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Redesign of a cross-reactive antibody to dengue virus with broad-spectrum activity and increased in vivo potency

https://doi.org/10.1073/pnas.1303645110
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/prot.10389openalex-snapshot
ZDOCK: An initial‐stage protein‐docking algorithm
inferredcites →https://doi.org/10.1002/prot.21373openalex-snapshot
ZRANK: Reranking protein docking predictions with an optimized energy function
inferredcites →https://doi.org/10.1002/prot.21442openalex-snapshot
Identification of near‐native structures by clustering protein docking conformations
inferredcites →https://doi.org/10.1002/prot.21474openalex-snapshot
An automated decision‐tree approach to predicting protein interaction hot spots
inferredcites →https://doi.org/10.1002/prot.22764openalex-snapshot
Performance of ZDOCK and ZRANK in CAPRI rounds 13–19
inferredcites →https://doi.org/10.1007/978-3-642-01144-3_41openalex-snapshot
Affinity Measurements by Competition ELISA
inferredcites →https://doi.org/10.1016/0022-1759(85)90044-4openalex-snapshot
Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay
inferredcites →https://doi.org/10.1016/j.bbapap.2011.12.007openalex-snapshot
Antigen–antibody interface properties: Composition, residue interactions, and features of 53 non-redundant structures
inferredcites →https://doi.org/10.1016/j.bmcl.2009.05.005openalex-snapshot
Improving the species cross-reactivity of an antibody using computational design
inferredcites →https://doi.org/10.1016/j.chom.2010.08.007openalex-snapshot
The Human Immune Response to Dengue Virus Is Dominated by Highly Cross-Reactive Antibodies Endowed with Neutralizing and Enhancing Activity
inferredcites →https://doi.org/10.1016/j.jmb.2005.03.041openalex-snapshot
Molecular Recognition by a Binary Code
inferredcites →https://doi.org/10.1016/j.jmb.2009.12.053openalex-snapshot
Rapid Structural Characterization of Human Antibody–Antigen Complexes through Experimentally Validated Computational Docking
inferredcites →https://doi.org/10.1016/j.jmb.2011.09.031openalex-snapshot
Community-Wide Assessment of Protein-Interface Modeling Suggests Improvements to Design Methodology
inferredcites →https://doi.org/10.1016/j.str.2012.01.001openalex-snapshot
Mechanism of Dengue Virus Broad Cross-Neutralization by a Monoclonal Antibody
inferredcites →https://doi.org/10.1016/s0022-2836(05)80360-2openalex-snapshot
Basic Local Alignment Search Tool
inferredcites →https://doi.org/10.1016/s0140-6736(12)61428-7openalex-snapshot
Protective efficacy of the recombinant, live-attenuated, CYD tetravalent dengue vaccine in Thai schoolchildren: a randomised, controlled phase 2b trial
inferredcites →https://doi.org/10.1016/s0165-022x(03)00145-3openalex-snapshot
Determination of antibody affinity by ELISA. Theory
inferredcites →https://doi.org/10.1016/s0167-7799(97)84205-9openalex-snapshot
Designing and optimizing library selection strategies for generating high-affinity antibodies
inferredcites →https://doi.org/10.1016/s0168-1656(99)00037-1openalex-snapshot
A recombinant Fab neutralizes dengue virus in vitro
inferredcites →https://doi.org/10.1016/s0958-1669(98)80092-xopenalex-snapshot
Strategies for selection of antibodies by phage display
inferredcites →https://doi.org/10.1016/s1286-4579(00)01258-2openalex-snapshot
Dengue viral infections; pathogenesisand epidemiology
inferredcites →https://doi.org/10.1021/bi026947qopenalex-snapshot
Redesigning an Antibody Fragment for Faster Association with Its Antigen
inferredcites →https://doi.org/10.1038/76744openalex-snapshot
Rational design of faster associating and tighter binding protein complexes.
inferredcites →https://doi.org/10.1038/nbt1336openalex-snapshot
Computational design of antibody-affinity improvement beyond in vivo maturation
inferredcites →https://doi.org/10.1038/nri1837openalex-snapshot
Potent antibody therapeutics by design
inferredcites →https://doi.org/10.1038/nrmicro1690openalex-snapshot
Prospects for a dengue virus vaccine
inferredcites →https://doi.org/10.1038/nrmicro2460openalex-snapshot
Dengue: a continuing global threat
inferredcites →https://doi.org/10.1038/nsb0596-427openalex-snapshot
Rapid, electrostatically assisted association of proteins
inferredcites →https://doi.org/10.1038/nsmb.1382openalex-snapshot
Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins
inferredcites →https://doi.org/10.1073/pnas.0401786101openalex-snapshot
Synthetic antibodies from a four-amino-acid code: A dominant role for tyrosine in antigen recognition
inferredcites →https://doi.org/10.1073/pnas.0801221105openalex-snapshot
Affinity maturation of antibodies assisted by in silico modeling
inferredcites →https://doi.org/10.1073/pnas.93.1.13openalex-snapshot
Principles of protein-protein interactions.
