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3981por Ge, Hu, Liu, Ge, Xiang, Yang-Fei, Wang, Yu, Guo, Chao-Wan, Chen, Nan-Hao, Zhang, Ying-Jun, Wang, Yi-Fei, Kitazato, Kaio, Xu, Jun“…We found that (1) star-shaped pGG analogs exhibit HA-inhibition activity by interacting with the conserved structural elements of the receptor binding domain (RBD); (2) HA inhibition depends on the number of galloyl substituents in a pGG analog; the best number is four; and when PGG binds with two HA trimers at their conserved receptor binding domains (loop 130, loop 220, and 190-α-helix), PGG acts as a molecular glue by aggregating viral particles so as to prevent viral entry into host cells (this was revealed via an in silico simulation on the binding of penta-galloyl-glucose (PGG) with HA). pGGs are also effective on a broad-spectrum influenza A subtypes (including H1, H3, H5, H7); this suggests that pGG analogs can be applied to most influenza A subtypes as a prophylactic against influenza viral infections.…”
Publicado 2014
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3982“…ZnO NP loaded with Torula Yeast RNA (TYRNA)(640 nm), polyinosinic: polycytidylic acid (pIC)(680 nm), or splice switching oligonucleotide (SSO)(650 nm) each revealed a shift in emission. Ras-Binding domain (RBD) at three concentrations (25, 37.5, 50 μg/mL) showed that fluorescent intensity was inversely related to the concentration of protein loaded. …”
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3983por Gui, Miao, Song, Wenfei, Zhou, Haixia, Xu, Jingwei, Chen, Silian, Xiang, Ye, Wang, Xinquan“…Conformations 2-4 determined at 7.3, 5.7 and 6.8 Å resolutions are all asymmetric, in which one RBD rotates away from the “down” position by different angles to an “up” position. …”
Publicado 2017
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3984“…In this study we identified the receptor-binding domain (RBD) of the spike of the prototype IBV strain M41. …”
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3985por Yuan, Meng, Wu, Nicholas C., Zhu, Xueyong, Lee, Chang-Chun D., So, Ray T. Y., Lv, Huibin, Mok, Chris K. P., Wilson, Ian A.“…We therefore determined the crystal structure of CR3022, a neutralizing antibody previously isolated from a convalescent SARS patient, in complex with the receptor binding domain (RBD) of the SARS-CoV-2 spike (S) protein at 3.1-angstrom resolution. …”
Publicado 2020
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3986por Wrapp, Daniel, Wang, Nianshuang, Corbett, Kizzmekia S., Goldsmith, Jory A., Hsieh, Ching-Lin, Abiona, Olubukola, Graham, Barney S., McLellan, Jason S.“…Additionally, we tested several published SARS-CoV RBD-specific monoclonal antibodies and found that they do not have appreciable binding to 2019-nCoV S, suggesting that antibody cross-reactivity may be limited between the two RBDs. …”
Publicado 2020
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3987por Sheikh, Javaid Ahmad, Singh, Jasdeep, Singh, Hina, Jamal, Salma, Khubaib, Mohd., Kohli, Sunil, Dobrindt, Ulrich, Rahman, Syed Asad, Ehtesham, Nasreen Zafar, Hasnain, Seyed Ehtesham“…We could identify mutational hotspots which appear to be major drivers of diversity among strains, with RBD of spike protein emerging as the key region involved in interaction with ACE2 and consequently a major determinant of infection outcome. …”
Publicado 2020
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3988“…SARS-CoV-2-specific antibodies targeting the spike receptor binding domain (RBD) may lead to antibody dependent enhancement (ADE) of infection, possibly hampering the field of vaccine development. …”
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3989por Zhang, Ziyang, Gao, Rong, Hu, Qi, Peacock, Hayden, Peacock, D. Matthew, Dai, Shizhong, Shokat, Kevan M., Suga, Hiroaki“…Replacing this threonine with non-natural amino acids afforded peptides with improved potency at inhibiting the interaction between Raf1-RBD and K-Ras(G12D) but not wildtype K-Ras. The union of G12D over wildtype selectivity and GTP state/GDP state selectivity is particularly desirable, considering that oncogenic K-Ras(G12D) exists predominantly in the GTP state in cancer cells, and wildtype K-Ras signaling is important for the maintenance of healthy cells.…”
Publicado 2020
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3990por Pan, Boyu, Fang, Senbiao, Zhang, Ju, Pan, Ya, Liu, Han, Wang, Yun, Li, Min, Liu, Liren“…Notably, quercetin could also bind to the RBD domain of S-protein, suggesting not only a receptor blocking, but also a virus neutralizing effect of quercetin on SARS-CoV-2. …”
Publicado 2020
