Structural analysis of der p 1-antibody complexes and comparison with complexes of proteins or peptides with monoclonal antibodies

Journal of Immunology

Volumn 195, Issue 1, 2015, Pages 307-316

  Osinski, Tomasz ^a,b   Pomés, Anna ^c   Majorek, Karolina A ^a,b   Glesner, Jill ^c   Offermann, Lesa R ^d   Vailes, Lisa D ^c   Chapman, Martin D ^c   Minor, Wladek ^a   Chruszcz, Maksymilian ^d  

^a UNIVERSITY OF VIRGINIA   (United States)

^b ADAM MICKIEWICZ UNIVERSITY   (Poland)

^c INDOOR Biotechnologies Inc   (United States)

^d UNIVERSITY OF SOUTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DER F 1 ANTIGEN; DER P 1 ANTIGEN; EPITOPE; HOUSE DUST ALLERGEN; IMMUNOGLOBULIN F(AB) FRAGMENT; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 10B9; MONOCLONAL ANTIBODY 4C1; MONOCLONAL ANTIBODY 5H8; UNCLASSIFIED DRUG; ANTIGEN ANTIBODY COMPLEX; ARTHROPOD PROTEIN; CYSTEINE PROTEINASE; DERMATOPHAGOIDES FARINAE ANTIGEN F 1; DERMATOPHAGOIDES PTERONYSSINUS ANTIGEN P 1; PEPTIDE; PROTEIN BINDING;

ALPHA HELIX; ANTIGEN ANTIBODY COMPLEX; ANTIGEN STRUCTURE; ANTIGENICITY; ARTICLE; COMPLEMENTARITY DETERMINING REGION; CONTROLLED STUDY; CROSS REACTION; CRYSTAL STRUCTURE; DERMATOPHAGOIDES PTERONYSSINUS; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; SURFACE PROPERTY; AMINO ACID SEQUENCE; ANIMAL; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; IMMUNOLOGY; ISOLATION AND PURIFICATION; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; PYROGLYPHIDAE; SEQUENCE ALIGNMENT; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES, MONOCLONAL; ANTIGEN-ANTIBODY COMPLEX; ANTIGENS, DERMATOPHAGOIDES; ARTHROPOD PROTEINS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; CYSTEINE ENDOPEPTIDASES; EPITOPES; HYDROGEN BONDING; IMMUNOGLOBULIN FAB FRAGMENTS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PYROGLYPHIDAE; SEQUENCE ALIGNMENT;

EID: 84932090487     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1402199     Document Type: Article

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