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202 results on '"Babcock, Gregory"'

1. A humanized IL-2 mutein expands Tregs and prolongs transplant survival in preclinical models

Author

Efe, Orhan, Gassen, Rodrigo B., Morena, Leela, Ganchiku, Yoshikazu, Jurdi, Ayman Al, Lape, Isadora T., Ventura- Aguiar, Pedro, LeGuern, Christian, Madsen, Joren C., Shriver, Zachary, Babcock, Gregory J., Borges, Thiago J., and Riella, Leonardo V.

Subjects
Prevention, Complications and side effects, Physiological aspects, Models, Research, Health aspects, Immunosuppression -- Research, Immunologic research, Organ transplantation -- Models -- Complications and side effects, Interleukin-2 -- Health aspects -- Physiological aspects, Graft rejection -- Models -- Prevention, Transplantation of organs, tissues, etc. -- Models -- Complications and side effects, Immunological research
Abstract

Introduction Immunosuppression is crucial in solid organ transplantation to prevent allograft rejection. Current approaches involve combinations of drugs targeting different immune components. These include calcineurin inhibitors (e.g., tacrolimus), antiproliferative agents [...], Long-term organ transplant survival remains suboptimal, and life-long immunosuppression predisposes transplant recipients to an increased risk of infection, malignancy, and kidney toxicity. Promoting the regulatory arm of the immune system by expanding Tregs may allow immunosuppression minimization and improve long-term graft outcomes. While low-dose IL-2 treatment can expand Tregs, it has a short half-life and off-target expansion of NK and effector T cells, limiting its clinical applicability. Here, we designed a humanized mutein IL-2 with high Treg selectivity and a prolonged half-life due to the fusion of an Fc domain, which we termed mIL-2. We showed selective and sustainable Treg expansion by mIL-2 in 2 murine models of skin transplantation. This expansion led to donor-specific tolerance through robust increases in polyclonal and antigen-specific Tregs, along with enhanced Treg-suppressive function. We also showed that Treg expansion by mIL-2 could overcome the failure of calcineurin inhibitors or costimulation blockade to prolong the survival of major-mismatched skin grafts. Validating its translational potential, mIL-2 induced a selective and sustainable in vivo Treg expansion in cynomolgus monkeys and showed selectivity for human Tregs in vitro and in a humanized mouse model. This work demonstrated that mIL-2 can enhance immune regulation and promote long-term allograft survival, potentially minimizing immunosuppression.

Published
2024
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3. CD209L (L-SIGN) Is a Receptor for Severe Acute Respiratory Syndrome Coronavirus

Author

Jeffers, Scott A., Tusell, Sonia M., Gillim-Ross, Laura, Hemmila, Erin M., Achenbach, Jenna E., Babcock, Gregory J., Thomas,, William D., Thackray, Larissa B., Young, Mark D., Mason, Robert J., Ambrosino, Donna M., Wentworth, David E., DeMartini, James C., Holmes, Kathryn V., and Palese, Peter

Published
2004

4. VIS832, a novel CD138-targeting monoclonal antibody, potently induces killing of human multiple myeloma and further synergizes with IMiDs or bortezomib in vitro and in vivo

Author

Yu, Tengteng, Chaganty, Bharat, Lin, Liang, Xing, Lijie, Ramakrishnan, Boopathy, Wen, Kenneth, Hsieh, Phillip A., Wollacott, Andrew, Viswanathan, Karthik, Adari, Hedy, Cho, Shih-Feng, Li, Yuyin, Chen, Hailin, Yang, Wenjuan, Xu, Yan, An, Gang, Qiu, Lugui, Munshi, Nikhil, Babcock, Gregory, Shriver, Zachary, Myette, James R., Anderson, Kenneth C., and Tai, Yu-Tzu

Published
2020
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8. Structure-Guided Design of an Anti-dengue Antibody Directed to a Non-immunodominant Epitope

