000			01939 a2200529 4500
005			20250513031358.0
264		0	_c19950222
008			199502s 0 0 eng d
022			_a0021-9258
024	7		_a10.1074/jbc.270.4.1711 _2doi
040			_aNLM _beng _cNLM
100	1		_aCarson, M R
245	0	0	_aThe two nucleotide-binding domains of cystic fibrosis transmembrane conductance regulator (CFTR) have distinct functions in controlling channel activity. _h[electronic resource]
260			_bThe Journal of biological chemistry _cJan 1995
300			_a1711-7 p. _bdigital
500			_aPublication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
650	0	4	_a3T3 Cells
650	0	4	_aAdenosine Triphosphate _xanalogs & derivatives
650	0	4	_aAdenylyl Imidodiphosphate _xpharmacology
650	0	4	_aAmino Acid Sequence
650	0	4	_aAnimals
650	0	4	_aAzides _xmetabolism
650	0	4	_aBinding Sites
650	0	4	_aChloride Channels _xchemistry
650	0	4	_aConserved Sequence
650	0	4	_aCyclic AMP-Dependent Protein Kinases _xmetabolism
650	0	4	_aCystic Fibrosis Transmembrane Conductance Regulator
650	0	4	_aGenetic Variation
650	0	4	_aHeLa Cells
650	0	4	_aHumans
650	0	4	_aIon Channel Gating
650	0	4	_aLysine
650	0	4	_aMembrane Potentials
650	0	4	_aMembrane Proteins _xchemistry
650	0	4	_aMice
650	0	4	_aMolecular Sequence Data
650	0	4	_aMutagenesis, Site-Directed
650	0	4	_aPatch-Clamp Techniques
650	0	4	_aPhosphorylation
650	0	4	_aPoint Mutation
650	0	4	_aRecombinant Proteins _xchemistry
650	0	4	_aTransfection
700	1		_aTravis, S M
700	1		_aWelsh, M J
773	0		_tThe Journal of biological chemistry _gvol. 270 _gno. 4 _gp. 1711-7
856	4	0	_uhttps://doi.org/10.1074/jbc.270.4.1711 _zAvailable from publisher's website
999			_c7529708 _d7529708