inferredcites →https://doi.org/10.1086/382280openalex-snapshot
Relationship of Preexisting Dengue Virus (DV) Neutralizing Antibody Levels to Viremia and Severity of Disease in a Prospective Cohort Study of DV Infection in Thailand
inferredcites →https://doi.org/10.1086/431520openalex-snapshot
Dengue Virus (DV) Enhancing Antibody Activity in Preillness Plasma Does Not Predict Subsequent Disease Severity or Viremia in Secondary DV Infection
inferredcites →https://doi.org/10.1093/bioinformatics/btg371openalex-snapshot
ClusPro: an automated docking and discrimination method for the prediction of protein complexes
inferredcites →https://doi.org/10.1093/protein/gzs024openalex-snapshot
Computer-aided antibody design
inferredcites →https://doi.org/10.1097/qco.0b013e32834a1b0bopenalex-snapshot
Critical issues in dengue vaccine development
inferredcites →https://doi.org/10.1099/0022-1317-82-8-1885openalex-snapshot
Mapping of a dengue virus neutralizing epitope critical for the infectivity of all serotypes: insight into the neutralization mechanism
inferredcites →https://doi.org/10.1099/vir.0.83028-0openalex-snapshot
Mapping to completeness and transplantation of a group-specific, discontinuous, neutralizing epitope in the envelope protein of dengue virus
inferredcites →https://doi.org/10.1110/ps.052030506openalex-snapshot
Affinity enhancement of an in vivo matured therapeutic antibody using structure‐based computational design
inferredcites →https://doi.org/10.1111/j.1742-4658.2005.05045.xopenalex-snapshot
Diversity and junction residues as hotspots of binding energy in an antibody neutralizing the dengue virus
inferredcites →https://doi.org/10.1126/science.1205669openalex-snapshot
A Neutralizing Antibody Selected from Plasma Cells That Binds to Group 1 and Group 2 Influenza A Hemagglutinins
inferredcites →https://doi.org/10.1128/jvi.00316-08openalex-snapshot
Antibodies to Envelope Glycoprotein of Dengue Virus during the Natural Course of Infection Are Predominantly Cross-Reactive and Recognize Epitopes Containing Highly Conserved Residues at the Fusion Loop of Domain II
inferredcites →https://doi.org/10.1128/jvi.69.8.4792-4796.1995openalex-snapshot
Antiviral defense in mice lacking both alpha/beta and gamma interferon receptors
inferredcites →https://doi.org/10.1128/jvi.73.1.783-786.1999openalex-snapshot
New Mouse Model for Dengue Virus Vaccine Testing
inferredcites →https://doi.org/10.1136/pgmj.2004.019638openalex-snapshot
Dengue viral infections
inferredcites →https://doi.org/10.1146/annurev-immunol-031210-101315openalex-snapshot
Immune Response to Dengue Virus and Prospects for a Vaccine
inferredcites →https://doi.org/10.1146/annurev.micro.62.081307.163005openalex-snapshot
Global Spread and Persistence of Dengue
inferredcites →https://doi.org/10.2149/tmh.2010-21openalex-snapshot
An Updated Loop-Mediated Isothermal Amplification Method for Rapid Diagnosis of H5N1 Avian Influenza Viruses
inferredcites →https://doi.org/10.2149/tmh.2011-s05openalex-snapshot
Dengue, Urbanization and Globalization: The Unholy Trinity of the 21st Century
inferredcites →https://doi.org/10.2174/1381612053382106openalex-snapshot
Docking: Successes and Challenges
inferredcites →https://doi.org/10.3390/ijms12010226openalex-snapshot
Computational Docking of Antibody-Antigen Complexes, Opportunities and Pitfalls Illustrated by Influenza Hemagglutinin
inferredcites →https://doi.org/10.3390/v3122374openalex-snapshot
The Human Antibody Response to Dengue Virus Infection

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.3155754openalex-extracted
Structural and Functional Characterization of a CrosssReactive Dengue Virus Neutralizing Antibody That Recognizes a Cryptic Epitope
inferred← citeshttps://doi.org/10.1001/jamanetworkopen.2026.29979openalex-snapshot
Safety and Preliminary Efficacy of Dengue Monoclonal Antibody in Adult Patients
inferred← citeshttps://doi.org/10.1002/iid3.834openalex-snapshot
The validation of artificial anti‐monkeypox antibodies by in silico and experimental approaches
inferred← citeshttps://doi.org/10.1002/prot.24761openalex-snapshot
Inferring the microscopic surface energy of protein–protein interfaces from mutation data
inferred← citeshttps://doi.org/10.1007/978-3-030-11566-1_8openalex-snapshot
Feature Design for Protein Interface Hotspots Using KFC2 and Rosetta
inferred← citeshttps://doi.org/10.1007/s11426-019-9513-2openalex-snapshot
Chimeric protein probes for C5a receptors through fusion of the anaphylatoxin C5a core region with a small-molecule antagonist
