Camelid single-domain antibody fragments: Uses and prospects to investigate protein misfolding and aggregation, and to treat diseases associated with these phenomena

Biochimie

Volumn 111, Issue , 2015, Pages 82-106

  Pain, Coralie ^a   Dumont, Janice ^a   Dumoulin, Mireille ^a  

^a UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

aggregation; Amyloidoses; Inhibition of protein misfolding and; Nanobody; Protein misfolding diseases; VHH; Variable domain of heavy chain antibody

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; ANTIBODY; LYSOZYME; NANOBODY; OLIGOMER; POLYADENYLIC ACID BINDING PROTEIN; SYNUCLEIN; IMMUNOGLOBULIN HEAVY CHAIN;

ALZHEIMER DISEASE; AMYLOIDOSIS; ANTIGEN BINDING; ARTIODACTYLA; BLOOD BRAIN BARRIER; HUMAN; IMMUNOGENICITY; MAJOR HISTOCOMPATIBILITY COMPLEX; MUSCULAR DYSTROPHY; NONHUMAN; PARKINSON DISEASE; PRION; PRION DISEASE; PROTEIN AGGREGATION; PROTEIN FOLDING; REVIEW; ANIMAL; GENETICS; IMMUNOLOGY; NEW WORLD CAMELID; PROTEIN AGGREGATION, PATHOLOGICAL; PROTEOSTASIS DEFICIENCIES;

CAMELIDAE;

ANIMALS; CAMELIDS, NEW WORLD; HUMANS; IMMUNOGLOBULIN HEAVY CHAINS; PROTEIN AGGREGATION, PATHOLOGICAL; PROTEOSTASIS DEFICIENCIES; SINGLE-DOMAIN ANTIBODIES;

EID: 84923634070     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2015.01.012     Document Type: Review

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