Fully human VH single domains that rival the stability and cleft recognition of camelid antibodies

Journal of Biological Chemistry

Volumn 290, Issue 19, 2015, Pages 11905-11917

  Rouet, Romain ^a   Dudgeon, Kip ^a   Christie, Mary ^a,b   Langley, David ^a   Christ, Daniel ^a,b  

^a GARVAN INSTITUTE OF MEDICAL RESEARCH   (Australia)

^b UNIVERSITY OF NEW SOUTH WALES   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN-ANTIBODY REACTIONS; BINDERS; BINDING ENERGY; EPITOPES; PHAGE DISPLAY;

ANTIGEN RECOGNITION; BINDING PROPERTIES; BIOPHYSICAL PROPERTIES; COMPLEMENTARITY-DETERMINING REGION 3; HEN EGG WHITE LYSOZYME; PHAGE DISPLAY LIBRARIES; STRUCTURE DETERMINATION; THERAPEUTIC MODALITY;

ANTIBODIES;

EGG WHITE; LYSOZYME; ANTIBODY; COMPLEMENTARITY DETERMINING REGION; EPITOPE; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN VARIABLE REGION; MONOCLONAL ANTIBODY; PEPTIDE LIBRARY; PROTEIN BINDING;

ANTIBODY COMBINING SITE; ANTIBODY ENGINEERING; ANTIGEN BINDING; ANTIGEN RECOGNITION; ARTICLE; CAMELID; IMMUNOGENICITY; MUTATION; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MODIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE; AMINO ACID SEQUENCE; ANIMAL; ANTIBODY AFFINITY; ANTIBODY SPECIFICITY; CAMEL; CHEMISTRY; COMPLEMENTARITY DETERMINING REGION; ENZYME ACTIVE SITE; ENZYME LINKED IMMUNOSORBENT ASSAY; HEAT; HUMAN; IMMUNOGLOBULIN VARIABLE REGION; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PEPTIDE LIBRARY; PROCEDURES; PROTEIN ENGINEERING; SEQUENCE HOMOLOGY; SURFACE PLASMON RESONANCE;

CAMELIDAE;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES; ANTIBODIES, MONOCLONAL; ANTIBODY AFFINITY; ANTIBODY SPECIFICITY; BASE SEQUENCE; CAMELS; CATALYTIC DOMAIN; COMPLEMENTARITY DETERMINING REGIONS; ENZYME-LINKED IMMUNOSORBENT ASSAY; EPITOPES; HOT TEMPERATURE; HUMANS; IMMUNOGLOBULIN HEAVY CHAINS; IMMUNOGLOBULIN VARIABLE REGION; MOLECULAR SEQUENCE DATA; MURAMIDASE; PEPTIDE LIBRARY; PROTEIN BINDING; PROTEIN ENGINEERING; SEQUENCE HOMOLOGY, AMINO ACID; SURFACE PLASMON RESONANCE;

EID: 84929103639     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.614842     Document Type: Article

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