID1	M, H, D
Aspartate aminotransferase, mitochondrial	GOT2	H, T, D
Basement membrane-specific heparan sulfate proteoglycan core protein	HSPG2	M, H, D
Serine peptidase	HTRA1	M, H, D
Isocitrate dehydrogenase [NAD] subunit, mitochondrial	IDH3B	T, D, F
Laminin subunit- alpha-5, gamma-1	LAMA5, LAMC1	M, H, D, F
Neural cell adhesion molecule 1	NCAM1	H, T, D
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial	NDUFA9	H, T, D
Peptidyl-prolyl cis–trans isomerase A	PPIA	T, D, N
Ras-related protein Rac1	RAC1	H, T, D
Serine/arginine-rich splicing factor 4	SRSF2	M, H, D
Synapsin-1	SYN1	H, T, D
Thy-1 membrane glycoprotein	THY1	M, T, D
Tubulointerstitial nephritis antigen-like	TINAGL1	M, H, D
Tropomyosin alpha-3 chain	TPM3	H, T, D

Summary of proteins identified in our analyses that have not yet been reported to be associated with Aβ fibrils. Experimental evidence in this study- M Mouse (LFQ MS/MS), H Human (LFQ MS/MS), D Multiprotease digestion (LFQ MS/MS), T TMT analysis (MS3), N primary neurons (LFQ MS/MS); F Fly (LFQ MS/MS)

ISSN: 1750-1326