G-protein-coupled receptor inactivation by an allosteric inverse-agonist antibody

Nature

Volumn 482, Issue 7384, 2012, Pages 237-240

  Hino, Tomoya ^a,b,l   Arakawa, Takatoshi ^a,b   Iwanari, Hiroko ^c   Yurugi Kobayashi, Takami ^a,b   Ikeda Suno, Chiyo ^a,b   Nakada Nakura, Yoshiko ^c,d   Kusano Arai, Osamu ^c,e   Weyand, Simone ^a,f,g,h   Shimamura, Tatsuro ^a,b   Nomura, Norimichi ^a,b   Cameron, Alexander D ^a,f,g,h   Kobayashi, Takuya ^a,b,i   Hamakubo, Takao ^c   Iwata, So ^a,b,f,g,h,j   Murata, Takeshi ^a,b,j,k  

^a JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^b KYOTO UNIVERSITY   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

^d Perseus Proteomics   (Japan)

^e Institute of Immunology Co Ltd   (Japan)

^f IMPERIAL COLLEGE LONDON   (United Kingdom)

^g DIAMOND LIGHT SOURCE LTD   (United Kingdom)

^h RUTHERFORD APPLETON LABORATORY   (United Kingdom)

ⁱ KYOTO UNIVERSITY FACULTY OF MEDICINE   (Japan)

^j RIKEN   (Japan)

^k CHIBA UNIVERSITY   (Japan)

^l TOTTORI UNIVERSITY   (Japan)

more..

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE A2 RECEPTOR; ADENOSINE A2 RECEPTOR AGONIST; ADENOSINE A2 RECEPTOR ANTAGONIST; BETA 2 ADRENERGIC RECEPTOR; G PROTEIN COUPLED RECEPTOR; G PROTEIN COUPLED RECEPTOR ANTIBODY; IMMUNOGLOBULIN F(AB) FRAGMENT; MONOCLONAL ANTIBODY; OPSIN; RECEPTOR ANTIBODY; UNCLASSIFIED DRUG;

ANTIBODY; BLOOD; BRAIN; LIGAND; MEMBRANE; MOLECULAR ANALYSIS; PROTEIN; RODENT;

ALLOSTERISM; ANTIBODY STRUCTURE; ANTIGEN BINDING; ANTIGEN RECOGNITION; ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPLEMENTARITY DETERMINING REGION; CRYSTALLOGRAPHY; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN CONFORMATION;

ALLOSTERIC REGULATION; ANIMALS; ANTIBODIES, MONOCLONAL; COMPLEMENTARITY DETERMINING REGIONS; DRUG INVERSE AGONISM; HUMANS; IMMUNOGLOBULIN FAB FRAGMENTS; LIGANDS; MICE; MODELS, MOLECULAR; OPSINS; PICHIA; PROTEIN CONFORMATION; RECEPTOR, ADENOSINE A2A; RECEPTORS, G-PROTEIN-COUPLED;

EID: 84862776818     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature10750     Document Type: Article

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