HUGO ID Detailed Result 1325

PMID	Match String	Actual String	Score	Flanking text	Edited by	Edit
10742195	PrP	PrP	1.9	a theme echoed in the recent proposal that A_amp_#x3b2 and PrP the proteins respectively involved in Alzheimer_amp_#x2019 s disease and prion
10742195	PrP	PrP	1.9	also how well known toxic proteins such as A_amp_#x3b2 and PrP could function as antioxidants (see see below
10742195	PrP	PrP	1.9	The infectious particle is a protein PrP Sc that collects in the CJD-affected brain and is a
10742195	PrP	PrP	1.9	is a modified and protease-resistant form of a ubiquitous protein PrP c
10742195	PrP	PrP	1.9	was the publication by David Brown et al 35 that PrP c possesses SOD activity
10742195	PrP	PrP	1.9	of the earlier work of Brown (and and others characterizing PrP c as a Cu 2 -binding protein exhibiting high-affinity cooperative
10742195	PrP	PrP	1.9	out of cells 40 an activity resembling that proposed for PrP c
10742195	PrP	PrP	1.9	Unlike PrP c interaction with Cu 2 37 the A_amp_#x3b2 precursor interaction
10742195	PrP	PrP	1.9	The SOD activity of PrP c is also intriguing because of the neuropathological similarities between
10742195	PrP	PrP	1.9	Assuming that PrP c and A_amp_#x3b2 are indeed also physiological SOD-type antioxidants then
10742195	PrP	PrP	1.9	Like mutant SOD1 PrP sc might be a modification of PrP that induces a
10742195	PrP	PrP	1.9	Like mutant SOD1 PrP sc might be a modification of PrP that induces a Cu 2 -related gain of function perhaps
10742195	PrP	PrP	1.9	supported by recent reports that Cu 2 treatment of denatured PrP Sc restores protease resistance and infectivity 42
10742195	PrP	PrP	1.9	Also the respective conformations of strain variants of PrP Sc have now been reported to depend upon Cu 2
10742195	PrP	PrP	1.9	Recently we have reported 44 that the copper-binding domain of PrP c reduces Cu 2 and uses O 2 to produce
10742195	PrP	PrP	1.9	In normal SOD1 Cu A_amp_#x3b2 or PrP c the Cu 2 active site would be shielded from