000			01863 a2200541 4500
005			20250513213411.0
264		0	_c20000721
008			200007s 0 0 eng d
022			_a1072-8368
024	7		_a10.1038/76819 _2doi
040			_aNLM _beng _cNLM
100	1		_aMayer, M P
245	0	0	_aMultistep mechanism of substrate binding determines chaperone activity of Hsp70. _h[electronic resource]
260			_bNature structural biology _cJul 2000
300			_a586-93 p. _bdigital
500			_aPublication Type: Journal Article; Research Support, Non-U.S. Gov't
650	0	4	_aAdenosine Diphosphate _xmetabolism
650	0	4	_aAdenosine Triphosphatases _xchemistry
650	0	4	_aAdenosine Triphosphate _xmetabolism
650	0	4	_aAllosteric Site _xdrug effects
650	0	4	_aBacterial Proteins _xchemistry
650	0	4	_aCatalytic Domain
650	0	4	_aEnzyme Activation
650	0	4	_aEscherichia coli _xchemistry
650	0	4	_aEscherichia coli Proteins
650	0	4	_aGenetic Complementation Test
650	0	4	_aHSP70 Heat-Shock Proteins _xchemistry
650	0	4	_aHeat-Shock Proteins _xmetabolism
650	0	4	_aHydrolysis _xdrug effects
650	0	4	_aKinetics
650	0	4	_aModels, Biological
650	0	4	_aModels, Molecular
650	0	4	_aMolecular Chaperones _xchemistry
650	0	4	_aMutation _xgenetics
650	0	4	_aPhenotype
650	0	4	_aProtein Binding _xdrug effects
650	0	4	_aProtein Structure, Secondary _xdrug effects
650	0	4	_aSigma Factor
650	0	4	_aThermodynamics
650	0	4	_aTranscription Factors _xmetabolism
700	1		_aSchröder, H
700	1		_aRüdiger, S
700	1		_aPaal, K
700	1		_aLaufen, T
700	1		_aBukau, B
773	0		_tNature structural biology _gvol. 7 _gno. 7 _gp. 586-93
856	4	0	_uhttps://doi.org/10.1038/76819 _zAvailable from publisher's website
999			_c10826907 _d10826907