PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12122994-1	2002	Cytochrome c was adsorbed readily and remained electroactive, with a redox potential of 32 mV, on TiO2 films placed on SnO2; similar behaviour was observed in glycerol, whereas in acetonitrile, irreversible oxidation occurred at a potential of 800 mV.	Glycerol	159-167	cytochrome c, somatic	Homo sapiens	0-12	
15893966-6	2005	Finally, we discuss in detail our own molecular dynamics simulations on cytochrome c and show what happens under high pressure, how glycerol influences structure and volume fluctuations, and how all this compares with experiments.	Glycerol	132-140	cytochrome c, somatic	Homo sapiens	72-84	
15659779-7	2004	In this study, we demonstrate that a mixture of glycerol and cyanide reduced cytochrome c and nitroblue tetrazolium, both of which are superoxide anion indicators.	Glycerol	48-56	cytochrome c, somatic	Homo sapiens	77-89	
14695290-1	2004	We performed pressure-tuning hole-burning experiments on a modified cytochrome c protein in a glycerol/buffer glass.	Glycerol	94-102	cytochrome c, somatic	Homo sapiens	68-80	
11867476-1	2002	We determined the stability diagram of a modified cytochrome c protein in a glycerol water mixture by measuring the first and the second moment of the fluorescence from the chromophore as a function of temperature and pressure.	Glycerol	76-84	cytochrome c, somatic	Homo sapiens	50-62	
11902665-0	2002	Glycerol-induced formation of the molten globule from acid-denatured cytochrome c: implication for hierarchical folding.	Glycerol	0-8	cytochrome c, somatic	Homo sapiens	69-81	
11902665-1	2002	At high concentration (98% or higher, v/v), glycerol induces collapse of acid-denatured cytochrome c into a compact state, the G(U) state, showing a molten globule character.	Glycerol	44-52	cytochrome c, somatic	Homo sapiens	88-100	
11902665-3	2002	The spectroscopic properties of the G(U) state closely resemble those of the molten globule stabilized by the organic solvent from the native protein (called the G(N) state), indicating that glycerol can stabilize the molten globule of cytochrome c either from the native or the acid-denatured protein.	Glycerol	191-199	cytochrome c, somatic	Homo sapiens	236-248	
11321294-3	2001	Adding glycerol to acidified aqueous solutions of cytochrome c shifts the most abundant charge state from 17+ to 21+, shifts the maximum charge state from 20+ to 23+, and shifts the average charge state from 16.6+ to 20.9+.	Glycerol	7-15	cytochrome c, somatic	Homo sapiens	50-62	
31877449-1	2020	An orderly investigation of the levels of secondary and tertiary structures, kinetics of tertiary structural changes, and self diffusion coefficient of lysozyme and cytochrome c in the 0-70% (weight/volume) range of glycerol is reported.	Glycerol	216-224	cytochrome c, somatic	Homo sapiens	165-177	
10492021-0	1999	Formation of a molten-globule-like state of cytochrome c induced by high concentrations of glycerol.	Glycerol	91-99	cytochrome c, somatic	Homo sapiens	44-56	
10492021-1	1999	The effect of glycerol on the structure of cytochrome c was investigated by circular dichroism, absorbance and EPR spectroscopy.	Glycerol	14-22	cytochrome c, somatic	Homo sapiens	43-55	
8241386-3	1993	Glycerol promotes complex formation between cytochrome c and cytochrome b5 but inhibits that between cytochrome c and cytochrome c oxidase.	Glycerol	0-8	cytochrome c, somatic	Homo sapiens	44-56	
8241386-3	1993	Glycerol promotes complex formation between cytochrome c and cytochrome b5 but inhibits that between cytochrome c and cytochrome c oxidase.	Glycerol	0-8	cytochrome c, somatic	Homo sapiens	101-113	
8241386-3	1993	Glycerol promotes complex formation between cytochrome c and cytochrome b5 but inhibits that between cytochrome c and cytochrome c oxidase.	Glycerol	0-8	cytochrome c, somatic	Homo sapiens	101-113	
8241386-7	1993	We interpret them to mean that either glycerol is binding to the oxidase, thereby displacing the cytochrome c, or that water is required at this protein-protein interface.	Glycerol	38-46	cytochrome c, somatic	Homo sapiens	97-109	
6251919-1	1980	It has been shown that during fast (< 1 ms) photosensitized by anthraquinone or benzophenone reduction of cytochrome c in 0.15 N NaOH water-glycerol solutions ferrocytochrome c in a nonequilibrium state with increased reactivity was formed.	Glycerol	143-151	cytochrome c, somatic	Homo sapiens	109-121	
27479029-3	2016	To demonstrate this, the flipping motion of aromatic rings of F10 and Y97 amino acid residues of cytochrome c has been studied in glycerol/water mixtures by cross relaxation-suppressed exchange nuclear magnetic resonance spectroscopy.	Glycerol	130-138	cytochrome c, somatic	Homo sapiens	97-109