PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
26313597-2	2015	In plants, cryptochrome (cry1, cry2) biological activity has been linked to flavin photoreduction via an electron transport chain to the protein surface comprising 3 evolutionarily conserved tryptophan residues known as the "Trp triad."	4,6-dinitro-o-cresol	76-82	cryptochrome 2	Arabidopsis thaliana	31-35	
31832774-0	2019	The Arabidopsis cryptochrome 2 I404F mutant is hypersensitive and shows flavin reduction even in the absence of light.	4,6-dinitro-o-cresol	72-78	cryptochrome 2	Arabidopsis thaliana	16-30	
27423124-2	2016	Photon absorption by Arabidopsis cryptochromes cry1 and cry2 initiates electron transfer to the oxidized flavin cofactor (FADox) and formation of the presumed biological signaling state FADH .	4,6-dinitro-o-cresol	105-111	cryptochrome 2	Arabidopsis thaliana	56-60	
27446119-2	2016	Arabidopsis cryptochromes (cry1 and cry2) absorb light through an oxidized flavin (FADox) cofactor which undergoes reduction to both FADH  and FADH(-) redox states.	4,6-dinitro-o-cresol	75-81	cryptochrome 2	Arabidopsis thaliana	36-40	
27446119-5	2016	Our model fits the experimental data for flavin photoconversion in vitro for both cry1 and cry2, providing calculated quantum yields which are significantly lower in cry1 than for cry2.	4,6-dinitro-o-cresol	41-47	cryptochrome 2	Arabidopsis thaliana	91-95	
27446119-5	2016	Our model fits the experimental data for flavin photoconversion in vitro for both cry1 and cry2, providing calculated quantum yields which are significantly lower in cry1 than for cry2.	4,6-dinitro-o-cresol	41-47	cryptochrome 2	Arabidopsis thaliana	180-184	
27446119-7	2016	The fit to the in vivo data provided quantum yields for cry1 and cry2 flavin reduction similar to those obtained in vitro, with decreased cry1 quantum yield as compared to cry2.	4,6-dinitro-o-cresol	70-76	cryptochrome 2	Arabidopsis thaliana	65-69	
26313597-4	2015	However, photoreduction of the flavin in Arabidopsis cry2 proteins occurs in vivo even with mutations in the Trp triad, indicating the existence of alternative electron transfer pathways to the flavin.	4,6-dinitro-o-cresol	31-37	cryptochrome 2	Arabidopsis thaliana	53-57	
26313597-4	2015	However, photoreduction of the flavin in Arabidopsis cry2 proteins occurs in vivo even with mutations in the Trp triad, indicating the existence of alternative electron transfer pathways to the flavin.	4,6-dinitro-o-cresol	194-200	cryptochrome 2	Arabidopsis thaliana	53-57	
25428980-2	2014	Plant cryptochrome (cry1 and cry2) biological activity has been linked to flavin photoreduction via an electron transport chain comprising three evolutionarily conserved tryptophan residues known as the Trp triad.	4,6-dinitro-o-cresol	74-80	cryptochrome 2	Arabidopsis thaliana	29-33	
17355959-7	2007	Here we have shown that Arabidopsis Cry2 undergoes a photocycle in which semireduced flavin (FADH(.))	4,6-dinitro-o-cresol	85-91	cryptochrome 2	Arabidopsis thaliana	36-40	
17355959-9	2007	Green light irradiation of Cry2 causes a change in the equilibrium of flavin oxidation states and attenuates Cry2-controlled responses such as flowering.	4,6-dinitro-o-cresol	70-76	cryptochrome 2	Arabidopsis thaliana	27-31