000			01669 a2200445 4500
005			20250516133535.0
264		0	_c20131022
008			201310s 0 0 eng d
022			_a1471-2180
024	7		_a10.1186/1471-2180-13-26 _2doi
040			_aNLM _beng _cNLM
100	1		_aShin, Jae Yen
245	0	0	_aGlutamate 83 and arginine 85 of helix H3 bend are key residues for FtsZ polymerization, GTPase activity and cellular viability of Escherichia coli: lateral mutations affect FtsZ polymerization and E. coli viability. _h[electronic resource]
260			_bBMC microbiology _cFeb 2013
300			_a26 p. _bdigital
500			_aPublication Type: Journal Article; Research Support, Non-U.S. Gov't
650	0	4	_aAmino Acid Sequence
650	0	4	_aArginine _xgenetics
650	0	4	_aBacterial Proteins _xgenetics
650	0	4	_aCell Cycle Proteins _xgenetics
650	0	4	_aCell Division
650	0	4	_aCytoskeletal Proteins _xgenetics
650	0	4	_aEscherichia coli _xenzymology
650	0	4	_aGTP Phosphohydrolases _xmetabolism
650	0	4	_aGlutamic Acid _xgenetics
650	0	4	_aMicrobial Viability
650	0	4	_aModels, Molecular
650	0	4	_aMolecular Sequence Data
650	0	4	_aMutant Proteins _xgenetics
650	0	4	_aMutation, Missense
650	0	4	_aProtein Binding
650	0	4	_aProtein Conformation
650	0	4	_aProtein Interaction Mapping
650	0	4	_aProtein Multimerization
700	1		_aVollmer, Waldemar
700	1		_aLagos, Rosalba
700	1		_aMonasterio, Octavio
773	0		_tBMC microbiology _gvol. 13 _gp. 26
856	4	0	_uhttps://doi.org/10.1186/1471-2180-13-26 _zAvailable from publisher's website
999			_c22480267 _d22480267