Bjorkman, Pamela

Combined from CaltechAUTHORS

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• Yang, Zhi and Dam, Kim-Marie A., et el. (2022) Antibody Recognition of CD4-Induced Open HIV-1 Env Trimers; Journal of Virology; Vol. 96; No. 24; e0108222; PMCID PMC9769388; 10.1128/jvi.01082-22
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• Dam, Kim-Marie A. and Barnes, Christopher O., et el. (2022) HIV-1 CD4-binding site germline antibody-Env structures inform vaccine design; Nature Communications; Vol. 13; Art. No. 6123; PMCID PMC9576718; 10.1038/s41467-022-33860-2
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• Yang, Zhi and Dam, Kim-Marie A., et el. (2022) Antibody recognition of CD4-induced open HIV-1 Env trimers; 10.1101/2022.07.27.501785
• Fan, Chengcheng and Cohen, Alexander A., et el. (2022) Neutralizing monoclonal antibodies elicited by mosaic RBD nanoparticles bind conserved sarbecovirus epitopes; 10.1101/2022.06.28.497989
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• Bozhanova, Nina G. and Flyak, Andrew I., et el. (2022) Computational identification of HCV neutralizing antibodies with a common HCDR3 disulfide bond motif in the antibody repertoires of infected individuals; Nature Communications; Vol. 13; Art. No. 3178; PMCID PMC9177688; 10.1038/s41467-022-30865-9
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• Dam, Kim-Marie A. and Barnes, Christopher O., et el. (2022) HIV-1 CD4-binding site germline antibody-Env structures inform vaccine design; 10.1101/2022.03.25.485873
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• Yang, Zhi and Dam, Kim-Marie A., et el. (2022) Neutralizing antibodies induced in immunized macaques recognize the CD4-binding site on an occluded-open HIV-1 envelope trimer; Nature Communications; Vol. 13; Art. No. 732; PMCID PMC8826976; 10.1038/s41467-022-28424-3
• Tanaka, Shiho and Olson, C. Anders, et el. (2022) Rapid identification of neutralizing antibodies against SARS-CoV-2 variants by mRNA display; Cell Reports; Vol. 38; No. 6; Art. No. 110348; PMCID PMC8769934; 10.1016/j.celrep.2022.110348
• Weber, Timm and Potthoff, Julian, et el. (2022) Analysis of antibodies from HCV elite neutralizers identifies genetic determinants of broad neutralization; Immunity; Vol. 55; No. 2; 341-354; PMCID PMC10089621; 10.1016/j.immuni.2021.12.003
• Vanshylla, Kanika and Fan, Chengcheng, et el. (2022) Discovery of ultrapotent broadly neutralizing antibodies from SARS-CoV-2 elite neutralizers; Cell Host and Microbe; Vol. 30; No. 1; 69-82; PMCID PMC8683262; 10.1016/j.chom.2021.12.010
• Ogega, Clinton O. and Skinner, Nicole E., et el. (2022) B cell overexpression of FCRL5 and PD-1 is associated with low antibody titers in HCV infection; PLOS Pathogens; Vol. 18; No. 1; Art. No. e1010179; PMCID PMC8769295; 10.1371/journal.ppat.1010179
• Barnes, Christopher and Scheid, Johannes F., et el. (2021) Structural insights into antibody-mediated neutralization of SARS-CoV-2; Glycobiology; Vol. 31; No. 12; 1696-1697; 10.1093/glycob/cwab121
• Escolano, Amelia and Gristick, Harry B., et el. (2021) Sequential immunization of macaques elicits heterologous neutralizing antibodies targeting the V3-glycan patch of HIV-1 Env; Science Translational Medicine; Vol. 13; No. 621; Art. No. abk1533; PMCID PMC8932345; 10.1126/scitranslmed.abk1533
• Brune, Karl D. and Liekniņa, Ilva, et el. (2021) N-Terminal Modification of Gly-His-Tagged Proteins with Azidogluconolactone; ChemBioChem; Vol. 22; No. 22; 3199-3207; 10.1002/cbic.202100381
• Woodward, Denise and Ricks, Ernest, Jr., et el. (2021) The Path of Science in Future Tibetan Buddhist Education; Frontiers in Communication; Vol. 6; Art. No. 731604; 10.3389/fcomm.2021.731604
• Abernathy, Morgan E. and Gristick, Harry B., et el. (2021) Antibody elicited by HIV-1 immunogen vaccination in macaques displaces Env fusion peptide and destroys a neutralizing epitope; npj Vaccines; Vol. 6; Art. No. 126; PMCID PMC8545924; 10.1038/s41541-021-00387-4
• Abernathy, Morgan E. and Dam, Kim-Marie A., et el. (2021) How Antibodies Recognize Pathogenic Viruses: Structural Correlates of Antibody Neutralization of HIV-1, SARS-CoV-2, and Zika; Viruses; Vol. 13; No. 10; Art. No. 2106; PMCID PMC8537525; 10.3390/v13102106
