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Journal of Biotechnology, ISSN 0168-1656, 2005, Volume 120, Issue 4, pp. 347 - 359
The peroxidase gene ( ) was genetically fused to either the 5′- or 3′-terminal ends of the gene encoding llama variable heavy chain antibody fragment V R9,... 
Arthromyces ramosus peroxidase (ARP) | Magic Bullets | Fusion proteins | Aspergillus awamori ;Heterologous protein production | Llama variable heavy chain antibody fragments (V HHs) | Llama variable heavy chain antibody fragments (V | "Magic Bullets" | Heterologous protein production | Aspergillus awamori | fusion proteins | heterologous protein production | DOMAIN | "magic bullets" | llama variable heavy chain antibody fragments (V(HH)s) | FILAMENTOUS FUNGI | GENE | INTEGRATION | OXIDASE | CLONING | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | ENDOPLASMIC-RETICULUM | SECRETION | HETEROLOGOUS EXPRESSION | SELECTION | Recombinant Fusion Proteins - biosynthesis | Recombinant Fusion Proteins - immunology | Fungi, Unclassified - enzymology | Immunoglobulin Heavy Chains - biosynthesis | Fungal Proteins - biosynthesis | Antibodies, Monoclonal - biosynthesis | Immunoglobulin Variable Region - biosynthesis | Fungal Proteins - genetics | Immunoglobulin Variable Region - immunology | Camelids, New World - genetics | Antibodies, Monoclonal - genetics | Aspergillus | Animals | Camelids, New World - immunology | Recombinant Fusion Proteins - genetics | Immunoglobulin Variable Region - genetics | Peroxidase - genetics | Peroxidase - biosynthesis | Fungi, Unclassified - genetics | Immunoglobulin Heavy Chains - immunology | Antibodies, Monoclonal - immunology | Immunoglobulin Heavy Chains - genetics | Proteins | Viral antibodies | Antibodies | Antigens | Peroxidase | Ammunition | fusion | filamentous fungi | secretion | saccharomyces-cerevisiae | gene | thaumatin production | domain | light-chains | heterologous expression | endoplasmic-reticulum
Journal Article
Journal Article
JOURNAL OF IMMUNOLOGICAL METHODS, ISSN 0022-1759, 05/2002, Volume 263, Issue 1-2, pp. 97 - 109
A llama single domain antibody (dAb) library designed and constructed to contain only heavy chain antibody variable domains (V(H)Hs) also contained a... 
REPERTOIRE | DOMAIN | phage display library | CRYSTAL-STRUCTURE | IMMUNOGLOBULINS | BIOCHEMICAL RESEARCH METHODS | ANTIGEN-BINDING | IMMUNOLOGY | ANGSTROM RESOLUTION | POLYSACCHARIDE ANTIGENS | VARIABLE REGION | llama V(H)s and V(H)Hs | anti-idiotypic antibodies | SMALL RECOGNITION UNITS | single domain antibodies | LIGHT-CHAINS
Journal Article
Journal of Immunological Methods, ISSN 0022-1759, 05/2002, Volume 263, Issue 1-2, pp. 97 - 109
A llama single domain antibody (dAb) library designed and constructed to contain only heavy chain antibody variable domains (V Hs) also contained a substantial... 
Phage display library | Single domain antibodies | s and V | Llama V | Anti-idiotypic antibodies
Journal Article
Journal Article
Journal Article
Journal Article
Journal of Immunological Methods, ISSN 0022-1759, 2009, Volume 350, Issue 1, pp. 54 - 62
Journal Article
Protein Engineering, Design & Selection, ISSN 1741-0126, 4/2009, Volume 22, Issue 4, pp. 273 - 280
Journal Article
Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 07/2018, Volume 86, Issue 7, pp. 697 - 706
Nanobodies are a class of antigen‐binding protein derived from camelids that achieve comparable binding affinities and specificities to classical antibodies,... 
antibody | framework | single domain antibody | heavy chain antibody | loop | VHH | HcAb | camelid | REPERTOIRE | BIOCHEMISTRY & MOLECULAR BIOLOGY | LLAMA | MECHANISMS | SINGLE-DOMAIN ANTIBODIES | CONFORMATIONS | PREDICTION | BIOPHYSICS | AFFINITY | Viral antibodies | Antigens | Crystals | Antibodies | Comparative analysis | Structure | Protein binding | Proteins | Molecular chains | Crystal structure
Journal Article
PLoS Pathogens, ISSN 1553-7366, 2013, Volume 9, Issue 3, p. e1003202