Hsp90-tau complex reveals molecular basis for specificity in chaperone action

Cell

Volumn 156, Issue 5, 2014, Pages 963-974

  Karagöz, G Elif ^a,b   Duarte, Afonso M S ^a,c   Akoury, Elias ^d   Ippel, Hans ^a,e   Biernat, Jacek ^f   Morán Luengo, Tania ^a   Radli, Martina ^a   Didenko, Tatiana ^a,m   Nordhues, Bryce A ^g   Veprintsev, Dmitry B ^h   Dickey, Chad A ^g   Mandelkow, Eckhard ^f,i   Zweckstetter, Markus ^d,f,j   Boelens, Rolf ^a   Madl, Tobias ^a,k,l   Rüdiger, Stefan G D ^a  

^a UTRECHT UNIVERSITY   (Netherlands)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c INSTITUTO DE TECNOLOGIA QUÍMICA E BIOLÓGICA   (Portugal)

^d MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^e MAASTRICHT UNIVERSITY   (Netherlands)

^f GERMAN CENTER FOR NEURODEGENERATIVE DISEASES DZNE   (Germany)

^g UNIVERSITY OF SOUTH FLORIDA   (United States)

^h PAUL SCHERRER INSTITUTE   (Switzerland)

ⁱ CENTER OF ADVANCED EUROPEAN STUDIES AND RESEARCH CAESAR   (Germany)

^j University Medical Center   (Germany)

^k TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^l UNIVERSITY OF GRAZ   (Austria)

^m SCRIPPS RESEARCH INSTITUTE   (United States)

more..

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 90; INTRINSICALLY DISORDERED PROTEIN; MULTIPROTEIN COMPLEX; TAU PROTEIN; ADENOSINE TRIPHOSPHATE;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; COMPLEX FORMATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; HYDROPHOBICITY; MICROTUBULE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; CONTROLLED STUDY; HUMAN; MOLECULAR DYNAMICS; PROTEIN FUNCTION; STRUCTURE ANALYSIS;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; HSP90 HEAT-SHOCK PROTEINS; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; SCATTERING, SMALL ANGLE; TAU PROTEINS; X-RAY DIFFRACTION;

EID: 84896837095     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2014.01.037     Document Type: Article

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