PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28747495-1	2017	A highly conserved threonine near the C terminus of gp120 of human immunodeficiency virus (HIV) and simian immunodeficiency virus (SIV) was investigated for its contributions to envelope protein function and virion infectivity.	Threonine	19-28	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	52-57	
28747495-3	2017	We found that this Thr was critical for the association of gp120 with the virion and that amino acid substitution increased the amount of dissociated gp120 in the cell culture supernatant.	Threonine	19-22	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	59-64	
28747495-3	2017	We found that this Thr was critical for the association of gp120 with the virion and that amino acid substitution increased the amount of dissociated gp120 in the cell culture supernatant.	Threonine	19-22	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	150-155	
28747495-8	2017	Nonetheless, it remains theoretically possible that the repertoire of GalNAc transferase isoforms in natural target cells for HIV and SIV in vivo could result in O-glycosylation of the threonine residue in question and that this could boost the infectivity of virions beyond the levels seen in the absence of such O-glycosylation.IMPORTANCE Approximately 50% of the mass of the gp120 envelope glycoprotein of both HIV and SIV is N-linked carbohydrate.	Threonine	185-194	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	378-383	
19666543-8	2009	Very strong selection for sequons with both Thr and Ser in glycoprotein of M(r) 120,000 (gp120) of HIV and related retroviruses results from this same mechanism, as well as amino acid composition bias and increases in AT content.	Threonine	44-47	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	89-94	
15043212-1	2003	Peptide T, named for its high threonine content (ASTTTNYT), was derived by a database search which assumed that a relevant receptor binding epitope within env (gp120) would have sequence homology to a known signaling peptide.	Threonine	30-39	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	160-165	
9173240-0	1997	[Theoretical study of the spatial structure of the Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr segment of the HIV gp120 protein, responsible for binding of the virus with the T-cell T4 receptor].	Threonine	59-62	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	102-107	
9173240-0	1997	[Theoretical study of the spatial structure of the Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr segment of the HIV gp120 protein, responsible for binding of the virus with the T-cell T4 receptor].	Threonine	63-66	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	102-107	
9173240-0	1997	[Theoretical study of the spatial structure of the Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr segment of the HIV gp120 protein, responsible for binding of the virus with the T-cell T4 receptor].	Threonine	63-66	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	102-107	
7503990-4	1993	However, this antibody efficiently recognized linear V3 loop peptides containing either the Ala or Thr residue at position 21, indicating that a local change in conformation was responsible for the epitope loss in the native gp120.	Threonine	99-102	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	225-230	
8356803-7	1993	Furthermore, the ability of 10 human HIV-1-positive sera to block the binding of soluble CD4 to mammalian-recombinant gp120 correlated weakly with their differentiation of neutralization between the wild-type and the Env:Ala582(-->Thr)-mutant virus.	Threonine	234-237	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	118-123	
1575731-1	1992	Peptide T (H-Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr-OH), a fragment of HIV gp120, has been reported to inhibit binding of the virus to the CD4 receptor.	Threonine	21-24	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	68-73	
1575731-1	1992	Peptide T (H-Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr-OH), a fragment of HIV gp120, has been reported to inhibit binding of the virus to the CD4 receptor.	Threonine	25-28	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	68-73	
1898096-5	1991	In addition, the N-glycanase-resistant oligosaccharides of gp120 were found to contain N-acetyl-galactosamine, a common constituent of Ser/Thr-linked oligosaccharides.	Threonine	139-142	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	59-64	
2677400-9	1989	An arginine to threonine mutation at gp120 amino acid 518, the terminal residue of gp120, abolishes both gp160 cleavage and syncytium formation.	Threonine	15-24	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	37-42	
2677400-9	1989	An arginine to threonine mutation at gp120 amino acid 518, the terminal residue of gp120, abolishes both gp160 cleavage and syncytium formation.	Threonine	15-24	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	83-88	
2436231-1	1987	A highly immunogenic epitope from a conserved COOH-terminal region of the human immunodeficiency virus (HIV) gp120 envelope protein has been identified with antisera from HIV-seropositive subjects and a synthetic peptide (SP-22) containing 15 amino acids from this region (Ala-Pro-Thr-Lys-Ala-Lys-Arg-Arg-Val-Val-Gln-Arg-Glu-Lys-Arg).	Threonine	281-284	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	109-114