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Your search keyword '"Bollini, Sagarika"' showing total 4 results
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4 results on '"Bollini, Sagarika"'

1. Efficacy and safety of a single dose of casirivimab and imdevimab for the prevention of COVID-19 over an 8-month period: a randomised, double-blind, placebo-controlled trial

Author

Chani, Achint, Adepoju, Adebiyi, Mahmood, Adnan, Mortagy, Aisha, Dupljak, Ajla, Baum, Alina, Brown, Alison, Froment, Amy, Hooper, Andrea, Margiotta, Andrea, Bombardier, Andrew, Islam, Anita, Smith, Anne, Dhillon, Arvinder, McMillian, Audra, Breazna, Aurora, Aslam, Ayesha, Carpentino, Barabara, Kowal, Bari, Siliverstein, Barry, Horel, Benjamin, Zhu, Bo, Musser, Bret, Bush, Brian, Head, Brian, Snow, Brian, Zhu, Bryan, Debray, Camille, Phillips, Careta, Simiele, Carmella, Lee, Carol, Nienstedt, Carolyn, Trbovic, Caryn, Chan, Casey (Kuo-Chen), Elliott, Catherine, Fish, Chad, Ni, Charlie, Polidori, Christa, Enciso, Christine, Caira, Christopher, Powell, Christopher, Kyratsous, Christos A., Baum, Cliff, McDonald, Colin, Leigh, Cynthia, Pan, Cynthia, Wolken, Dana, Manganello, Danielle, Liu, David, Stein, David, Weinreich, David M., Hassan, Dawlat, Gulabani, Daya, Fix, Deborah, Leonard, Deborah, Sarda, Deepshree, Bonhomme, Denise, Kennedy, Denise, Darcy, Devin, Barron, Dhanalakshmi, Hughes, Diana, Rofail, Diana, Kaur, Dipinder, Ramesh, Divya, Bianco, Dona, Cohen, Donna, Forleo-Neto, Eduardo, Jean-Baptiste, Edward, Bukhari, Ehsan, Doyle, Eileen, Bucknam, Elizabeth, Labriola-Tomkins, Emily, Nanna, Emily, Huffman O'Keefe, Esther, Gasparino, Evelyn, Fung, Evonne, Isa, Flonza, To, Fung-Yee, Herman, Gary, Yancopoulos, George D., Bellingham, Georgia, Sumner, Giane, Moggan, Grainne, Power, Grainne, Zeng, Haixia, Mariveles, Hazel, Gonzalez, Heath, Kang, Helen, Noor, Hibo, Minns, Ian, Heirman, Ingeborg, Peszek, Izabella, Donohue, James, Rusconi, Jamie, Austin, Janice, Parrino, Janie, Yo, Jeannie, McDonnell, Jenna, Hamilton, Jennifer D., Boarder, Jessica, Wei, Jianguo, Yu, Jingchun, Malia, Joanne, Tucciarone, Joanne, Tyler-Gale, Jodie, Davis, John