PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22345481-9	2012	We conclude that potent CD4bs bnMAbs can display differences in the way they recognize and access the CD4bs and that mimicry of CD4, as assessed by inducing conformational changes in monomeric gp120 that lead to enhanced exposure of the CD4i site, is not uniquely correlated with effective neutralization at the site of CD4 binding on HIV-1.	cd4bs	24-29	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	193-198	
22345481-9	2012	We conclude that potent CD4bs bnMAbs can display differences in the way they recognize and access the CD4bs and that mimicry of CD4, as assessed by inducing conformational changes in monomeric gp120 that lead to enhanced exposure of the CD4i site, is not uniquely correlated with effective neutralization at the site of CD4 binding on HIV-1.	cd4bs	102-107	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	193-198	
18076768-8	2007	CONCLUSION: Enhanced fusogenicity is a phenotype of the A-R5 Envs studied, which was associated with the presence of N362, enhanced HIV-1 entry kinetics and increased CD4bs exposure in gp120.	cd4bs	167-172	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	185-190	
15542540-1	2004	In an attempt to design immunogens that elicit broadly HIV-neutralizing antibodies, we recently engineered monomeric HIV-1 gp120 to bind preferentially b12, a broadly neutralizing antibody to the CD4-binding site (CD4bs) on gp120, by mutating four central residues in the CD4bs to alanine and introducing extra N-glycosylation sites potentially to mask unwanted B-cell epitopes.	cd4bs	214-219	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	123-128	
15542540-1	2004	In an attempt to design immunogens that elicit broadly HIV-neutralizing antibodies, we recently engineered monomeric HIV-1 gp120 to bind preferentially b12, a broadly neutralizing antibody to the CD4-binding site (CD4bs) on gp120, by mutating four central residues in the CD4bs to alanine and introducing extra N-glycosylation sites potentially to mask unwanted B-cell epitopes.	cd4bs	214-219	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	224-229	
12477867-1	2003	Alanine scanning mutagenesis was performed on monomeric gp120 of human immunodeficiency virus type 1 to systematically identify residues important for gp120 recognition by neutralizing and nonneutralizing monoclonal antibodies (MAbs) to the CD4 binding site (CD4bs).	cd4bs	259-264	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	151-156