PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17914241-6	2007	Whereas residues valine, leucine, methionine were highly conserved for insulin receptor.	Leucine	25-32	insulin receptor	Homo sapiens	71-87	
8093054-0	1994	Leu 193 mutation in the cysteine rich region of the insulin receptor inhibits the cleavage of the insulin receptor precursor but not insulin binding.	Leucine	0-3	insulin receptor	Homo sapiens	52-68	
7989492-3	1994	The nucleotide sequence analysis of the patient"s genomic DNA revealed a 3-basepair in-frame deletion in one allele, resulting in the loss of leucine at position 999 of the insulin receptor (delta Leu999).	Leucine	142-149	insulin receptor	Homo sapiens	173-189	
7665623-0	1995	Replacements of leucine 87 in human insulin receptor alter affinity for insulin.	Leucine	16-23	insulin receptor	Homo sapiens	36-52	
7665623-1	1995	In a previous analysis, we identified a point mutation that substituted Pro (CCG) for Leu (CTG) at amino acid 87 in the alpha-subunit of the insulin receptor (IR) in a Japanese patient with leprechaunism.	Leucine	86-89	insulin receptor	Homo sapiens	141-157	
7665623-1	1995	In a previous analysis, we identified a point mutation that substituted Pro (CCG) for Leu (CTG) at amino acid 87 in the alpha-subunit of the insulin receptor (IR) in a Japanese patient with leprechaunism.	Leucine	86-89	insulin receptor	Homo sapiens	159-161	
7665623-5	1995	The Pro-87 IR reduced the insulin binding affinity to about 15% of Leu-87 IR, and the dissociation of insulin in Pro-87 IR was more rapid than in Leu-87 IR.	Leucine	67-70	insulin receptor	Homo sapiens	11-13	
7665623-5	1995	The Pro-87 IR reduced the insulin binding affinity to about 15% of Leu-87 IR, and the dissociation of insulin in Pro-87 IR was more rapid than in Leu-87 IR.	Leucine	67-70	insulin receptor	Homo sapiens	74-76	
8093054-0	1994	Leu 193 mutation in the cysteine rich region of the insulin receptor inhibits the cleavage of the insulin receptor precursor but not insulin binding.	Leucine	0-3	insulin receptor	Homo sapiens	98-114	
8093054-1	1994	To characterize the Leu 193 mutant insulin receptor, which was found in a patient with extreme insulin resistance, the mutant insulin receptor was overexpressed in Rat-1 fibroblasts by transfection of mutated insulin receptor cDNA.	Leucine	20-23	insulin receptor	Homo sapiens	35-51	
2318937-5	1990	Polymorphisms in the nucleotide sequences for codons 523 (Ala), 1058 (His), and 1062 (Leu) provided useful markers to differentiate the patient"s two alleles of the insulin receptor gene.	Leucine	86-89	insulin receptor	Homo sapiens	165-181	
8270132-5	1993	One allele contains in-frame 12 additional base pairs in exon 3 coding for the amino acids Leu-His-Leu-Val located between Asp-261 and Leu-262 in the receptor"s extracellular domain, being the first report of an insertion mutation of the insulin receptor gene.	Leucine	91-94	insulin receptor	Homo sapiens	238-254	
2192846-4	1990	Replacing A3-Val with Leu, B24-Phe with Ser, or B25-Phe with Leu results in molecules that have essentially normal immunoreactivity but greatly reduced insulin-receptor-binding potency.	Leucine	22-25	insulin receptor	Homo sapiens	152-168	
2192846-4	1990	Replacing A3-Val with Leu, B24-Phe with Ser, or B25-Phe with Leu results in molecules that have essentially normal immunoreactivity but greatly reduced insulin-receptor-binding potency.	Leucine	61-64	insulin receptor	Homo sapiens	152-168	
24121506-5	2013	Within L1C domains, five amino acid residues (Leu-135, Gly-188, Arg-244, and vicinal His-318 and Lys-319) were identified as IRR-specific by species conservation analysis of the IR family.	Leucine	46-49	insulin receptor	Homo sapiens	125-127	
2479553-0	1989	A leucine-to-proline mutation in the insulin receptor in a family with insulin resistance.	Leucine	2-9	insulin receptor	Homo sapiens	37-53	
26950281-8	2017	The surface area around position A3 was increased when valine was substituted by leucine, while at positions B24 and B25 aromatic amino acid phenylalanine replaced by non-aromatic serine and leucine might be responsible for fewer binding interactions at the binding site of IR that leads to instability of the complex.	Leucine	191-198	insulin receptor	Homo sapiens	274-276