• Jette, Claudia A. and Cohen, Alexander A., et el. (2021) Broad cross-reactivity across sarbecoviruses exhibited by a subset of COVID-19 donor-derived neutralizing antibodies; Cell Reports; Vol. 36; No. 13; Art. No. 109760; PMCID PMC8423902; 10.1016/j.celrep.2021.109760
• Ullah, Irfan and Prévost, Jérémie, et el. (2021) Live imaging of SARS-CoV-2 infection in mice reveals that neutralizing antibodies require Fc function for optimal efficacy; Immunity; Vol. 54; No. 9; 2143-2158; PMCID PMC8372518; 10.1016/j.immuni.2021.08.015
• Muecksch, Frauke and Weisblum, Yiska, et el. (2021) Affinity maturation of SARS-CoV-2 neutralizing antibodies confers potency, breadth, and resilience to viral escape mutations; Immunity; Vol. 54; No. 8; 1853-1868; PMCID PMC8323339; 10.1016/j.immuni.2021.07.008
• West, Anthony P., Jr. and Wertheim, Joel O., et el. (2021) Detection and characterization of the SARS-CoV-2 lineage B.1.526 in New York; Nature Communications; Vol. 12; Art. No. 4886; PMCID PMC8352861; 10.1038/s41467-021-25168-4
• Hensley, Matthew K. and Bain, William G., et el. (2021) Intractable Coronavirus Disease 2019 (COVID-19) and Prolonged Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) Replication in a Chimeric Antigen Receptor-Modified T-Cell Therapy Recipient: A Case Study; Clinical Infectious Diseases; Vol. 73; No. 3; e815-e821; PMCID PMC7929077; 10.1093/cid/ciab072
• Bjorkman, Pamela J. (2021) Neutralizing antibodies against coronaviruses
• Garber, Arkadiy I. and Kupper, Maria, et el. (2021) The Evolution of Interdependence in a Four-Way Mealybug Symbiosis; Genome Biology and Evolution; Vol. 13; No. 8; Art. No. evab123; PMCID PMC8331144; 10.1093/gbe/evab123
• Bjorkman, Pamela (2021) Neutralizing antibodies against coronaviruses; Microscopy and Microanalysis; Vol. 27; No. S1; 1112-1113; 10.1017/s1431927621004177
• Greaney, Allison J. and Starr, Tyler N., et el. (2021) Mapping mutations to the SARS-CoV-2 RBD that escape binding by different classes of antibodies; Nature Communications; Vol. 12; Art. No. 4196; PMCID PMC8263750; 10.1038/s41467-021-24435-8
• Haugh, Kelsey A. and Ladinsky, Mark S., et el. (2021) In vivo imaging of retrovirus infection reveals a role for Siglec-1/CD169 in multiple routes of transmission; eLife; Vol. 10; Art. No. e64179; PMCID PMC8298093; 10.7554/eLife.64179
• Hoffmann, Magnus A. G. and Kieffer, Collin, et el. (2021) In vitro characterization of engineered red blood cells as viral traps against HIV-1 and SARS-CoV-2; Molecular Therapy - Methods and Clinical Development; Vol. 21; 161-170; PMCID PMC7944778; 10.1016/j.omtm.2021.03.003
• Scheid, Johannes F. and Barnes, Christopher O., et el. (2021) B cell genomics behind cross-neutralization of SARS-CoV-2 variants and SARS-CoV; Cell; Vol. 184; No. 12; 3205-3221; PMCID PMC8064835; 10.1016/j.cell.2021.04.032
• Livanos, Alexandra E. and Jha, Divya, et el. (2021) Intestinal Host Response to SARS-CoV-2 Infection and COVID-19 Outcomes in Patients With Gastrointestinal Symptoms; Gastroenterology; Vol. 160; No. 7; 2435-2450; PMCID PMC7931673; 10.1053/j.gastro.2021.02.056
• De Gasparo, Raoul and Pedotti, Mattia, et el. (2021) Bispecific IgG neutralizes SARS-CoV-2 variants and prevents escape in mice; Nature; Vol. 593; No. 7859; 424-428; PMCID PMC8330819; 10.1038/s41586-021-03461-y
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• Agudelo, Marianna and Palus, Martin, et el. (2021) Broad and potent neutralizing human antibodies to tick-borne flaviviruses protect mice from disease; Journal of Experimental Medicine; Vol. 218; No. 5; Art. No. e20210236; PMCID PMC8040517; 10.1084/jem.20210236
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• Jette, Claudia A. and Barnes, Christopher O., et el. (2021) Cryo-EM structures of HIV-1 trimer bound to CD4-mimetics BNM-III-170 and M48U1 adopt a CD4-bound open conformation; Nature Communications; Vol. 12; Art. No. 1950; PMCID PMC8007822; 10.1038/s41467-021-21816-x
• Gaebler, Christian and Wang, Zijun, et el. (2021) Evolution of antibody immunity to SARS-CoV-2; Nature; Vol. 591; No. 7851; 639-644; PMCID PMC8221082; 10.1038/s41586-021-03207-w
