AGGRESCAN: a server for the prediction and evaluation of

BMC Bioinformatics

Table 1 List and ranking of the predicted aggregation-prone regions in the different disease-linked polypeptides analyzed in this study and comparison with the available experimental data.

Protein	Experimental region^a	Predicted region^b	Ranking^c	References
Abri	1–34	4–9	2/2	[52]
		15–28	1/2
Adan	1–34	4–9	2/2	[53]
		15–24	1/2
	68–78	66–77	1/6	[54–56]
α-Synuclein	31–109	36–42	2/6	[56]
		49–55	4/6
		87–94	5/6
Amphoterin	12–27	14–22	2/3	[57]
Amyloid-β-protein	17–21	17–22	2/2	[58]
	31–36/38–42	30–42	1/2
Apoliprotein A-I	1–83	13–21	2/2	[59]
Apoliprotein A-II	N-terminal fragments	1–19	1/3	[11]
Apoliprotein A-IV	N-terminal fragments	1–19	1/6	[11]
Apoliprotein C-II	57–74	60–67	2/3	[60]
		69–76	1/3
β2-Microgobulin	21–41	22–30	2/2	[61]
	59–79	59–70	1/2	[62]
Exon 30 Tropoelastin	1–25	1–7	2/2	[63]
		9/18	1/2
Fibrinogen A α-chain	501–506	499–521	1/6	[64]
	482–504	501–506	1/5
Glycophorin A	70–98	74–98	1/4	[65]
Insulin	1–38	12–19	1/3	[66]
		21–27	3/3
Islet amyloid polypeptide	8–20	13–18	1/2	[67]
	20–29	24–28	2/2	[68]
Lysozyme (Hen)	40–64	54–62	2/4	[69]
	49–101	76–84	3/4	[70]
Medin	47–54	49–55	1/3	[71]
Myoglobin (Horse)	101–118	101–115	1/4	[72]
Prion Protein	106–147	117–136	3/6	[73]
		138–142	6/6
Prolactin	1–34	10–32	2/9	[74]
Pulmonary surfactant protein	24–58	31–59	1/5	[25]
Serum Amyloid A	2–12	1–9	1/2	[75]
Tau	301–320	304–311	1/2	[27]
	10–20	12–19	2/7	[76]
Transthyretin	105–115	105–112	3/7	[77]
		114–123	4/7

^aSequence stretches experimentally identified as critical for protein aggregation.
^bCoincident aggregation-prone segments as predicted by AGGRESCAN.
^cThe rank position refers to the entire protein and reflects the importance of this specific "hot spot" (HS) relative to all the aggregation-prone regions identified by AGGRESCAN in the protein. (i.e., 1/4 indicates that this HS has the highest aggregation propensity of the four detected in a particular sequence by the software)

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