inferred← citeshttps://doi.org/10.1016/j.antiviral.2021.105105openalex-snapshot
An antibody engineering platform using amino acid networks: A case study in development of antiviral therapeutics
inferred← citeshttps://doi.org/10.1016/j.bbapap.2014.07.006openalex-snapshot
Antibody informatics for drug discovery
inferred← citeshttps://doi.org/10.1016/j.cell.2015.06.057openalex-snapshot
Structure-Guided Design of an Anti-dengue Antibody Directed to a Non-immunodominant Epitope
inferred← citeshttps://doi.org/10.1016/j.celrep.2023.112711openalex-snapshot
Improved HIV-1 neutralization breadth and potency of V2-apex antibodies by in silico design
inferred← citeshttps://doi.org/10.1016/j.chom.2018.04.004openalex-snapshot
Rational Engineering and Characterization of an mAb that Neutralizes Zika Virus by Targeting a Mutationally Constrained Quaternary Epitope
inferred← citeshttps://doi.org/10.1016/j.coviro.2015.03.019openalex-snapshot
Amino acid interaction networks provide a new lens for therapeutic antibody discovery and anti-viral drug optimization
inferred← citeshttps://doi.org/10.1016/j.febslet.2013.10.014openalex-snapshot
Protein engineering strategies for the development of viral vaccines and immunotherapeutics
inferred← citeshttps://doi.org/10.1016/j.isci.2025.112534openalex-snapshot
A two-component cocktail of engineered DIII nanoparticles elicits broadly neutralizing antibody responses against dengue virus in mice
inferred← citeshttps://doi.org/10.1016/j.molimm.2023.12.006openalex-snapshot
Recombinant human scFv antibody fragments against phospholipase A2 from Naja naja and Echis carinatus snake venoms: In vivo neutralization and mechanistic insights
inferred← citeshttps://doi.org/10.1016/j.molliq.2021.118086openalex-snapshot
Molecular dynamics simulations and Gaussian network model for designing antibody mimicking protein towards dengue envelope protein
inferred← citeshttps://doi.org/10.1016/j.nexres.2025.100670openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.sbi.2013.06.017openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.sbi.2020.12.016openalex-snapshot
Residue-based pharmacophore approaches to study protein–protein interactions
inferred← citeshttps://doi.org/10.1016/j.str.2017.11.017openalex-snapshot
Structural and Functional Characterization of a Cross-Reactive Dengue Virus Neutralizing Antibody that Recognizes a Cryptic Epitope
inferred← citeshttps://doi.org/10.1016/j.virol.2015.08.011openalex-snapshot
Comprehensive mapping of functional epitopes on dengue virus glycoprotein E DIII for binding to broadly neutralizing antibodies 4E11 and 4E5A by phage display
inferred← citeshttps://doi.org/10.1016/j.yjsbx.2020.100028openalex-snapshot
A complex between the Zika virion and the Fab of a broadly cross-reactive neutralizing monoclonal antibody revealed by cryo-EM and single particle analysis at 4.1 Å resolution
inferred← citeshttps://doi.org/10.1021/acsinfecdis.4c00058openalex-snapshot
An Engineered N-Glycosylated Dengue Envelope Protein Domain III Facilitates Epitope-Directed Selection of Potently Neutralizing and Minimally Enhancing Antibodies
inferred← citeshttps://doi.org/10.1021/acsomega.6c02114openalex-snapshot
Potent Cross-Serotype Dengue Neutralization with Low ADE by AG-Strand-Targeting Anti-EDIII Antibodies
inferred← citeshttps://doi.org/10.1021/ci400416eopenalex-snapshot
Energetic and Dynamic Aspects of the Affinity Maturation Process: Characterizing Improved Variants from the Bevacizumab Antibody with Molecular Simulations
inferred← citeshttps://doi.org/10.1038/s41541-016-0003-3openalex-snapshot
A potent neutralizing antibody with therapeutic potential against all four serotypes of dengue virus
inferred← citeshttps://doi.org/10.1038/s41551-026-01718-3openalex-snapshot
CD98hc-targeted antibody shuttles for central nervous system delivery with broad cross-species reactivity
inferred← citeshttps://doi.org/10.1038/s41598-017-01097-5openalex-snapshot
Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells
inferred← citeshttps://doi.org/10.1038/s41598-018-26800-yopenalex-snapshot
Molecular basis for dengue virus broad cross-neutralization by humanized monoclonal antibody 513
inferred← citeshttps://doi.org/10.1038/s42003-019-0457-8openalex-snapshot
THETA system allows one-step isolation of tagged proteins through temperature-dependent protein–peptide interaction
inferred← citeshttps://doi.org/10.1038/s42004-023-01037-7openalex-snapshot
Enhancing antibody affinity through experimental sampling of non-deleterious CDR mutations predicted by machine learning
