PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
214303-6	1978	Antimycin A binding causes a complex set of changes in the CD spectrum of the complex, which can be attributed to a severe and specific distortion of the environment of the chromophore of cytochrome b.	Antimycin A	0-11	cytochrome b	Saccharomyces cerevisiae S288C	188-200	
2517475-2	1989	The results concerning the structure-function relationship of cytochrome b in this complex, analyzed within the framework of the eight transmembrane alpha helice cytochrome b folding model, agree with the following features of the proton motive Q cycle (or SQ cycle): i) the antimycin A and myxothiazol binding domains are located on opposite sides of the inner mitochondrial membrane; and ii) the antimycin A binding domain is associated with the b562 domain, the myxothiazol domain with the b565 domain.	Antimycin A	275-286	cytochrome b	Saccharomyces cerevisiae S288C	62-74	
2517475-2	1989	The results concerning the structure-function relationship of cytochrome b in this complex, analyzed within the framework of the eight transmembrane alpha helice cytochrome b folding model, agree with the following features of the proton motive Q cycle (or SQ cycle): i) the antimycin A and myxothiazol binding domains are located on opposite sides of the inner mitochondrial membrane; and ii) the antimycin A binding domain is associated with the b562 domain, the myxothiazol domain with the b565 domain.	Antimycin A	398-409	cytochrome b	Saccharomyces cerevisiae S288C	62-74	
2517475-4	1989	However, functional studies are reported here that are not in agreement with the following features of the above models: i) the serial arrangement of the two hemes of cytochrome b and ii) the isolation of cytochrome b from redox changes with the couple fumarate/succinate in the presence of antimycin A and myxothiazol.	Antimycin A	291-302	cytochrome b	Saccharomyces cerevisiae S288C	205-217	
2615656-0	1989	Mitochondrial cytochrome b genes with a six-nucleotide deletion or single-nucleotide substitutions confer resistance to antimycin A in the yeast Kluyveromyces lactis.	Antimycin A	120-131	cytochrome b	Saccharomyces cerevisiae S288C	14-26	
6262574-1	1980	Complex III isolated from yeast mitochondria catalyzed an antimycin A and Diuron-sensitive coenzyme QH2-cytochrome c reductase activity with a turnover number of 15.7 sec(-1) and contained 10 nmoles of cytochrome b and 4.6 nmoles of cytochrome c1 per mg of protein.	Antimycin A	58-69	cytochrome b	Saccharomyces cerevisiae S288C	202-214	
7002556-5	1980	Two different methods have been used to determine the cytochrome b-565 content: anaerobic titrations and antimycin-A-induced reduction of cytochrome b-565.	Antimycin A	105-116	cytochrome b	Saccharomyces cerevisiae S288C	54-66	
7002556-5	1980	Two different methods have been used to determine the cytochrome b-565 content: anaerobic titrations and antimycin-A-induced reduction of cytochrome b-565.	Antimycin A	105-116	cytochrome b	Saccharomyces cerevisiae S288C	138-150	
19224349-7	2009	Our results suggest that lipoperoxidation impairs electron transfer mainly at cytochrome b in complex III, which leads to increased resistance to antimycin A and ROS generation due to an electron leak at the level of the Q(O) site of complex III.	Antimycin A	146-157	cytochrome b	Saccharomyces cerevisiae S288C	78-90	
340894-4	1977	The mapping relationship of mutants resistant to antimycin A or funiculosin to various cob mutants is described.	Antimycin A	49-60	cytochrome b	Saccharomyces cerevisiae S288C	87-90	
5533677-0	1970	Interactions of uncoupling agents and of antimycin A with cytochrome b in yeast and heart muscle preparation under anaerobic conditions.	Antimycin A	41-52	cytochrome b	Saccharomyces cerevisiae S288C	58-70	
28960782-5	2018	In Saccharomyces cerevisiae, amino acid substitutions N31K, G37C and L198F at the Qi quinone binding site of cytochrome b reduced sensitivity to fenpicoxamid, UK-2A and antimycin A.	Antimycin A	169-180	cytochrome b	Saccharomyces cerevisiae S288C	109-121