His primary areas of investigation include Glycosylation, Glycoprotein, Glycan, Virology and Biochemistry. His Glycosylation research includes elements of Decay-accelerating factor, Crystallography and Mutation. His Glycoprotein study combines topics in areas such as Epitope, Gp41, Viral Vaccine and Recombinant DNA.
His work deals with themes such as Antibody, Neutralization, Carbohydrate conformation, Cell biology and Coronavirus, which intersect with Glycan. His Antibody research is multidisciplinary, relying on both Mutagenesis and Mannose. The concepts of his Virology study are interwoven with issues in Protein structure, Immunogen and Immune system.
His scientific interests lie mostly in Glycan, Glycoprotein, Virology, Antibody and Glycosylation. His Glycan research includes themes of Epitope, Plasma protein binding, Cell biology and Immunogen. He merges many fields, such as Glycoprotein and Trimer, in his writings.
His studies deal with areas such as HIV vaccine and Immunogenicity as well as Virology. His Antibody research is multidisciplinary, incorporating perspectives in Immune system and Antigen. His biological study deals with issues like Antibody-dependent cell-mediated cytotoxicity, which deal with fields such as Receptor.
The scientist’s investigation covers issues in Antibody, Glycan, Glycoprotein, Virology and Glycosylation. His Antibody research incorporates themes from Virus, Disease and Severe acute respiratory syndrome coronavirus 2. The Glycan study combines topics in areas such as Epitope, Immunogen, Recombinant DNA and Cell biology.
His work on Epitope mapping as part of general Epitope research is frequently linked to Trimer, bridging the gap between disciplines. He combines subjects such as Computational biology and Antigen with his study of Glycoprotein. Max Crispin has researched Glycosylation in several fields, including Druggability, Virus maturation, Pathogen and Mutation.
His main research concerns Glycan, Glycoprotein, Antibody, Immunogen and Virology. His Glycan study frequently draws connections between adjacent fields such as Glycosylation. His Glycoprotein research is multidisciplinary, incorporating elements of Respiratory epithelium, Respiratory system, Interferon, Downregulation and upregulation and Gene isoform.
Saliva, Allergy and Neutralizing antibody is closely connected to Antigen in his research, which is encompassed under the umbrella topic of Antibody. His research integrates issues of Epitope, Immune system, Lipid bilayer fusion and Betacoronavirus in his study of Immunogen. His research in Virology focuses on subjects like Coronavirus, which are connected to Specific antibody, Severe acute respiratory syndrome coronavirus 2, Dried blood spot, Serum samples and 2019-20 coronavirus outbreak.
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Site-specific glycan analysis of the SARS-CoV-2 spike.
Yasunori Watanabe;Yasunori Watanabe;Joel D. Allen;Daniel Wrapp;Jason S. McLellan.
Molecular Architecture of the SARS-CoV-2 Virus
Hangping Yao;Yutong Song;Yong Chen;Nanping Wu.
Emerging Principles for the Therapeutic Exploitation of Glycosylation
Martin Dalziel;Max Crispin;Christopher N. Scanlan;Nicole Zitzmann.
Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens
Katherine Doores;Camille Bonomelli;David J Harvey;Snezana Vasiljevic.
Proceedings of the National Academy of Sciences of the United States of America (2010)
Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B and G
Guillaume B.E. Stewart-Jones;Cinque Soto;Thomas Lemmin;Thomas Lemmin;Gwo Yu Chuang.
Glycoprotein Structural Genomics: Solving the Glycosylation Problem
V T Chang;M Crispin;M Crispin;A R Aricescu;D J Harvey.
Exploitation of glycosylation in enveloped virus pathobiology.
Yasunori Watanabe;Thomas A. Bowden;Ian A. Wilson;Max Crispin.
Biochimica et Biophysica Acta (2019)
Quantitative mass imaging of single biological macromolecules
Gavin Young;Nikolas Hundt;Daniel Cole;Adam Fineberg.
Immunogenicity of Stabilized HIV-1 Envelope Trimers with Reduced Exposure of Non-neutralizing Epitopes
Steven W. de Taeye;Gabriel Ozorowski;Alba Torrents de la Peña;Miklos Guttman.
Contrasting IgG structures reveal extreme asymmetry and flexibility.
Erica Ollmann Saphire;Robyn L. Stanfield;M.D. Max Crispin;M.D. Max Crispin;Paul W.H.I. Parren.
Journal of Molecular Biology (2002)
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