PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
9342868-6	1997	The amino acid sequence deduced from an apparently full-length gl8 cDNA exhibits highly significant sequence similarity to a group of enzymes from plants, eubacteria, and mammals that catalyzes the reduction of ketones.	Ketones	211-218	glossy 8	Zea mays	63-66
9342868-7	1997	This finding suggests that the GL8 protein probably functions as a reductase during fatty acid elongation in the cuticular wax biosynthetic pathway.	Fatty Acids	84-94	glossy 8	Zea mays	31-34
9342868-7	1997	This finding suggests that the GL8 protein probably functions as a reductase during fatty acid elongation in the cuticular wax biosynthetic pathway.	Waxes	123-126	glossy 8	Zea mays	31-34
27519736-0	1987	Epicuticular waxes if maize as affected by the interaction of mutant gl8 with gl2, gl3, gl4 and gl14.	alpha-methylhomocysteine thiolactone	78-81	glossy 8	Zea mays	69-72
27519736-0	1987	Epicuticular waxes if maize as affected by the interaction of mutant gl8 with gl2, gl3, gl4 and gl14.	GL3	83-86	glossy 8	Zea mays	69-72
27519736-0	1987	Epicuticular waxes if maize as affected by the interaction of mutant gl8 with gl2, gl3, gl4 and gl14.	gl14	96-100	glossy 8	Zea mays	69-72
11891248-2	2002	The predicted GL8 protein exhibits significant sequence similarity to a class of enzymes that catalyze the reduction of a ketone group to a hydroxyl group.	Ketones	122-128	glossy 8	Zea mays	14-17
11891248-6	2002	In addition, anti-GL8 immunoglobulin G inhibited the in vitro elongation of stearoyl-CoA by leek and maize microsomal acyl-CoA elongase.	stearoyl-coenzyme A	76-88	glossy 8	Zea mays	18-21