000			02156 a2200577 4500
005			20250516101539.0
264		0	_c20130426
008			201304s 0 0 eng d
022			_a1477-9137
024	7		_a10.1242/jcs.106963 _2doi
040			_aNLM _beng _cNLM
100	1		_aIsabelle, Maxim
245	0	0	_aQuantitative proteomics and dynamic imaging reveal that G3BP-mediated stress granule assembly is poly(ADP-ribose)-dependent following exposure to MNNG-induced DNA alkylation. _h[electronic resource]
260			_bJournal of cell science _cOct 2012
300			_a4555-66 p. _bdigital
500			_aPublication Type: Journal Article; Research Support, Non-U.S. Gov't
650	0	4	_aAlkylation _xdrug effects
650	0	4	_aAmino Acid Sequence
650	0	4	_aBlotting, Western
650	0	4	_aCarrier Proteins _xchemistry
650	0	4	_aCluster Analysis
650	0	4	_aCytoplasmic Granules _xdrug effects
650	0	4	_aDNA _xmetabolism
650	0	4	_aDNA Damage
650	0	4	_aDNA Helicases
650	0	4	_aFatty Acids, Unsaturated _xpharmacology
650	0	4	_aGreen Fluorescent Proteins _xmetabolism
650	0	4	_aHeLa Cells
650	0	4	_aHumans
650	0	4	_aImaging, Three-Dimensional _xmethods
650	0	4	_aIsotope Labeling
650	0	4	_aMethylnitronitrosoguanidine _xpharmacology
650	0	4	_aMolecular Sequence Data
650	0	4	_aPoly Adenosine Diphosphate Ribose _xmetabolism
650	0	4	_aPoly-ADP-Ribose Binding Proteins
650	0	4	_aProtein Binding _xdrug effects
650	0	4	_aProtein Structure, Tertiary
650	0	4	_aProtein Transport _xdrug effects
650	0	4	_aProteomics _xmethods
650	0	4	_aRNA Helicases
650	0	4	_aRNA Recognition Motif Proteins
650	0	4	_aReproducibility of Results
650	0	4	_aStress, Physiological _xdrug effects
650	0	4	_aSubcellular Fractions _xdrug effects
650	0	4	_aTime Factors
700	1		_aGagné, Jean-Philippe
700	1		_aGallouzi, Imed-Eddine
700	1		_aPoirier, Guy G
773	0		_tJournal of cell science _gvol. 125 _gno. Pt 19 _gp. 4555-66
856	4	0	_uhttps://doi.org/10.1242/jcs.106963 _zAvailable from publisher's website
999			_c21922477 _d21922477