PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29223806-3	2018	In this paper we overcome this heterogeneity, using engineered interferon derivatives with phenylalanine residue directly downstream of the N-terminal methionine (Met-Phe-IFN).	Phenylalanine	91-104	interferon alpha 1	Homo sapiens	171-174	
29223806-8	2018	This latter protein also had a heterogeneous N-terminal but addition of phenylalanine following Met, (Met-Phe-IFN-b5-chimera), resolved this problem and gave enhanced biological activity.	Phenylalanine	72-85	interferon alpha 1	Homo sapiens	110-113	
28498306-3	2017	A phenylalanine (F) substitution of this Y84 residue abolishes NS1-mediated downregulation of IFN-inducible STAT phosphorylation, and surface IFNAR1 expression.	Phenylalanine	2-15	interferon alpha 1	Homo sapiens	94-97	
12860366-6	2003	We found evidence for IFN-alpha to decrease concentrations of all AA except phenylalanine.	Phenylalanine	76-89	interferon alpha 1	Homo sapiens	22-31	
23072726-8	2013	These results indicate that IFN-alpha is associated with decreased peripheral conversion of Phen to Tyr, which in turn is associated with reduced DA in the brain as well as fatigue.	Phenylalanine	92-96	interferon alpha 1	Homo sapiens	28-37	
22191466-3	2012	This study aimed to investigate whether treatment with cytokine interferon-alpha (IFN-alpha) influences Phe concentrations and the Phe to Tyr ratios (Phe/Tyr) measured by HPLC.	Phenylalanine	104-107	interferon alpha 1	Homo sapiens	82-91	
22191466-8	2012	The increase of Phe concentrations and of Phe/Tyr in HCV infected individuals is caused by IFN-alpha therapy.	Phenylalanine	16-19	interferon alpha 1	Homo sapiens	91-100	
22191466-8	2012	The increase of Phe concentrations and of Phe/Tyr in HCV infected individuals is caused by IFN-alpha therapy.	Phenylalanine	42-45	interferon alpha 1	Homo sapiens	91-100	
22191466-10	2012	Future studies should show whether side effects of IFN-alpha treatment such as mood changes and depression will be associated with the alterations of Phe metabolism.	Phenylalanine	150-153	interferon alpha 1	Homo sapiens	51-60	
11277596-3	2001	After the 36th Phe residue, which was located closely to the 122nd Tyr residue in the tertiary structure, was mutated to Ser using site-directed mutagenesis, the analgesic activity of this mutant lost completely, but the antiviral activity of IFNalpha still maintained 40.5% of wild type IFNalpha.	Phenylalanine	15-18	interferon alpha 1	Homo sapiens	243-251	
11277596-3	2001	After the 36th Phe residue, which was located closely to the 122nd Tyr residue in the tertiary structure, was mutated to Ser using site-directed mutagenesis, the analgesic activity of this mutant lost completely, but the antiviral activity of IFNalpha still maintained 40.5% of wild type IFNalpha.	Phenylalanine	15-18	interferon alpha 1	Homo sapiens	288-296	
11277596-4	2001	The results suggest that the 36th Phe residue is one of the constituent for the analgesic domain of IFNalpha and inferred that the analgesic domain of IFNalpha consists of the 122nd Tyr and the residues around the 122nd in the tertiary structure, which include the 36th Phe.	Phenylalanine	34-37	interferon alpha 1	Homo sapiens	100-108	
11277596-4	2001	The results suggest that the 36th Phe residue is one of the constituent for the analgesic domain of IFNalpha and inferred that the analgesic domain of IFNalpha consists of the 122nd Tyr and the residues around the 122nd in the tertiary structure, which include the 36th Phe.	Phenylalanine	34-37	interferon alpha 1	Homo sapiens	151-159	
11277596-4	2001	The results suggest that the 36th Phe residue is one of the constituent for the analgesic domain of IFNalpha and inferred that the analgesic domain of IFNalpha consists of the 122nd Tyr and the residues around the 122nd in the tertiary structure, which include the 36th Phe.	Phenylalanine	270-273	interferon alpha 1	Homo sapiens	100-108	
11277596-4	2001	The results suggest that the 36th Phe residue is one of the constituent for the analgesic domain of IFNalpha and inferred that the analgesic domain of IFNalpha consists of the 122nd Tyr and the residues around the 122nd in the tertiary structure, which include the 36th Phe.	Phenylalanine	270-273	interferon alpha 1	Homo sapiens	151-159	
8910507-7	1996	IFN-alpha-induced receptor tyrosine phosphorylation was not critical for signaling because mutation of Tyr residues to Phe did not prevent the biological response to IFN-alpha.	Phenylalanine	119-122	interferon alpha 1	Homo sapiens	0-9