D., Strein, John, Cohen, Jonathan, Meyer, Jonathan, Ursino, Jordan, Im, Joseph, Tramaglini, Joseph, Wolken, Joseph, Potter, Kaitlyn, Scacalossi, Kaitlyn, Naidu, Kamala, Browning, Karen, Rutkowski, Karen, Yau, Karen, Woloshin, Katherine, Lewis-Amezcua, Kelly, Turner, Kenneth, Dornheim, Kimberly, Chiu, Kit, Mohan, Kosalai, McGuire, Kristina, Macci, Kristy, Ringleben, Kurt, Mohammadi, Kusha, Foster, Kyle, Knighton, Latora, Lipsich, Leah, Darling, Lindsay, Boersma, Lisa, Cowen, Lisa, Hersh, Lisa, Jackson, Lisa, Purcell, Lisa, Sherpinsky, Lisa, Lai, Livia, Faria, Lori, Geissler, Lori, Boppert, Louise, Fiske, Lyra, Dickens, Marc, Mancini, Marco, Leigh, Maria C., O'Brien, Meagan P., Batchelder, Michael, Klinger, Michael, Partridge, Michael, Tarabocchia, Michel, Wong, Michelle, Rodriguez, Mivianisse, Albizem, Moetaz, O'Byrne, Muriel, Braunstein, Ned, Sarkar, Neena, Stahl, Neil, Deitz, Nicole, Memblatt, Nicole, Shah, Nirav, Kumar, Nitin, Herrera, Olga, Adedoyin, Oluchi, Yellin, Ori, Snodgrass, Pamela, Floody, Patrick, D'Ambrosio, Paul, Gao, Paul (Xiaobang), Hou, Peijie, Hearld, Philippa, Li, Qin, Kitchenoff, Rachel, Ali, Rakiyya, Iyer, Ramya, Chava, Ravikanth, Alaj, Rinol, Pedraza, Rita, Hamlin, Robert, Hosain, Romana, Gorawala, Ruchin, White, Ryan, Yu, Ryan, Fogarty, Rylee, Dass, S. Balachandra, Bollini, Sagarika, Ganguly, Samit, DeCicco, Sandra, Patel, Sanket, Cassimaty, Sarah, Somersan-Karakaya, Selin, McCarthy, Shane, Henkel, Sharon, Ali, Shazia, Geila Shapiro, Shelley, Kim, Somang, Nossoughi, Soraya, Bisulco, Stephanie, Elkin, Steven, Long, Steven, Sivapalasingam, Sumathi, Irvin, Susan, Wilt, Susan, Min, Tami, Constant, Tatiana, Devins, Theresa, DiCioccio, Thomas, Norton, Thomas, Bernardo, Travis, Chuang, Tzu-Chien, Wei, Victor (Jianguo), Nuce, Vinh, Battini, Vishnu, Caldwell, Wilson, Gao, Xiaobang, Chen, Xin, Tian, Yanmei, Khan, Yasmin, Zhao, Yuming, Kim, Yunji, Dye, Bonnie, Hurt, Christopher B., Burwen, Dale R., Barouch, Dan H., Burns, David, Brown, Elizabeth, Bar, Katharine J., Marovich, Mary, Clement, Meredith, Cohen, Myron S., Sista, Nirupama, Barnabas, Ruanne V., Zwerski, Sheryl, Herman, Gary A, O'Brien, Meagan P, Chan, Kuo-Chen, Bar, Katharine J, Barnabas, Ruanne V, Barouch, Dan H, Cohen, Myron S, Hurt, Christopher B, Burwen, Dale R, Marovich, Mary A, Musser, Bret J, Davis, John D, Turner, Kenneth C, Hooper, Andrea T, Hamilton, Jennifer D, Subramaniam, Danise, Kyratsous, Christos A, DiCioccio, A Thomas, Yancopoulos, George D, and Weinreich, David M