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3991por Andreano, Emanuele, Piccini, Giulia, Licastro, Danilo, Casalino, Lorenzo, Johnson, Nicole V., Paciello, Ida, Dal Monego, Simeone, Pantano, Elisa, Manganaro, Noemi, Manenti, Alessandro, Manna, Rachele, Casa, Elisa, Hyseni, Inesa, Benincasa, Linda, Montomoli, Emanuele, Amaro, Rommie E., McLellan, Jason S., Rappuoli, Rino“…At day 73, an E484K substitution in the receptor-binding domain (RBD) occurred, followed at day 80 by an insertion in the NTD N5 loop containing a new glycan sequon, which generated a variant completely resistant to plasma neutralization. …”
Publicado 2020
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3992“…Studies showed that this mutation results in an open conformation of the S glycoprotein receptor-binding domain (RBD), and increased angiotensin 1-converting enzyme 2 (ACE2) binding and fusion, which result in an increase in SARS-CoV-2 transmissibility and infectivity. …”
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3993“…Recombinant SARS-CoV-2 spike protein (RBD) domain and ACE2 of RPTEC/SerC cell-binding assays confirmed that SARS-Cov-2 can bind to ACE2 on the surface of these cells. …”
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3994por Lenza, Maria Pia, Oyenarte, Iker, Diercks, Tammo, Quintana, Jon Imanol, Gimeno, Ana, Coelho, Helena, Diniz, Ana, Peccati, Francesca, Delgado, Sandra, Bosch, Alexandre, Valle, Mikel, Millet, Oscar, Abrescia, Nicola G. A., Palazón, Asís, Marcelo, Filipa, Jiménez‐Osés, Gonzalo, Jiménez‐Barbero, Jesús, Ardá, Ana, Ereño‐Orbea, June“…The interaction of the RBD (13)C‐labelled glycans with different human lectins, which are expressed in different organs and tissues that may be affected during the infection process, has also been evaluated by NMR. …”
Publicado 2020
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3995“…Adaptive molecular evolution was observed in SARS-CoV-2 displayed by positive selection pressure at N-terminal domain (NTD; codons 41, 163, 174 and 218), Receptor binding domain (RBD; codons 378 and 404) and S1/S2 Cleavage site (codon 690). …”
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3996“…Although it is not obvious from the primary sequence alignment of ACE1 and ACE2, comparison of X-ray crystallographic structures show striking similarities in the regions of the peptidase domains (PD) of these proteins, which is known (for ACE2) to interact with the receptor binding domain (RBD) of the SARS-CoV-2 spike protein. Critical amino acids in ACE2 that mediate interaction with the viral spike protein are present and organized in the same order in the PD of ACE1. …”
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3997“…Our results suggest that the spike homotrimer undergoes drastic changes in the topology of the hydrogen bonding interactions and important changes on the secondary structure of the receptor binding domain (RBD), while electrostatic interactions (i.e. salt bridges) are mainly preserved. …”
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3998por Liu, Xuelan, Chang, Xinyue, Rothen, Dominik, Derveni, Mariliza, Krenger, Pascal, Roongta, Salony, Wright, Edward, Vogel, Monique, Tars, Kaspars, Mohsen, Mona O., Bachmann, Martin F.“…Importantly, immunized mice were able to generate high levels of IgG antibodies recognizing eukaryotically expressed receptor binding domain (RBD) as well as spike protein of SARS-CoV-2. Furthermore, induced antibodies were able to neutralize SARS-CoV-2/ABS/NL20. …”
Publicado 2021
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3999por Adeniji, Opeyemi S., Giron, Leila B., Purwar, Mansi, Zilberstein, Netanel F., Kulkarni, Abhijeet J., Shaikh, Maliha W., Balk, Robert A., Moy, James N., Forsyth, Christopher B., Liu, Qin, Dweep, Harsh, Kossenkov, Andrew, Weiner, David B., Keshavarzian, Ali, Landay, Alan, Abdel-Mohsen, Mohamed“…We found that anti-S1 and anti-RBD antibodies from hospitalized COVID-19 patients elicited higher ADCD but lower ADCP compared to antibodies from nonhospitalized COVID-19 patients. …”
Publicado 2021
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4000por Taylor, Sean C., Hurst, Beth, Charlton, Carmen L., Bailey, Ashley, Kanji, Jamil N., McCarthy, Mary K., Morrison, Thomas E., Huey, Leah, Annen, Kyle, DomBourian, Melkon G., Knight, Vijaya“…A new assay technology measuring the interaction of the purified SARS-CoV-2 spike protein receptor binding domain (RBD) with the extracellular domain of the human angiotensin-converting enzyme 2 (hACE2) receptor detects these important antibodies. …”
Publicado 2021
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