Structure of a single-chain Fv bound to the 17 N-terminal residues of huntingtin provides insights into pathogenic amyloid formation and suppression

Journal of Molecular Biology

Volumn 427, Issue 12, 2015, Pages 2166-2178

  De Genst, Erwin ^a   Chirgadze, Dimitri Y ^a   Klein, Fabrice A C ^b   Butler, David C ^c,d   Matak Vinković, Dijana ^a   Trottier, Yvon ^b   Huston, James S ^e   Messer, Anne ^c,d   Dobson, Christopher M ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b INSTITUT DE GÉNÉTIQUE ET DE BIOLOGIE MOLÉCULAIRE ET CELLULAIRE   (France)

^c Regenerative Research Foundation   (United States)

^d STATE UNIVERSITY OF NEW YORK   (United States)

^e the Antibody Society   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; HTT PROTEIN, HUMAN; NERVE PROTEIN; PROTEIN BINDING; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY;

ANTAGONISTS AND INHIBITORS; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METABOLISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHYSICAL CHEMISTRY; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

AMYLOID; CRYSTALLOGRAPHY, X-RAY; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; NERVE TISSUE PROTEINS; PHYSICOCHEMICAL PHENOMENA; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; SINGLE-CHAIN ANTIBODIES;

EID: 84937759580     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2015.03.021     Document Type: Article

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