Immunological hotspots analyzed by docking simulations: Evidence for a general mechanism in pemphigus vulgaris pathology and transformation

• Main Authors: Tong, J.C, Sinha, A.A
• 其他作者: BIOCHEMISTRY
• 格式: Article
• 出版: 2020
• 主題: desmoglein 1; desmoglein 3; glycoprotein; HLA DR antigen; autoantibody; epitope; amino acid sequence; article; binding affinity; controlled study; disease course; epitope mapping; immunological technique; immunopathology; molecular docking; molecular model; nonhuman; pemphigus vulgaris; protein binding; protein domain; protein structure; protein targeting; screening; sequence alignment; sequence homology; T lymphocyte; biological model; chemical structure; chemistry; comparative study; computer simulation; extracellular space; genetics; human; immunology; metabolism; molecular genetics; pathology; pemphigus; protein tertiary structure; Amino Acid Sequence; Autoantibodies; Computer Simulation; Desmoglein 1; Desmoglein 3; Epitopes, T-Lymphocyte; Extracellular Space; Humans; Models, Immunological; Models, Molecular; Molecular Sequence Data; Pemphigus; Protein Structure, Tertiary
• 在線閱讀: https://scholarbank.nus.edu.sg/handle/10635/177970

10.1186/1471-2172-9-30