Author

Robinson, Luke N., Tharakaraman, Kannan, Rowley, Kirk J., Costa, Vivian V., Chan, Kuan Rong, Wong, Yee Hwa, Ong, Li Ching, Tan, Hwee Cheng, Koch, Tyree, Cain, David, Kirloskar, Rama, Viswanathan, Karthik, Liew, Chong Wai, Tissire, Hamid, Ramakrishnan, Boopathy, Myette, James R., Babcock, Gregory J., Sasisekharan, V., Alonso, Sylvie, Chen, Jianzhu, Lescar, Julien, Shriver, Zachary, Ooi, Eng Eong, and Sasisekharan, Ram

Published
2015
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11. Development of an antibody fused with an antimicrobial peptide targetingPseudomonas aeruginosa:a new approach to prevent and treat bacterial infections

Author

Johnson, Kenneth, primary, Delaney, James C., additional, Guillard, Thomas, additional, Reffuveille, Fanny, additional, Varin-Simon, Jennifer, additional, Li, Kai, additional, Wollacott, Andrew, additional, Frapy, Eric, additional, Mong, Surin, additional, Tissire, Hamid, additional, Viswanathan, Karthik, additional, Touti, Faycal, additional, Babcock, Gregory J., additional, Shriver, Zachary, additional, Pentelute, Bradley L., additional, Plante, Obadiah, additional, and Skurnik, David, additional

Published
2022
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12. Development of an antibody fused with an antimicrobial peptide targeting Pseudomonas aeruginosa: A new approach to prevent and treat bacterial infections.

Author

Johnson, Kenneth, Delaney, James C., Guillard, Thomas, Reffuveille, Fany, Varin-Simon, Jennifer, Li, Kai, Wollacott, Andrew, Frapy, Eric, Mong, Surin, Tissire, Hamid, Viswanathan, Karthik, Touti, Faycal, Babcock, Gregory J., Shriver, Zachary, Pentelute, Bradley L., Plante, Obadiah, and Skurnik, David

Subjects
ANTIMICROBIAL peptides, BACTERIAL diseases, PSEUDOMONAS aeruginosa, GRAM-negative bacterial diseases, PATHOGENIC microorganisms, CATHELICIDINS, MONOCLONAL antibodies
Abstract

The increase in emerging drug resistant Gram-negative bacterial infections is a global concern. In addition, there is growing recognition that compromising the microbiota through the use of broad-spectrum antibiotics can impact long term patient outcomes. Therefore, there is the need to develop new bactericidal strategies to combat Gram-negative infections that would address these specific issues. In this study, we report and characterize one such approach, an antibody-drug conjugate (ADC) that combines (i) targeting the surface of a specific pathogenic organism through a monoclonal antibody with (ii) the high killing activity of an antimicrobial peptide. We focused on a major pathogenic Gram-negative bacterium associated with antibacterial resistance: Pseudomonas aeruginosa. To target this organism, we designed an ADC by fusing an antimicrobial peptide to the C-terminal end of the VH and/or VL-chain of a monoclonal antibody, VSX, that targets the core of P. aeruginosa lipopolysaccharide. This ADC demonstrates appropriately minimal levels of toxicity against mammalian cells, rapidly kills P. aeruginosa strains, and protects mice from P. aeruginosa lung infection when administered therapeutically. Furthermore, we found that the ADC was synergistic with several classes of antibiotics. This approach described in this study might result in a broadly useful strategy for targeting specific pathogenic microorganisms without further augmenting antibiotic resistance. Author summary: The increasing incidence of emerging drug resistant bacterial infections is a worldwide public health issue. Infections caused by antibiotic-resistant Gram-negative pathogens are particularly concerning. In addition, there is now growing recognition that disruption of the microbiota through the use of broad-spectrum antibiotics can have detrimental effects on long-term patient outcomes. Therefore, there is a need to develop new bactericidal strategies to combat Gram-negative infections while preserving the microbiota and avoiding the enhancement of antibiotic resistance. Here, we report on and characterize one such approach by using a specific monoclonal antibody associated with the potent killing activity of antimicrobial peptides in the form of an antibody-drug conjugate (ADC). The selected pathogenic bacterium was Pseudomonas aeruginosa, which presents numerous markers of both innate and acquired antibiotic resistance. The ADC lacked significant cytotoxicity against mammalian cells and was shown to be effective both in vitro and in vivo against P. aeruginosa. [ABSTRACT FROM AUTHOR]

