000			02033 a2200529 4500
005			20250517082835.0
264		0	_c20160811
008			201608s 0 0 eng d
022			_a1091-6490
024	7		_a10.1073/pnas.1516167113 _2doi
040			_aNLM _beng _cNLM
100	1		_aSung, Nuri
245	0	0	_aMitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate. _h[electronic resource]
260			_bProceedings of the National Academy of Sciences of the United States of America _cMar 2016
300			_a2952-7 p. _bdigital
500			_aPublication Type: Comparative Study; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
650	0	4	_aAdenosine Triphosphate _xchemistry
650	0	4	_aAllosteric Regulation
650	0	4	_aAllosteric Site
650	0	4	_aAmino Acid Motifs
650	0	4	_aAmino Acid Sequence
650	0	4	_aAmino Acid Substitution
650	0	4	_aAnimals
650	0	4	_aBinding Sites
650	0	4	_aComputer Simulation
650	0	4	_aCrystallography, X-Ray
650	0	4	_aHSP70 Heat-Shock Proteins _xmetabolism
650	0	4	_aHSP90 Heat-Shock Proteins _xchemistry
650	0	4	_aHumans
650	0	4	_aMitochondria _xmetabolism
650	0	4	_aModels, Molecular
650	0	4	_aMolecular Sequence Data
650	0	4	_aProtein Binding
650	0	4	_aProtein Conformation
650	0	4	_aProtein Folding
650	0	4	_aRabbits
650	0	4	_aRecombinant Fusion Proteins _xchemistry
650	0	4	_aSequence Homology, Amino Acid
700	1		_aLee, Jungsoon
700	1		_aKim, Ji-Hyun
700	1		_aChang, Changsoo
700	1		_aJoachimiak, Andrzej
700	1		_aLee, Sukyeong
700	1		_aTsai, Francis T F
773	0		_tProceedings of the National Academy of Sciences of the United States of America _gvol. 113 _gno. 11 _gp. 2952-7
856	4	0	_uhttps://doi.org/10.1073/pnas.1516167113 _zAvailable from publisher's website
999			_c25783154 _d25783154