000 01411 a2200397 4500
005 20250517004908.0
264 0 _c20150715
008 201507s 0 0 eng d
022 _a1937-9145
024 7 _a10.1126/scisignal.2005786
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aLittlefield, Peter
245 0 0 _aStructural analysis of the EGFR/HER3 heterodimer reveals the molecular basis for activating HER3 mutations.
_h[electronic resource]
260 _bScience signaling
_cDec 2014
300 _ara114 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
650 0 4 _aCloning, Molecular
650 0 4 _aCrystallization
650 0 4 _aDimerization
650 0 4 _aErbB Receptors
_xchemistry
650 0 4 _aHumans
650 0 4 _aModels, Molecular
650 0 4 _aMolecular Dynamics Simulation
650 0 4 _aMutagenesis, Site-Directed
650 0 4 _aMutation
_xgenetics
650 0 4 _aProtein Structure, Tertiary
650 0 4 _aReceptor, ErbB-3
_xchemistry
650 0 4 _aSignal Transduction
_xgenetics
700 1 _aLiu, Lijun
700 1 _aMysore, Venkatesh
700 1 _aShan, Yibing
700 1 _aShaw, David E
700 1 _aJura, Natalia
773 0 _tScience signaling
_gvol. 7
_gno. 354
_gp. ra114
856 4 0 _uhttps://doi.org/10.1126/scisignal.2005786
_zAvailable from publisher's website
999 _c24422925
_d24422925