@article {4448,
	title = {A phosphinate inhibitor of the meso-diaminopimelic acid-adding enzyme (MurE) of peptidoglycan biosynthesis},
	journal = {Journal of Organic Chemistry},
	volume = {63},
	number = {26},
	year = {1998},
	note = {ISI Document Delivery No.: 153LPTimes Cited: 37Cited Reference Count: 50},
	month = {Dec},
	pages = {10081-10085},
	type = {Article},
	keywords = {AMINO-ACIDS, COLI GLUTAMINE-SYNTHETASE, D-ALANINE LIGASE, ESCHERICHIA-COLI, GLUTATHIONE SYNTHETASE, INACTIVATION, KINETIC MECHANISM, MECHANISM-BASED, N-ACETYLMURAMATE, RAPID-QUENCH, VANCOMYCIN RESISTANCE},
	isbn = {0022-3263},
	url = {<Go to ISI>://000077834800087},
	author = {Zeng, B. Q. and Kwong, K. and Pompliano, D. L. and Reddy, S. and Tanner, M. E.}
}
@article {3832,
	title = {Phosphinate inhibitors of the D-glutamic acid-adding enzyme of peptidoglycan biosynthesis},
	journal = {Journal of Organic Chemistry},
	volume = {61},
	number = {5},
	year = {1996},
	note = {ISI Document Delivery No.: TZ997Times Cited: 66Cited Reference Count: 31},
	month = {Mar},
	pages = {1756-1760},
	type = {Article},
	abstract = {We report the synthesis and initial evaluation of the first effective inhibitors of the D-glutamic acid-adding enzyme (UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase or MurD). This enzyme plays a key role in bacterial peptidoglycan biosynthesis and is therefore a target for antibiotic design. Phosphinic acid 3 is a dipeptide analog linked to uridine diphosphate by a hydrophobic spacer. It is a good inhibitor of the enzyme (IC50 = 0.68 mu M) as it closely resembles the tetrahedral intermediate that is presumed to form in the ligation reaction. Compound 4 lacks the terminal UMP group, and compound 5 lacks both the linker and UDP functionalities. These are less effective inhibitors of the enzyme with IC50 values of 29 mu M and > 1 mM, respectively. Preincubation of the enzyme in the presence of inhibitor 3 and ATP does not result in irreversible inhibition or in the formation of a slowly decomplexing species, suggesting that the phosphinic acid is not phosphorylated in the active site.},
	keywords = {(AMINOALKYL)PHOSPHINATE, ATP, D-ALANINE LIGASE, ESCHERICHIA-COLI, INACTIVATION, MECHANISM, PHOSPHINOTHRICIN, PURIFICATION, RAPID-QUENCH, SYNTHETASE},
	isbn = {0022-3263},
	url = {<Go to ISI>://A1996TZ99700030},
	author = {Tanner, M. E. and Vaganay, S. and vanHeijenoort, J. and Blanot, D.}
}
@article {3017,
	title = {1993 SYNTEX-AWARD LECTURE - PHOTOMEDICINE AND PHOTODYNAMIC THERAPY},
	journal = {Canadian Journal of Chemistry-Revue Canadienne De Chimie},
	volume = {72},
	number = {4},
	year = {1994},
	note = {ISI Document Delivery No.: NN830Times Cited: 84Cited Reference Count: 47},
	month = {Apr},
	pages = {1005-1013},
	type = {Article},
	abstract = {Photodynamic therapy (PDT) involves the treatment of diseased tissue and cells using a photosensitizer and visible light. Such photomedical treatments have been known since the time of the ancient Egyptians but it was only just this year that this therapeutic modality was made available to modern medicine with the approval, in Canada, of Photofrin(R) for the treatment of bladder cancer. This paper reviews PDT with an emphasis on drug development, particulary for the second generation drugs, especially BPDMA (benzoporphyrin derivative-mono acid), which is now in human clinical trials.},
	keywords = {BENZOPORPHYRIN DERIVATIVES, CELLS, HEMATOPORPHYRIN, INACTIVATION, MICE, PHOTOSENSITIZATION, PLASMA-LIPOPROTEINS, porphyrins, PROTEIN DAMAGE, PROTOPORPHYRIN},
	isbn = {0008-4042},
	url = {<Go to ISI>://A1994NN83000001},
	author = {Dolphin, D.}
}
@article {3114,
	title = {IN-VIVO INHIBITION OF BETA-GLUCOSIDASE AND BETA-MANNOSIDASE ACTIVITY IN RATS BY 2-DEOXY-2-FLUORO-BETA-GLYCOSYL FLUORIDES AND RECOVERY OF ACTIVITY IN-VIVO AND IN-VITRO},
	journal = {Biochemical Journal},
	volume = {301},
	year = {1994},
	note = {ISI Document Delivery No.: PA559Times Cited: 12Cited Reference Count: 25Part 2},
	month = {Jul},
	pages = {343-348},
	type = {Article},
	abstract = {2-Deoxy-2-fluoro-beta-glucosyl and -beta-mannosyl fluorides administered to rats in a single dose(10 mg/kg) inhibited beta-glucosidase and beta-mannosidase activity respectively after 1 h in brain, spleen, liver and kidney tissues. This inhibition, presumably caused by accumulation of 2-deoxy-2-fluoroglycosyl-enzyme intermediates, indicates that intact 2-deoxy-2-fluoroglycosyl fluorides are distributed to these organs and, in the case of brain, that they cross the blood/brain barrier. beta-Glucosidase activity recovered completely or partially in brain, spleen, liver and kidney by 20-48 h. beta-Mannosidase activity partially recovered in all tissues by 48 h. beta-Galactosidase activity in brain and kidney was not significantly affected by administration of either the gluco or manno compounds at this dosage, indicating that these inhibitors are directed towards specific glycosidases. Observation of similar relatively rapid rates of beta-glycosidase re-activation in vivo and in tissue homogenates in vitro at 37 degrees C suggests that hydrolysis or transglycosylation of 2-deoxy-2-fluoroglycosyl-enzymes, not protein synthesis, are the primary mechanisms involved in the recovery of glycosidase activity inhibited by this class of compounds in vivo.},
	keywords = {DEFICIENCY, ENZYME INTERMEDIATE, FORMS, GLUCOCEREBROSIDASE, GLYCOSIDASES, INACTIVATION, LIVER, MICE},
	isbn = {0264-6021},
	url = {<Go to ISI>://A1994PA55900006},
	author = {McCarter, J. D. and Adam,Michael J. and Hartman, N. G. and Withers, S. G.}
}
