PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27489265-11 2016 IMPORTANCE: The HIV-1 Env glycoprotein presents a dense patchwork of host cell-derived N-linked glycans. n-linked glycans 87-103 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 22-25 30355496-1 2018 Densely arranged N-linked glycans shield the HIV-1 envelope (Env) trimer from antibody recognition. n-linked glycans 17-33 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 51-59 30355496-1 2018 Densely arranged N-linked glycans shield the HIV-1 envelope (Env) trimer from antibody recognition. n-linked glycans 17-33 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 61-64 29579062-11 2018 Overall, our data demonstrate that HIV-1 isolates display differential sensitivity to lectins, in part due to the microheterogeneity of N-linked glycans expressed on the surface of the virus Env glycoprotein. n-linked glycans 136-152 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 191-194 28632942-1 2017 N-linked glycans such as 234 and 276 gp120 glycans are vital components of HIV evasion from humoral immunity and important for HIV-1 neutralization of many broadly neutralizing antibodies (bNAbs). n-linked glycans 0-16 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 37-42 26277072-1 2015 The glycan shield on the human immunodeficiency virus 1 (HIV-1) envelope (Env) glycoprotein has drawn attention as a target for HIV-1 vaccine design given that an increasing number of potent and broadly neutralizing antibodies (bNAbs) recognize epitopes entirely or partially comprised of high mannose type N-linked glycans. n-linked glycans 307-323 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 74-77 26972002-1 2016 The HIV-1 envelope glycoprotein trimer is covered by an array of N-linked glycans that shield it from immune surveillance. n-linked glycans 65-81 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 10-31 24967714-1 2014 N-linked glycans covering the surface of the HIV-1 glycoprotein gp120 are of major importance for the correct folding of this glycoprotein. n-linked glycans 0-16 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 64-69 26085151-1 2015 UNLABELLED: The gp120/gp41 HIV-1 envelope glycoprotein (Env) is highly glycosylated, with up to 50% of its mass consisting of N-linked glycans. n-linked glycans 126-142 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 16-21 26085151-1 2015 UNLABELLED: The gp120/gp41 HIV-1 envelope glycoprotein (Env) is highly glycosylated, with up to 50% of its mass consisting of N-linked glycans. n-linked glycans 126-142 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 33-54 26085151-1 2015 UNLABELLED: The gp120/gp41 HIV-1 envelope glycoprotein (Env) is highly glycosylated, with up to 50% of its mass consisting of N-linked glycans. n-linked glycans 126-142 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 56-59 25546301-1 2015 The crystal structure of a fully glycosylated HIV-1 gp120 core in complex with CD4 receptor and Fab 17b at 4.5-A resolution reveals 9 of the 15 N-linked glycans of core gp120 to be partially ordered. n-linked glycans 144-160 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 52-57 25546301-1 2015 The crystal structure of a fully glycosylated HIV-1 gp120 core in complex with CD4 receptor and Fab 17b at 4.5-A resolution reveals 9 of the 15 N-linked glycans of core gp120 to be partially ordered. n-linked glycans 144-160 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 169-174 26121645-2 2015 Using a probability calculation, we here demonstrate that there is a co-localization of disulphide bridges and N-linked glycans in HIV-1 gp120, with a predominance of N-linked glycans in close proximity to disulphide bridges, at the C-terminal side of the involved cysteines. n-linked glycans 111-127 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 137-142 26121645-2 2015 Using a probability calculation, we here demonstrate that there is a co-localization of disulphide bridges and N-linked glycans in HIV-1 gp120, with a predominance of N-linked glycans in close proximity to disulphide bridges, at the C-terminal side of the involved cysteines. n-linked glycans 167-183 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 137-142 24992528-9 2014 Essential elements of the glycan V3 supersite, embodied by as few as 3 N-linked glycans and ~ 25 Env residues, can be segregated into acceptor scaffolds away from the immune-evading capabilities of the rest of HIV-1 Env, thereby providing a means to focus the immune response on the scaffolded supersite. n-linked glycans 71-87 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 216-219 21715597-0 2011 Removal of two high-mannose N-linked glycans on gp120 renders human immunodeficiency virus 1 largely resistant to the carbohydrate-binding agent griffithsin. n-linked glycans 28-44 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 48-53 23536670-1 2013 Griffithsin, which binds N-linked glycans on gp120 to prevent HIV entry, has the most potent HIV-1 inhibitory activity described for any antiviral lectin and is being developed for topical preexposure prophylaxis. n-linked glycans 25-41 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 45-50 21957147-4 2011 The interaction of DCs with HIV-1 involves C-type lectin receptors, such as DC-specific ICAM-3-grabbing nonintegrin, which bind to the envelope glycoprotein complex (Env), which is decorated heavily with N-linked glycans. n-linked glycans 204-220 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 166-169 21880749-5 2011 We show here that galectin-1 directly binds to HIV-1 in a beta-galactoside-dependent fashion through recognition of clusters of N-linked glycans on the viral envelope gp120. n-linked glycans 128-144 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 167-172 24303005-3 2013 Here, we use a computational approach to determine the influence of N-linked glycans on the