@article { ISI:000297606200009,
	title = {Comparative and chemical proteomic approaches reveal gatifloxacin deregulates enzymes involved in glucose metabolism},
	journal = {Journal of Toxicological Sciences},
	volume = {36},
	number = {6},
	year = {2011},
	month = {DEC},
	pages = {787-796},
	publisher = {JAPANESE SOC TOXICOLOGICAL SCIENCES},
	address = {INTERNATIONAL MEDICAL INFORMATION CENTER, SHINANOMACHI RENGAKAN, 35 SHINANO-MACHI, SHINJUKU-KU, TOKYO, 160-0016, JAPAN},
	abstract = {<p>Gatifloxacin has been associated with increased risks of hypoglycemic and hyperglycemic side effects. In order to understand the molecular mechanism of gatifloxacin induced deregulation of glucose metabolism, a Combination of comparative and chemical proteomic approaches were employed using yeast as a model system. Differential protein expression studies using two dimensional electrophoresis and mass spectrometry reveal that gatifloxacin deregulates the expression of key enzymes involved in glucose metabolism. Furthermore, affinity chromatography and LC-MSE analysis led to identification of enolase, as one of the key gatifloxacin binding proteins. Fluorescence spectrometric studies confirmed that the gatifloxacin indeed binds to enolase. Role of enolase in regulation of gatifloxacin induced dysglycemic effect is discussed.</p>},
	keywords = {antibiotics, Differential protein expression, Fluoroquinolone, Glycolysis, Yeast},
	issn = {0388-1350},
	doi = {10.2131/jts.36.787},
	author = {Suresh, Kesavan K. and Bhosale, Santosh D. and Thulasiram, Hirekodathakallu V. and Kulkarni, Mahesh J.}
}
@article {46380,
	title = {Crystal engineering principles: fluoroquinolone salts},
	journal = {Acta Crystallographica A-Foundation and Advances},
	volume = {70},
	year = {2014},
	month = {APR},
	pages = {C413},
	type = {Meeting Abstract},
	keywords = {ciprofloxacin, Fluoroquinolone, norfloxacin},
	issn = {2053-2733},
	author = {Dandela, Rambabu and Nangia, Ashwini}
}
