Helical structures of ESCRT-III are disassembled by VPS4

Science

Volumn 321, Issue 5894, 2008, Pages 1354-1357

  Lata, Suman ^a   Schoehn, Guy ^a,b   Jain, Ankur ^c,e   Pires, Ricardo ^a   Piehler, Jacob ^c   Gottlinger, Heinrich G ^d   Weissenhorn, Winfried ^a  

^a UNIV GRENOBLE ALPES   (France)

^b INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^c GOETHE UNIVERSITY   (Germany)

^d UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

^e University of Illinois at Urbana Champaign   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHARGED MULTIVESICULAR BODY PROTEIN 2A; CHARGED MULTIVESICULAR BODY PROTEIN 3; ENDOSOMAL SORTING COMPLEXES REQUIRED FOR TRANSPORT III; MEMBRANE PROTEIN; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATE; BC 2 PROTEIN, HUMAN; BC-2 PROTEIN, HUMAN; LIPOSOME; TUMOR MARKER; VESICULAR TRANSPORT PROTEIN; VPS24 PROTEIN, HUMAN;

CATALYSIS; GENE EXPRESSION; HYDROLYSIS; LIPID; PROTEIN; SOLUTION; VIRUS;

ARTICLE; CATALYST; HYDROLYSIS; IN VITRO STUDY; LIPID BILAYER; MUTANT; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN TARGETING; CHEMICAL STRUCTURE; CHEMISTRY; DENSITY GRADIENT CENTRIFUGATION; DIMERIZATION; HUMAN; METABOLISM; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; CENTRIFUGATION, DENSITY GRADIENT; DIMERIZATION; HUMANS; LIPID BILAYERS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; TUMOR MARKERS, BIOLOGICAL; UNILAMELLAR LIPOSOMES; VESICULAR TRANSPORT PROTEINS;

EID: 51149106799     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1161070     Document Type: Article

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28. We thank X. Siebert (Institut de Biologie Structurale) for advice on UROX. This work was supported by Deutsche Forschungsgemeinschaft (SPP 1175) (W.W.), the Agence Nationale de la Recherche sur le SIDA (W.W.), Université Joseph Fourier (W.W.), the Agence Nationale de la Recherche (G.S.), the CNRS (G.S.), the NIH (grant AI29873, H.G.), and by postdoctoral fellowships from the European Molecular Biology Organization (S.L.) and the International Human Frontier Science Program Organization (S.L.). The EM map has been deposited at the European Bioinformatics Institute, accession code EMD-1536.