Published
2023
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15. Development and Characterization of a Severe Acute Respiratory Syndrome-Associated CoronavirusNeutralizing Human Monoclonal Antibody That Provides Effective Immunoprophylaxis in Mice [with Discussion]

Author

Greenough, Thomas C., Babcock, Gregory J., Roberts, Anjeanette, Hernandez, Hector J., Thomas, William D., Coccia, Jennifer A., Graziano, Robert F., Srinivasan, Mohan, Lowy, Israel, Finberg, Robert W., Subbarao, Kanta, Vogel, Leatrice, Somasundaran, Mohan, Luzuriaga, Katherine, Sullivan, John L., and Ambrosino, Donna M.

Published
2005

20. Beta-turn Phe in HIV-1 Env binding site of CD4 and CD4 mimetic miniprotein enhances env binding affinity but is not required for activation of Co-receptor/17b site

Author

Dowd, Cynthia S., Leavitt, Stephanie, Babcock, Gregory, Godillot, Alexis P., Ryk, Don Van, Canziani, Gabriela A., Sodroski, Joseph, Freire, Ernesto, and Chaiken, Irwin M.

Subjects
HIV (Viruses) -- Receptors, Binding sites (Biochemistry) -- Analysis, Viral proteins -- Analysis, Conformational analysis -- Research, Biological sciences, Chemistry
Abstract

Research indicates that the CD4 residue Phe43 maintains the high affinity of gp120 ligands but is not needed for initiating the conformational isomerization in gp120, leading to exposure of the binding sites for 17b antibody and CCR5 receptor.

Published
2002

21. A Novel CD138-Targeting Monoclonal Antibody Induces Potent Myeloma Killing and Further Synergizes with IMiDs or Bortezomib in in Vitro and In Vivo Preclinical Models of Human Multiple Myeloma

Author

Yu, Tengteng, primary, Chaganty, Bharat, additional, Lin, Liang, additional, Xing, Lijie, additional, Ramakrishnan, Boopathy, additional, Wen, Kenneth, additional, Hsieh, Phillip A, additional, Wollacott, Andrew, additional, Viswanathan, Karthik, additional, Adari, Hedy, additional, Cho, Shih-Feng, additional, Li, Yuyin, additional, Yang, Wenjuan, additional, Chen, Hailin, additional, Xu, Yan, additional, An, Gang, additional, Qiu, Lugui, additional, Munshi, Nikhil C., additional, Babcock, Gregory, additional, Shriver, Zach, additional, Myette, James, additional, Anderson, Kenneth, additional, and Tai, Yu-Tzu, additional

Published
2020
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22. Monoclonal antibodies to SARS-associated coronavirus (SARS-CoV): Identification of neutralizing and antibodies reactive to S, N, M and E viral proteins

Author

Tripp, Ralph A., Haynes, Lia M., Moore, Deborah, Anderson, Barbara, Tamin, Azaibi, Harcourt, Brian H., Jones, Les P., Yilla, Mamadi, Babcock, Gregory J., Greenough, Thomas, Ambrosino, Donna M., Alvarez, Rene, Callaway, Justin, Cavitt, Sheana, Kamrud, Kurt, Alterson, Harold, Smith, Jonathan, Harcourt, Jennifer L., Miao, Congrong, Razdan, Raj, Comer, James A., Rollin, Pierre E., Ksiazek, Thomas G., Sanchez, Anthony, Rota, Paul A., Bellini, William J., and Anderson, Larry J.

