PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9828013-1	1998	Limited cleavage of oxidized and reduced horse heart cytochrome c (Cyt c) and the azide complex of Cyt c by proteinase K at room temperature yields a single cut within the central loop (36-60 in the sequence).	Azides	82-87	cytochrome c, somatic	Equus caballus	99-104	
9828013-4	1998	The results we obtain indicate that oxidized Cyt c is 2.0 kcal mol(-1) less stable than the reduced form, and 0.07 kcal mol(-1) is more stable than the Cyt c: azide complex at 25 degrees C. These values agree in magnitude with results from hydrogen exchange and unfolding studies, suggesting that the stability of a protein can be directly related to its structural dynamics.	Azides	159-164	cytochrome c, somatic	Equus caballus	45-50	
9828013-4	1998	The results we obtain indicate that oxidized Cyt c is 2.0 kcal mol(-1) less stable than the reduced form, and 0.07 kcal mol(-1) is more stable than the Cyt c: azide complex at 25 degrees C. These values agree in magnitude with results from hydrogen exchange and unfolding studies, suggesting that the stability of a protein can be directly related to its structural dynamics.	Azides	159-164	cytochrome c, somatic	Equus caballus	152-157	
8627283-0	1996	Azide, cyanide, fluoride, imidazole and pyridine binding to ferric and ferrous native horse heart cytochrome c and to its carboxymethylated derivative: a comparative study.	Azides	0-5	cytochrome c, somatic	Equus caballus	98-110	
8627283-1	1996	Azide, cyanide, fluoride, imidazole, and pyridine binding to ferric and ferrous native horse heart cytochrome c and to its carboxymethylated derivative has been investigated, from the thermodynamic viewpoint, at pH 7.5 and 25.0 degrees C. Ligand affinity for ferric and ferrous carboxymethylated cytochrome c is higher by about 30- and 400-fold, respectively, than that observed for the native protein.	Azides	0-5	cytochrome c, somatic	Equus caballus	99-111	
13072-14	1977	The spectrum of horse cytochrome c with added azide, cyanide, hydroxide, or imidazole as axial ligands has also been examined.	Azides	46-51	cytochrome c, somatic	Equus caballus	22-34	
6268262-5	1980	Both processes are sensitive to cyanide, but azide inhibits only the authentic cytochrome c oxidase catalyzed process and BCS the ferricytochrome c stimulated reaction.	Azides	45-50	cytochrome c, somatic	Equus caballus	79-91	
167834-1	1975	Azide and imidazole complexes of ferric cytochrome c.	Azides	0-5	cytochrome c, somatic	Equus caballus	40-52	
12504251-0	2003	NMR study of the conformational transition of cytochrome c upon the displacement of Met80 by exogenous ligand: structural and magnetic characterization of azidoferricytochrome c. As the exogenous ligand-cytochrome c complexes were purported to represent models for the unfolding intermediate of cytochrome c, NMR spectroscopy has been utilized to study the azide adduct of horse heart cytochrome c.	Azides	357-362	cytochrome c, somatic	Equus caballus	46-58