inferred← citeshttps://doi.org/10.1038/srep41306openalex-snapshot
Computational design of an epitope-specific Keap1 binding antibody using hotspot residues grafting and CDR loop swapping
inferred← citeshttps://doi.org/10.1039/c9me00034hopenalex-snapshot
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inferred← citeshttps://doi.org/10.1073/pnas.1502374112openalex-snapshot
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inferred← citeshttps://doi.org/10.1074/jbc.m117.783837openalex-snapshot
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inferred← citeshttps://doi.org/10.1080/22221751.2026.2686471openalex-snapshot
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inferred← citeshttps://doi.org/10.1093/bib/bbae488openalex-snapshot
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inferred← citeshttps://doi.org/10.1093/bib/bbaf445openalex-snapshot
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inferred← citeshttps://doi.org/10.1093/bioinformatics/bty274openalex-snapshot
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inferred← citeshttps://doi.org/10.1093/protein/gzaa006openalex-snapshot
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inferred← citeshttps://doi.org/10.1101/2023.06.02.543458openalex-snapshot
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inferred← citeshttps://doi.org/10.1101/2023.06.16.545250openalex-snapshot
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inferred← citeshttps://doi.org/10.1111/imm.12213openalex-snapshot
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inferred← citeshttps://doi.org/10.1128/jvi.01023-18openalex-snapshot
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inferred← citeshttps://doi.org/10.1145/2506583.2506693openalex-snapshot
MEGADOCK-GPU
inferred← citeshttps://doi.org/10.1146/annurev-bioeng-071114-040733openalex-snapshot
Advances in Antibody Design
inferred← citeshttps://doi.org/10.1177/0976500x231204401openalex-snapshot
Dengue Virus: Molecular Biology and Recent Developments in Control Strategies, Prevention, Management, and Therapeutics
inferred← citeshttps://doi.org/10.1371/journal.pone.0177012openalex-snapshot
Identification and characterization of a neutralizing monoclonal antibody that provides complete protection against Yersinia pestis
inferred← citeshttps://doi.org/10.1371/journal.pone.0209576openalex-snapshot
Designing antibody against highly conserved region of dengue envelope protein by in silico screening of scFv mutant library
inferred← citeshttps://doi.org/10.1586/14787210.2013.839941openalex-snapshot
Therapeutic antibodies as a treatment option for dengue fever
inferred← citeshttps://doi.org/10.2217/fmb.15.105openalex-snapshot
Dengue: An Update on Treatment Options
inferred← citeshttps://doi.org/10.32657/10356/74114openalex-snapshot
Study of two types of protein-protein interactions : i, a high affinity antigen-antibody complex and ii, a transient complex between an oncoprotein and a methyltransferase
inferred← citeshttps://doi.org/10.3389/fimmu.2018.01117openalex-snapshot
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inferred← citeshttps://doi.org/10.3389/fimmu.2021.574411openalex-snapshot
Prospective Artificial Intelligence to Dissect the Dengue Immune Response and Discover Therapeutics
inferred← citeshttps://doi.org/10.3389/fimmu.2023.1200195openalex-snapshot
Dengue virus neutralizing antibody: a review of targets, cross-reactivity, and antibody-dependent enhancement
inferred← citeshttps://doi.org/10.3389/fmicb.2019.00738openalex-snapshot
Structural Vaccinology for Viral Vaccine Design
inferred← citeshttps://doi.org/10.3389/fmolb.2023.1112738openalex-snapshot
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inferred← citeshttps://doi.org/10.3389/frai.2021.715462openalex-snapshot
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inferred← citeshttps://doi.org/10.3390/antib7030022openalex-snapshot
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inferred← citeshttps://doi.org/10.3390/ijms19010054openalex-snapshot
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inferred← citeshttps://doi.org/10.3390/ijms23084197openalex-snapshot
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inferred← citeshttps://doi.org/10.3390/pathogens9060470openalex-snapshot
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inferred← citeshttps://doi.org/10.3390/v15112177openalex-snapshot
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inferred← citeshttps://doi.org/10.7554/elife.52384openalex-snapshot
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