Published
2005
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24. Development and characterization of a severe acute respiratory syndrome-associated coronavirus-neutralizing human monoclonal antibody that provides effective immunoprophylaxis in mice

Author

Greenough, Thomas C., Babcock, Gregory J., Roberts, Anjeanette, Hernandez, Hector J., Thomas, William D., Jr., Coccia, Jennifer A., Graziano, Robert F., Srinivasan, Mohan, Lowy, Israel, Finberg, Robert W., Subbarao, Kanta, Vogel, Leatrice, Somasundaran, Mohan, Luzuriaga, Katherine, Sullivan, John Lawrence, and Ambrosino, Donna M.

Subjects
Severe acute respiratory syndrome -- Prevention, Monoclonal antibodies -- Health aspects, Monoclonal antibodies -- Physiological aspects, Coronaviruses -- Care and treatment, Mice as laboratory animals, Health
Published
2005

37. A Structural and Mathematical Modeling Analysis of the Likelihood of Antibody-Dependent Enhancement in Influenza

Author

Massachusetts Institute of Technology. Department of Biological Engineering, Tharakaraman, Kannan, Raman, Rahul, Sasisekharan, Ram, Ramakrishnan, Boopathy, Viswanathan, Karthik, Dančík, Vlado, Babcock, Gregory J., Shriver, Zachary, Massachusetts Institute of Technology. Department of Biological Engineering, Tharakaraman, Kannan, Raman, Rahul, Sasisekharan, Ram, Ramakrishnan, Boopathy, Viswanathan, Karthik, Dančík, Vlado, Babcock, Gregory J., and Shriver, Zachary

Abstract

Broadly neutralizing monoclonal antibodies (bNAbs) for viral infections, such as HIV, respiratory syncytial virus (RSV), and influenza, are increasingly entering clinical development. For influenza, most neutralizing antibodies target influenza virus hemagglutinin. These bNAbs represent an emerging, promising modality for treatment and prophylaxis of influenza due to their multiple mechanisms of antiviral action and generally safe profile. Preclinical work in other viral diseases, such as dengue, has demonstrated the potential for antibody-based therapies to enhance viral uptake, leading to enhanced viremia and worsening of disease. This phenomenon is referred to as antibody-dependent enhancement (ADE). In the context of influenza, ADE has been used to explain several preclinical and clinical phenomena. Using structural and viral kinetics modeling, we assess the role of ADE in the treatment of influenza with a bNAb., National Institutes of Health (U.S.) (Merit Award R37 GM057073-13), National Institutes of Health (U.S.) (Grant RO1 AI111395-03)

Published
2018

39. Neutralization of antibody-enhanced dengue infection by VIS513, a pan serotype reactive monoclonal antibody targeting domain III of the dengue E protein

Author

Budigi, Yadunanda, primary, Ong, Eugenia Z., additional, Robinson, Luke N., additional, Ong, Li Ching, additional, Rowley, Kirk J., additional, Winnett, Alexander, additional, Tan, Hwee Cheng, additional, Hobbie, Sven, additional, Shriver, Zachary, additional, Babcock, Gregory J., additional, Alonso, Sylvie, additional, and Ooi, Eng Eong, additional

Published
2018
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40. CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome coronavirus

Author

Sonia M. Tusell, David E. Wentworth, Robert J. Mason, Scott A. Jeffers, Jenna E. Achenbach, Larissa B. Thackray, William D. Thomas, Erin M. Hemmila, James C. DeMartini, Mark D. Young, Babcock Gregory J, Donna M. Ambrosino, Kathryn V. Holmes, and Laura Gillim-Ross

Subjects
Virus genetics, DNA, Complementary, viruses, Cell Cycle Proteins, CHO Cells, medicine.disease_cause, Virus, Cell Line, Retrovirus, Transduction, Genetic, Viral entry, Cricetinae, medicine, Animals, Humans, Lung, Gene Library, Coronavirus, Multidisciplinary, Base Sequence, biology, cDNA library, Chinese hamster ovary cell, fungi, virus diseases, Membrane Proteins, Biological Sciences, biology.organism_classification, Virology, Molecular biology, Recombinant Proteins, respiratory tract diseases, Severe acute respiratory syndrome-related coronavirus, Vesicular stomatitis virus, Receptors, Virus, Receptors, Coronavirus
Abstract

