My correspondence article discusses how next-generation sequencing technology may challenge antibody patent claims, sparking important discussions about intellectual property in the antibody discovery landscape.
Read in Nature →Book chapter describes how next generation sequencing, bioinformatics, and artificial intelligence are advancing modern antibody drug discovery by enabling comprehensive repertoire analysis and accelerating the identification of diverse therapeutic antibodies. Biopharmaceutical Informatics Learning to Discover Developable Biotherapeutics, Taylor & Francis (2025)
Read chapter →Study presents PairedAbNGS, the largest database of naturally paired human antibody sequences, revealing conserved heavy–light chain contacts and germline pairing preferences that inform safer and more effective therapeutic antibody design. Communications Biology (2025)
Read article →Study reveals unexpected bidirectional D gene recombination in antibody repertoires, identifying inverted D genes and diverse D-D fusions that expand understanding of antibody diversity generation and potential therapeutic applications. Communications Biology (2025)
Read article →Study demonstrates a high-efficiency antigen-specific B-cell purification method that increases antibody discovery hit rates to 51–88%, preserves cognate pairing, enhances functional diversity, and streamlines discovery by enriching rare, desirable clones in the repertoire. Communications Biology (2022)
Read article →Perspective highlights how integrating animal immunization with advanced technologies, including single B cell isolation, microfluidics, next generation sequencing, and machine learning, is redefining antibody discovery and accelerating the creation of next generation monoclonal antibodies. mAbs (2021)
Read article →Study reveals strategic incorporation of non-canonical cysteines in human antibody repertoires, uncovering disulfide-stabilized motifs in VH regions that expand paratope diversity and could enable design of antibodies targeting difficult epitopes with enhanced developability. Cell Reports (2020)
Read article →This editorial introduces 17 high-quality research papers published in the Research Topic which summarize recent developments and applications within the context of NGS analysis of human antibody repertoires, through a combination of Original Research, Methodology, and Review articles. Frontiers in Immunology (2020)
Read article →Study identifies a broadly neutralizing human antibody, C585, that targets a novel conserved epitope on the H3 hemagglutinin head, providing structural insights for designing next generation universal influenza vaccines. Journal of Virology (2020)
Read article →Book chapter provides a comprehensive overview of human antibody structure and function, detailing the immunogenetic and structural principles that guide therapeutic antibody design, engineering, and the development of diverse antibody formats. Protein Therapeutics, Wiley VCH (2017)
Read chapter →News & Views article in Nature Biotechnology discusses how a systems-level understanding of immune responses can accelerate the development of effective HIV-1 vaccines. Nature Biotechnology (2016)
Read article →Review explores how antibody sequence and structural features influence aggregation propensity, highlighting mechanisms of instability and strategies to improve the developability and stability of monoclonal antibodies and antibody-drug conjugates. Antibodies (2016)
Read article →Study reveals that junctional and allele-specific residues are key to the exceptional potency of the near-germline antibody m336 in neutralizing MERS-CoV, providing structural insights for vaccine and therapeutic antibody design. Nature Communications (2015)
Read article →Study characterizes human cord blood antibody repertoires using 454 sequencing and IMGT analysis, revealing diverse V-D-J rearrangements and VHCDR3 lengths comparable to adults but with distinct gene usage patterns and fewer somatic mutations. Immunogenetics (2011)
Read article →Review summarizes the discovery and structural characterization of potent human monoclonal antibodies against SARS-CoV, Hendra, and Nipah viruses, highlighting their neutralization mechanisms and therapeutic potential against emerging viral diseases. Expert Opinion on Biological Therapy (2009)
Read article →Study shows that germline-like precursors of broadly neutralizing antibodies fail to bind HIV-1 envelope glycoproteins, suggesting a viral evasion strategy that limits immune activation and informing new approaches for vaccine immunogen design. Biochemical and Biophysical Research Communications (2009)
Read article →Study reports the crystal structure of an isolated unglycosylated human antibody CH2 domain, revealing its monomeric nature, structural similarity to intact Fc regions, and potential as a stable scaffold for antibody engineering and therapeutic design. Acta Crystallographica D (2008)
Read article →Study identifies human monoclonal antibodies m396 and S230.15 that potently neutralize diverse SARS-CoV isolates by blocking ACE2 binding, providing broad protection across epidemic and zoonotic strains and informing therapeutic antibody development. Proceedings of the National Academy of Sciences (2007)
Read article →Study defines the crystal structure of a potent cross-reactive SARS-CoV neutralizing antibody (m396) bound to the spike RBD, revealing key ACE2-competing epitope features and providing structural insights for therapeutic and vaccine design against coronavirus infection. Journal of Biological Chemistry (2006)
Read article →Study reveals the crystal structure of the HIV-1 neutralizing antibody m18, showing structural mimicry of CD4 through unique CDR-H2 and H3 motifs that enable broad cross-reactivity and provide a framework for designing CD4-mimetic vaccines and entry inhibitors. Journal of Molecular Biology (2006)
Read article →Study establishes a quantitative classification of protein–DNA complexes using 11 interaction descriptors, revealing seven structural clusters that transcend motif boundaries and uncover general principles governing protein–DNA recognition. Structure (2006)
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