A llama-derived gelsolin single-domain antibody blocks gelsolin-G-actin interaction

Cellular and Molecular Life Sciences

Volumn 67, Issue 9, 2010, Pages 1519-1535

  Van Den Abbeele, Anske ^a,b   De Clercq, Sarah ^a,b   De Ganck, Ariane ^a,b   De Corte, Veerle ^a,b   Van Loo, Berlinda ^a,b   Soror, Sameh Hamdy ^a,c   Srinivasan, Vasundara ^a,c   Steyaert, Jan ^a,c   Vandekerckhove, Joël ^a,b   Gettemans, Jan ^a,b  

^a DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^b GHENT UNIVERSITY   (Belgium)

^c FREE UNIVERSITY OF BRUSSELS   (Belgium)

Author keywords

Calcium; Cancer cell; Cytoskeleton; Gelsolin; Immunomodulation; Intrabody; Single domain antibody; VHH

Indexed keywords

ACTIN BINDING PROTEIN; CALCIUM; EPIDERMAL GROWTH FACTOR; EPITOPE; F ACTIN; G ACTIN; GELSOLIN; PROTEIN ANTIBODY; STRUCTURAL PROTEIN; ACTIN; HYBRID PROTEIN; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY;

ANIMAL CELL; ANTIBODY STRUCTURE; ANTIGEN BINDING; ARTICLE; ARTIODACTYLA; CELL MIGRATION; CELL NUCLEUS; CELL STRAIN HEK293; CELL STRAIN MCF 7; CELL SUBPOPULATION; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; CYTOSKELETON; HELA CELL; HUMAN; HUMAN CELL; IMMUNOMODULATION; IN VITRO STUDY; IN VIVO STUDY; MAMMAL CELL; MITOCHONDRION; MOLECULAR RECOGNITION; NONHUMAN; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REGULATORY MECHANISM; ANIMAL; CELL LINE; CELL MOTION; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; IMMUNOLOGY; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; ULTRASTRUCTURE; X RAY CRYSTALLOGRAPHY;

CAMELIDAE; LAMA (MAMMAL); MAMMALIA;

ACTINS; ANIMALS; CALCIUM; CAMELIDS, NEW WORLD; CELL LINE; CELL MOVEMENT; CRYSTALLOGRAPHY, X-RAY; EPITOPES; GELSOLIN; HUMANS; MITOCHONDRIA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SINGLE-CHAIN ANTIBODIES;

EID: 77952298239     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-010-0266-1     Document Type: Article

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