Angiotensin-converting enzyme 2 (ACE2) is a receptor for SARS-CoV, the novel coronavirus that causes severe acute respiratory syndrome [Li, W. Moore, M. J., Vasilieva, N., Sui, J., Wong, S. K., Berne, M. A., Somasundaran, M., Sullivan, J. L., Luzuriaga, K., Greenough, T. C.,et al.(2003)Nature426, 450–454]. We have identified a different human cellular glycoprotein that can serve as an alternative receptor for SARS-CoV. A human lung cDNA library in vesicular stomatitis virus G pseudotyped retrovirus was transduced into Chinese hamster ovary cells, and the cells were sorted for binding of soluble SARS-CoV spike (S) glycoproteins, S590and S1180. Clones of transduced cells that bound SARS-CoV S glycoprotein were inoculated with SARS-CoV, and increases in subgenomic viral RNA from 1–16 h or more were detected by multiplex RT-PCR in four cloned cell lines. Sequencing of the human lung cDNA inserts showed that each of the cloned cell lines contained cDNA that encoded human CD209L, a C-type lectin (also called L-SIGN). When the cDNA encoding CD209L from clone 2.27 was cloned and transfected into Chinese hamster ovary cells, the cells expressed human CD209L glycoprotein and became susceptible to infection with SARS-CoV. Immunohistochemistry showed that CD209L is expressed in human lung in type II alveolar cells and endothelial cells, both potential targets for SARS-CoV. Several other enveloped viruses including Ebola and Sindbis also use CD209L as a portal of entry, and HIV and hepatitis C virus can bind to CD209L on cell membranes but do not use it to mediate virus entry. Our data suggest that the large S glycoprotein of SARS-CoV may use both ACE2 and CD209L in virus infection and pathogenesis.

Published
2004
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41. Structure-Guided Design of an Anti-dengue Antibody Directed to a Non-immunodominant Epitope

Author

Harvard University--MIT Division of Health Sciences and Technology, Massachusetts Institute of Technology. Department of Biological Engineering, Massachusetts Institute of Technology. Department of Biology, Koch Institute for Integrative Cancer Research at MIT, Robinson, Luke Nathaniel, Cain, David Joseph, Kirloskar, Rama Sanjay, Sasisekharan, Viswanathan, Chen, Jianzhu, Sasisekharan, Ram, Tharakaraman, Kannan, Rowley, Kirk J., Costa, Vivian V., Chan, Kuan Rong, Wong, Yee Hwa, Ong, Li Ching, Tan, Hwee Cheng, Koch, Tyree, Viswanathan, Karthik, Liew, Chong Wai, Tissire, Hamid, Ramakrishnan, Boopathy, Myette, James R., Babcock, Gregory J., Alonso, Sylvie, Lescar, Julien, Shriver, Zachary, Ooi, Eng Eong, Cain, David, Harvard University--MIT Division of Health Sciences and Technology, Massachusetts Institute of Technology. Department of Biological Engineering, Massachusetts Institute of Technology. Department of Biology, Koch Institute for Integrative Cancer Research at MIT, Robinson, Luke Nathaniel, Cain, David Joseph, Kirloskar, Rama Sanjay, Sasisekharan, Viswanathan, Chen, Jianzhu, Sasisekharan, Ram, Tharakaraman, Kannan, Rowley, Kirk J., Costa, Vivian V., Chan, Kuan Rong, Wong, Yee Hwa, Ong, Li Ching, Tan, Hwee Cheng, Koch, Tyree, Viswanathan, Karthik, Liew, Chong Wai, Tissire, Hamid, Ramakrishnan, Boopathy, Myette, James R., Babcock, Gregory J., Alonso, Sylvie, Lescar, Julien, Shriver, Zachary, Ooi, Eng Eong, and Cain, David