dynamics of the HIV-1 gp120 protein and, in particular, the V3 loop. n-linked glycans 68-84 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 114-119 22628288-1 2012 The human immunodeficiency virus type-1 (HIV-1) is able to shield immunogenic peptide epitopes on its envelope spike (a trimer of two glycoproteins, gp120 and gp41) by presenting numerous host-derived N-linked glycans. n-linked glycans 201-217 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 149-154 18434410-5 2008 These yeast proteins, like HIV-1 gp120, contain a large number and high density of N-linked glycans, with glycosidase digestion abrogating 2G12 cross-reactivity. n-linked glycans 83-99 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 33-38 19920089-1 2010 Design of an envelope glycoprotein (Env)-based vaccine against human immunodeficiency virus type-1 (HIV-1) is complicated by the large number of N-linked glycans that coat the protein and serve as a barrier to antibody-mediated neutralization. n-linked glycans 145-161 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 13-34 19920089-1 2010 Design of an envelope glycoprotein (Env)-based vaccine against human immunodeficiency virus type-1 (HIV-1) is complicated by the large number of N-linked glycans that coat the protein and serve as a barrier to antibody-mediated neutralization. n-linked glycans 145-161 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 36-39 8673525-0 1996 Influence of N-linked glycans in V4-V5 region of human immunodeficiency virus type 1 glycoprotein gp160 on induction of a virus-neutralizing humoral response. n-linked glycans 13-29 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 98-103 18322210-9 2008 Hence, N-linked glycans are critical determinants that can profoundly influence CD4 T cell recognition of HIV-1 gp120. n-linked glycans 7-23 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 112-117 11672902-2 2001 DNA encoding HIV-1 env is a poorly efficient B-cell immunogen and one probable explanation is that the numerous gp120 N-linked glycans gp120 may interfere with B-cell epitope presentation. n-linked glycans 118-134 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 19-22 11672902-2 2001 DNA encoding HIV-1 env is a poorly efficient B-cell immunogen and one probable explanation is that the numerous gp120 N-linked glycans gp120 may interfere with B-cell epitope presentation. n-linked glycans 118-134 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 112-117 11672902-2 2001 DNA encoding HIV-1 env is a poorly efficient B-cell immunogen and one probable explanation is that the numerous gp120 N-linked glycans gp120 may interfere with B-cell epitope presentation. n-linked glycans 118-134 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 135-140 11181557-0 2001 Loss of N-linked glycans in the V3-loop region of gp120 is correlated to an enhanced infectivity of HIV-1. n-linked glycans 8-24 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 50-55 11485624-4 2001 gp120 from both mutated viral clones had higher electrophoretic mobilities than gp120 from wild-type virus, confirming loss of N-linked glycans. n-linked glycans 127-143 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 0-5 8560759-0 1996 N-linked glycans in the CD4-binding domain of human immunodeficiency virus type 1 envelope glycoprotein gp160 are essential for the in vivo priming of T cells recognizing an epitope located in their vicinity. n-linked glycans 0-16 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 104-109 7523139-0 1994 Induction of HIV-1 envelope (gp120)-specific cytotoxic T lymphocyte responses in mice by recombinant CHO cell-derived gp120 is enhanced by enzymatic removal of N-linked glycans. n-linked glycans 160-176 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 29-34 2335819-1 1990 We have shown that enzymatic removal of N-linked glycans from human immunodeficiency virus type 1 (HIV-1) recombinant envelope glycoproteins gp160 and gp120 produced in BHK-21 cells did not significantly reduce their ability to bind to CD4, the cellular receptor for the virus. n-linked glycans 40-56 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 141-146 2335819-1 1990 We have shown that enzymatic removal of N-linked glycans from human immunodeficiency virus type 1 (HIV-1) recombinant envelope glycoproteins gp160 and gp120 produced in BHK-21 cells did not significantly reduce their ability to bind to CD4, the cellular receptor for the virus. n-linked glycans 40-56 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 151-156 7832633-1 1994 Glycosylation is necessary for HIV-1 gp120 to attain a functional conformation, and individual N-linked glycans of gp120 are important, but not essential, for replication of HIV-1 in cell culture. n-linked glycans 95-111 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 115-120 8129620-0 1994 Identification of three N-linked glycans in the V4-V5 region of HIV-1 gp 120, dispensable for CD4-binding and fusion activity of gp 120. n-linked glycans 24-40 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 70-76 8129620-0 1994 Identification of three N-linked glycans in the V4-V5 region of HIV-1 gp 120, dispensable for CD4-binding and fusion activity of gp 120. n-linked glycans 24-40 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 129-135 1281869-0 1992 Carbohydrate determinant NeuAc-Gal beta (1-4) of N-linked glycans modulates the antigenic activity of human immunodeficiency virus type 1 glycoprotein gp120. n-linked glycans 49-65 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 151-156 1281869-1 1992 In the present study we investigated to what extent the peripheral carbohydrate structure of N-linked glycans influences the antigenic properties of human immunodeficiency virus type 1 glycoprotein 120 (gp120). n-linked glycans 93-109 Envelope surface glycoprotein gp160, precursor Human immunodeficiency virus 1 203-208