• Muecksch, Frauke and Weisblum, Yiska, et el. (2021) Development of potency, breadth and resilience to viral escape mutations in SARS-CoV-2 neutralizing antibodies; PMCID PMC7987023; 10.1101/2021.03.07.434227
• Cohen, Alexander A. and Yang, Zhi, et el. (2021) Construction, characterization, and immunization of nanoparticles that display a diverse array of influenza HA trimers; PLoS ONE; Vol. 16; No. 3; Art. No. e0247963; PMCID PMC7932532; 10.1371/journal.pone.0247963
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• Cohen, Alexander A. and Gnanapragasam, Priyanthi N. P., et el. (2021) Mosaic nanoparticles elicit cross-reactive immune responses to zoonotic coronaviruses in mice; Science; Vol. 371; No. 6530; 735-741; PMCID PMC7928838; 10.1126/science.abf6840
• Esswein, Shannon R. and Bjorkman, Pamela J. (2021) Structural Basis for Germline Antibody Binding to Zika Virus Envelope Domain III; Biophysical Journal; Vol. 120; No. 3; 276A-277A; 10.1016/j.bpj.2020.11.1760
• Bárcena, Montserrat and Barnes, Christopher O., et el. (2021) Structural biology in the fight against COVID-19; Nature Structural & Molecular Biology; Vol. 28; No. 1; 2-7; 10.1038/s41594-020-00544-8
• Linsky, Thomas W. and Vergara, Renan, et el. (2020) De novo design of potent and resilient hACE2 decoys to neutralize SARS-CoV-2; Science; Vol. 370; No. 6521; 1208-1214; PMCID PMC7920261; 10.1126/science.abe0075
• Wang, Zijun and Barnes, Christopher O., et el. (2020) A broadly neutralizing macaque monoclonal antibody against the HIV-1 V3-Glycan patch; eLife; Vol. 9; Art. No. e61991; PMCID PMC7577740; 10.7554/eLife.61991
• Barnes, Christopher O. and Jette, Claudia A., et el. (2020) Structural classification of neutralizing antibodies against the SARS-CoV-2 spike receptor-binding domain suggests vaccine and therapeutic strategies; 10.1101/2020.08.30.273920
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• Hoffmann, Magnus A. G. and Bar-On, Yotam, et el. (2020) Nanoparticles presenting clusters of CD4 expose a universal vulnerability of HIV-1 by mimicking target cells; Proceedings of the National Academy of Sciences of the United States of America; Vol. 117; No. 31; 18719-18728; PMCID PMC7414181; 10.1073/pnas.2010320117
• Ladinsky, Mark S. and Gnanapragasam, Priyanthi N. P., et el. (2020) Electron tomography visualization of HIV-1 fusion with target cells using fusion inhibitors to trap the pre-hairpin intermediate; eLife; Vol. 9; Art. No. e58411; PMCID PMC7394545; 10.7554/eLife.58411
• Esswein, Shannon R. and Gristick, Harry B., et el. (2020) Structural basis for Zika envelope domain III recognition by a germline version of a recurrent neutralizing antibody; Proceedings of the National Academy of Sciences of the United States of America; Vol. 117; No. 18; 9865-9875; PMCID PMC7211955; 10.1073/pnas.1919269117
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• Van Rompay, Koen K. A. and Coffey, Lark L., et el. (2020) A Combination of Two Human Monoclonal Antibodies Limits Fetal Damage by Zika Virus in Macaques; Proceedings of the National Academy of Sciences of the United States of America; Vol. 117; No. 14; 7981-7989; PMCID PMC7149495; 10.1073/pnas.2000414117
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• Bjorkman, Pamela J. (2020) Can we use structural knowledge to design a protective vaccine against HIV-1?; HLA; Vol. 95; No. 2; 95-103; 10.1111/tan.13759
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• Flyak, Andrew I. and Ruiz, Stormy, et el. (2018) HCV Broadly Neutralizing Antibodies Use a CDRH3 Disulfide Motif to Recognize an E2 Glycoprotein Site that Can Be Targeted for Vaccine Design; Cell Host & Microbe; Vol. 24; No. 5; 703-716; PMCID PMC6258177; 10.1016/j.chom.2018.10.009
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• Wang, Haoqing and Barnes, Christopher O., et el. (2018) Partially Open HIV-1 Envelope Structures Exhibit Conformational Changes Relevant for Coreceptor Binding and Fusion; Cell Host & Microbe; Vol. 24; No. 4; 579-592; PMCID PMC6185872; 10.1016/j.chom.2018.09.003
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