Abstract

Dengue is the most common vector-borne viral disease, causing nearly 400 million infections yearly. Currently there are no approved therapies. Antibody epitopes that elicit weak humoral responses may not be accessible by conventional B cell panning methods. To demonstrate an alternative strategy to generating a therapeutic antibody, we employed a non-immunodominant, but functionally relevant, epitope in domain III of the E protein, and engineered by structure-guided methods an antibody directed to it. The resulting antibody, Ab513, exhibits high-affinity binding to, and broadly neutralizes, multiple genotypes within all four serotypes. To assess therapeutic relevance of Ab513, activity against important human clinical features of dengue was investigated. Ab513 mitigates thrombocytopenia in a humanized mouse model, resolves vascular leakage, reduces viremia to nearly undetectable levels, and protects mice in a maternal transfer model of lethal antibody-mediated enhancement. The results demonstrate that Ab513 may reduce the public health burden from dengue., National Institutes of Health (U.S.) (NIH Award (1R01AI111395)), National Institute of Environmental Health Sciences (NIEHS training grant (2T32ES007020)), National Institutes of Health (U.S.) (NIH Merit Award (R37 GM057073-13)), National Science Foundation (U.S.)

Published
2016

42. A broadly neutralizing human monoclonal antibody is effective against H7N9

Author

Massachusetts Institute of Technology. Department of Biological Engineering, Massachusetts Institute of Technology. School of Engineering, Koch Institute for Integrative Cancer Research at MIT, Tharakaraman, Kannan, Subramanian, Vidya, Wogan, Gerald N., Sasisekharan, Ram, Viswanathan, Karthik, Sloan, Susan, Yen, Hui-Ling, Barnard, Dale L., Leung, Y. H. Connie, Szretter, Kristy J., Koch, Tyree J., Delaney, James C., Babcock, Gregory J., Shriver, Zachary, Wogan, Gerald N, Massachusetts Institute of Technology. Department of Biological Engineering, Massachusetts Institute of Technology. School of Engineering, Koch Institute for Integrative Cancer Research at MIT, Tharakaraman, Kannan, Subramanian, Vidya, Wogan, Gerald N., Sasisekharan, Ram, Viswanathan, Karthik, Sloan, Susan, Yen, Hui-Ling, Barnard, Dale L., Leung, Y. H. Connie, Szretter, Kristy J., Koch, Tyree J., Delaney, James C., Babcock, Gregory J., Shriver, Zachary, and Wogan, Gerald N

Abstract

Emerging strains of influenza represent a significant public health threat with potential pandemic consequences. Of particular concern are the recently emerged H7N9 strains which cause pneumonia with acute respiratory distress syndrome. Estimates are that nearly 80% of hospitalized patients with H7N9 have received intensive care unit support. VIS410, a human antibody, targets a unique conserved epitope on influenza A. We evaluated the efficacy of VIS410 for neutralization of group 2 influenza strains, including H3N2 and H7N9 strains in vitro and in vivo. VIS410, administered at 50 mg/kg, protected DBA mice infected with A/Anhui/2013 (H7N9), resulting in significant survival benefit upon single-dose (−24 h) or double-dose (−12 h, +48 h) administration (P < 0.001). A single dose of VIS410 at 50 mg/kg (−12 h) combined with oseltamivir at 50 mg/kg (−12 h, twice daily for 7 d) in C57BL/6 mice infected with A/Shanghai 2/2013 (H7N9) resulted in significant decreased lung viral load (P = 0.002) and decreased lung cytokine responses for nine of the 11 cytokines measured. Based on these results, we find that VIS410 may be effective either as monotherapy or combined with antivirals in treating H7N9 disease, as well as disease from other influenza strains., National Institutes of Health (U.S.) (Merit Award R37 GM057073-13), Singapore. National Research Foundation (Singapore-MIT Alliance for Research and Technology)

