000 01466 a2200349 4500
005 20250516102021.0
264 0 _c20121119
008 201211s 0 0 eng d
022 _a1083-351X
024 7 _a10.1074/jbc.M112.352617
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aKim, Jin Hae
245 0 0 _aSpecialized Hsp70 chaperone (HscA) binds preferentially to the disordered form, whereas J-protein (HscB) binds preferentially to the structured form of the iron-sulfur cluster scaffold protein (IscU).
_h[electronic resource]
260 _bThe Journal of biological chemistry
_cSep 2012
300 _a31406-13 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, N.I.H., Extramural
650 0 4 _aAdenosine Triphosphate
_xchemistry
650 0 4 _aEscherichia coli
_xchemistry
650 0 4 _aEscherichia coli Proteins
_xchemistry
650 0 4 _aHSP70 Heat-Shock Proteins
_xchemistry
650 0 4 _aHeat-Shock Proteins
_xchemistry
650 0 4 _aIron-Sulfur Proteins
_xchemistry
650 0 4 _aMultiprotein Complexes
_xchemistry
650 0 4 _aNuclear Magnetic Resonance, Biomolecular
650 0 4 _aProtein Binding
700 1 _aTonelli, Marco
700 1 _aFrederick, Ronnie O
700 1 _aChow, Darius C-F
700 1 _aMarkley, John L
773 0 _tThe Journal of biological chemistry
_gvol. 287
_gno. 37
_gp. 31406-13
856 4 0 _uhttps://doi.org/10.1074/jbc.M112.352617
_zAvailable from publisher's website
999 _c21934599
_d21934599