Published
2022
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2. The discovery and preclinical evaluation of BMS-707035, a potent HIV-1 integrase strand transfer inhibitor.

Author

Naidu, B. Narasimhulu, Walker, Michael A., Sorenson, Margaret E., Ueda, Yasutsugu, Matiskella, John D., Connolly, Timothy P., Dicker, Ira B., Lin, Zeyu, Bollini, Sagarika, Terry, Brian J., Higley, Helen, Zheng, Ming, Parker, Dawn D., Wu, Dedong, Adams, Stephen, Krystal, Mark R., and Meanwell, Nicholas A.

Subjects
*INTEGRASES, *HIV infections, *THERAPEUTICS, *STRUCTURE-activity relationship in pharmacology, *SINGLE crystals, *X-rays, *ANTIVIRAL agents
Abstract

BMS-707035 is an HIV-1 integrase strand transfer inhibitor (INSTI) discovered by systematic optimization of N-methylpyrimidinone carboxamides guided by structure-activity relationships (SARs) and the single crystal X-ray structure of compound 10 . It was rationalized that the unexpectedly advantageous profiles of N-methylpyrimidinone carboxamides with a saturated C2-substitutent may be due, in part, to the geometric relationship between the C2-substituent and the pyrimidinone core. The single crystal X-ray structure of 10 provided support for this reasoning and guided the design of a spirocyclic series 12 which led to discovery of the morpholino-fused pyrimidinone series 13 . Several carboxamides derived from this bicyclic scaffold displayed improved antiviral activity and pharmacokinetic profiles when compared with corresponding spirocyclic analogs. Based on the excellent antiviral activity, preclinical profiles and acceptable in vitro and in vivo toxicity profiles, 13a (BMS-707035) was selected for advancement into phase I clinical trials. [ABSTRACT FROM AUTHOR]

Published
2018
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3. Synthesis and evaluation of C2-carbon-linked heterocyclic-5-hydroxy-6-oxo-dihydropyrimidine-4-carboxamides as HIV-1 integrase inhibitors.

Author

Naidu, B. Narasimhulu, Sorenson, Margaret E., Patel, Manoj, Ueda, Yasutsugu, Banville, Jacques, Beaulieu, Francis, Bollini, Sagarika, Dicker, Ira B., Higley, Helen, Lin, Zeyu, Pajor, Lori, Parker, Dawn D., Terry, Brian J., Zheng, Ming, Martel, Alain, Meanwell, Nicholas A., Krystal, Mark, and Walker, Michael A.

Subjects
*HIV integrase inhibitors, *PYRIMIDINES, *HETEROCYCLIC compounds, *CARBOXAMIDES, *CHEMICAL synthesis, *CATALYSIS, *PHARMACEUTICAL chemistry
Abstract

Integration of viral DNA into the host cell genome is an obligatory process for successful replication of HIV-1. Integrase catalyzes the insertion of viral DNA into the target DNA and is a validated target for drug discovery. Herein, we report the synthesis, antiviral activity and pharmacokinetic profiles of several C2-carbon-linked heterocyclic pyrimidinone-4-carboxamides that inhibit the strand transfer step of the integration process. [ABSTRACT FROM AUTHOR]

Published
2015
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4. Biochemical Analysis of HIV-1 Integrase Variants Resistant to Strand Transfer Inhibitors.

Author

Dicker, Ira B., Terry, Brian, Zeyu Lin, Zhufang Li, Bollini, Sagarika, Samanta, Himadri K., GaIi, Volodymyr, WaIker, Michael A., and Krystal, Mark R.

Subjects
*GENETIC mutation, *MICROORGANISMS, *MICROBIOLOGY, *ENZYMOLOGY, *BIOCHEMISTRY, *ANALYTICAL chemistry
Abstract

In this study, eight different HIV-1 integrase proteins containing mutations observed in strand transfer inhibitor-resistant viruses were expressed, purified, and used for detailed enzymatic analyses. All the variants examined were impaired for strand transfer activity compared with the wild type enzyme, with relative catalytic efficiencies (kp/Km) ranging from 0.6 to 50% of wild type. The origin of the reduced strand transfer efficiencies of the variant enzymes was predominantly because of poorer catalytic turnover (kr) values. However, smaller second-order effects were caused by up to 4-fold increases in Km values for target DNA utilization in some of the variants. All the variants were less efficient than the wild type enzyme in assembling on the viral long terminal repeat, as each variant required more protein than wild type to attain maximal activity. In addition, the variant integrases displayed up to 8-fold reductions in their catalytic efficiencies for 3′-processing. The Q148R variant was the most defective enzyme. The molecular basis for resistance of these enzymes was shown to be due to lower affinity binding of the strand transfer inhibitor to the integrase complex, a consequence of faster dissociation rates. In the case of the Q148R variant, the origin of reduced compound affinity lies in alterations to the active site that reduce the binding of a catalytically essential magnesium ion. Finally, except for T661, variant viruses harboring the resistance-inducing substitutions were defective for viral integration. [ABSTRACT FROM AUTHOR]

Published
2008
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