000 01525 a2200421 4500
005 20250513183238.0
264 0 _c19990615
008 199906s 0 0 eng d
022 _a0092-8674
024 7 _a10.1016/s0092-8674(00)80757-6
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aPrehoda, K E
245 0 0 _aStructure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly.
_h[electronic resource]
260 _bCell
_cMay 1999
300 _a471-80 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
650 0 4 _aActins
_xmetabolism
650 0 4 _aAmino Acid Sequence
650 0 4 _aAnimals
650 0 4 _aBinding Sites
650 0 4 _aCell Adhesion Molecules
_xchemistry
650 0 4 _aDNA-Binding Proteins
_xchemistry
650 0 4 _aHumans
650 0 4 _aMicrofilament Proteins
650 0 4 _aMolecular Sequence Data
650 0 4 _aPeptides
_xchemistry
650 0 4 _aPhosphoproteins
_xchemistry
650 0 4 _aProtein Conformation
650 0 4 _aProteins
_xchemistry
650 0 4 _aSequence Homology, Amino Acid
650 0 4 _aStructure-Activity Relationship
650 0 4 _aWiskott-Aldrich Syndrome Protein
650 0 4 _aVasodilator-Stimulated Phosphoprotein
700 1 _aLee, D J
700 1 _aLim, W A
773 0 _tCell
_gvol. 97
_gno. 4
_gp. 471-80
856 4 0 _uhttps://doi.org/10.1016/s0092-8674(00)80757-6
_zAvailable from publisher's website
999 _c10296924
_d10296924