PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16608305-0	2006	Complexation, structure, and superoxide dismutase activity of the imidazolate-bridged dinuclear copper moiety with beta-cyclodextrin and its guanidinium-containing derivative.	Guanidine	141-152	superoxide dismutase 1	Homo sapiens	29-49	
21549128-5	2011	Previously, we developed several time-resolved techniques to monitor structural changes in SOD1 as it unfolds in guanidine hydrochloride.	Guanidine	113-136	superoxide dismutase 1	Homo sapiens	91-95	
19325915-4	2009	When agitated at acidic pH in the presence of low concentrations of guanidine or acetonitrile, metalated SOD1 formed fibrillar material which bound both thioflavin T and Congo red and had circular dichroism and infrared spectra characteristic of amyloid.	Guanidine	68-77	superoxide dismutase 1	Homo sapiens	105-109	
15694395-5	2005	The observed effect is consistent with an exposed protein surface of SOD in the presence of 4M guanidinium chloride smaller than what could be expected for a random coil.	Guanidine	95-115	superoxide dismutase 1	Homo sapiens	69-72	
15485869-2	2004	The dissociation of apo- and metal-bound human copper-zinc superoxide dismutase (SOD1) dimers induced by the chaotrope guanidine hydrochloride (GdnHCl) or the reductant Tris(2-carboxyethyl)phosphine (TCEP) has been analyzed using analytical ultracentrifugation.	Guanidine	119-142	superoxide dismutase 1	Homo sapiens	81-85	
15485869-2	2004	The dissociation of apo- and metal-bound human copper-zinc superoxide dismutase (SOD1) dimers induced by the chaotrope guanidine hydrochloride (GdnHCl) or the reductant Tris(2-carboxyethyl)phosphine (TCEP) has been analyzed using analytical ultracentrifugation.	Guanidine	144-150	superoxide dismutase 1	Homo sapiens	81-85	
15485869-4	2004	Sedimentation velocity experiments show that apo-SOD1 dimers dissociate cooperatively over the range 0.5-1.0 M GdnHCl.	Guanidine	111-117	superoxide dismutase 1	Homo sapiens	49-53	
15485869-5	2004	In contrast, metal-bound SOD1 dimers possess a more compact shape and dissociate at significantly higher GdnHCl concentrations (2.0-3.0 M).	Guanidine	105-111	superoxide dismutase 1	Homo sapiens	25-29	
10845696-1	2000	The equilibrium unfolding process of human Cu,Zn superoxide dismutase has been quantitatively monitored through circular dichroism and fluorescence spectroscopy as a function of increasing guanidinium hydrochloride concentration.	Guanidine	189-214	superoxide dismutase 1	Homo sapiens	43-69	
18761352-5	2008	Here, we present a method by which we were able to measure the rates of metal release during SOD1 unfolding in guanidine hydrochloride.	Guanidine	111-134	superoxide dismutase 1	Homo sapiens	93-97	
16608305-5	2006	Interestingly, the guanidinium-containing 1/betaGCD system showed higher SOD activity (IC50 = 0.16 muM), which is enhanced at least by 30% in comparison with that of guanidinium-lacking 2.	Guanidine	19-30	superoxide dismutase 1	Homo sapiens	73-76	
16608305-5	2006	Interestingly, the guanidinium-containing 1/betaGCD system showed higher SOD activity (IC50 = 0.16 muM), which is enhanced at least by 30% in comparison with that of guanidinium-lacking 2.	Guanidine	166-177	superoxide dismutase 1	Homo sapiens	73-76	
16608305-6	2006	This result supports that the positive guanidinium plays a role in the catalytic mechanism of Cu,Zn-SOD by ensuring that superoxide enters and peroxide leaves rapidly from the coordination sphere of the copper ion.	Guanidine	39-50	superoxide dismutase 1	Homo sapiens	100-103