Published
2016

43. Identification of a Human Monoclonal Antibody to Replace Equine Diphtheria Anti-toxin for the Treatment of Diphtheria

Author

Sevigny, Leila M., Booth, Brian J., Rowley, Kirk J., Leav, Brett A., Cheslock, Peter S., Garrity, Kerry A., Sloan, Susan, Babcock, Gregory J., Thomas, William D., Klempner, Mark, and Wang, Yang

Subjects
complex mixtures
Abstract

Diphtheria anti-toxin (DAT) has been used to treat Corynebacterium diphtheriae infection for over one hundred years. While the global incidence of diphtheria has declined in the 20th century, the disease remains endemic in many parts of the world and significant outbreaks still occur. Diphtheria anti-toxin is an equine polyclonal antibody with considerable side effects that is in critically short supply globally. A safer, more readily available alternative to DAT would be desirable. In the current study, we cloned human monoclonal antibodies (HuMabs) directly from antibody secreting cells of human volunteers immunized with Td vaccine. We isolated a diverse panel of HuMabs that recognized diphtheria toxoid and recombinant protein fragments of diphtheria toxin. Forty-one unique HuMabs were expressed in 293T cells and tested for neutralization of diphtheria toxin in in vitro cytotoxicity assays. The lead candidate HuMab, 315C4 potently neutralized diphtheria toxin with an EC50 of 0.65 ng/mL. Additionally, 25 μg of 315C4 completely protected guinea pigs in an in vivo lethality model. In comparison, 1.6 IU of DAT was necessary for full protection resulting in an estimated relative potency of 64 IU/mg for 315C4. We further established that our lead candidate HuMab binds to the receptor binding domain of diphtheria toxin and blocks the toxin from binding to the putative receptor, heparin binding-epidermal growth factor like growth factor. The discovery of a specific and potent neutralizing antibody against diphtheria toxin holds promise as a potential human therapeutic and is being developed for human use.

Published
2013
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47. High-Throughput Sequencing Analysis of Post-Liver Transplantation HCV E2 Glycoprotein Evolution in the Presence and Absence of Neutralizing Monoclonal Antibody

Author

Babcock, Gregory J., primary, Iyer, Sowmya, additional, Smith, Heidi L., additional, Wang, Yang, additional, Rowley, Kirk, additional, Ambrosino, Donna M., additional, Zamore, Phillip D., additional, Pierce, Brian G., additional, Molrine, Deborah C., additional, and Weng, Zhiping, additional

Published
2014
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49. Identification of Human Monoclonal Antibodies Specific for Human SOD1 Recognizing Distinct Epitopes and Forms of SOD1

Author

Broering, Teresa J., primary, Wang, Hongyan, additional, Boatright, Naomi K., additional, Wang, Yang, additional, Baptista, Katherine, additional, Shayan, Gilda, additional, Garrity, Kerry A., additional, Kayatekin, Can, additional, Bosco, Daryl A., additional, Matthews, C. Robert, additional, Ambrosino, Donna M., additional, Xu, Zuoshang, additional, and Babcock, Gregory J., additional

Published
2013
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50. Human Monoclonal Antibody HCV1 Effectively Prevents and Treats HCV Infection in Chimpanzees

Author

Morin, Trevor J., primary, Broering, Teresa J., additional, Leav, Brett A., additional, Blair, Barbra M., additional, Rowley, Kirk J., additional, Boucher, Elisabeth N., additional, Wang, Yang, additional, Cheslock, Peter S., additional, Knauber, Michael, additional, Olsen, David B., additional, Ludmerer, Steve W., additional, Szabo, Gyongyi, additional, Finberg, Robert W., additional, Purcell, Robert H., additional, Lanford, Robert E., additional, Ambrosino, Donna M., additional, Molrine, Deborah C., additional, and Babcock, Gregory J., additional

Published
2012
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