Methionine recycling as a target for antiprotozoal drug development

Michael Riscoe, A. J. Ferro, J. H. Fitchen

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

The development of new and effective ontiprotozool drugs has been difficult because of the close metabolic relationship between protozoa and mammalian cells. In this article, Michael Riscoe, Al Ferro and john Fitchen present their hypothesis for chemotherapeutic exploitation of methylthioribose (MTR) kinase, an enzyme critical to methionine salvage in certain protozoa. They propose that analogues of MTR if properly designed, would be converted to toxic products in organisms that contain MTR kinase but not in mammalian cells, which lack this enzyme.

Original languageEnglish (US)
Pages (from-to)330-333
Number of pages4
JournalParasitology Today
Volume5
Issue number10
DOIs
StatePublished - 1989
Externally publishedYes

Fingerprint

Recycling
Methionine
Phosphotransferases
Poisons
Enzymes
Pharmaceutical Preparations

ASJC Scopus subject areas

  • Parasitology

Cite this

Methionine recycling as a target for antiprotozoal drug development. / Riscoe, Michael; Ferro, A. J.; Fitchen, J. H.

In: Parasitology Today, Vol. 5, No. 10, 1989, p. 330-333.

Research output: Contribution to journalArticle

Riscoe, Michael ; Ferro, A. J. ; Fitchen, J. H. / Methionine recycling as a target for antiprotozoal drug development. In: Parasitology Today. 1989 ; Vol. 5, No. 10. pp. 330-333.
@article{ba7f0eab74194589842ff8ad0f28b6b2,
title = "Methionine recycling as a target for antiprotozoal drug development",
abstract = "The development of new and effective ontiprotozool drugs has been difficult because of the close metabolic relationship between protozoa and mammalian cells. In this article, Michael Riscoe, Al Ferro and john Fitchen present their hypothesis for chemotherapeutic exploitation of methylthioribose (MTR) kinase, an enzyme critical to methionine salvage in certain protozoa. They propose that analogues of MTR if properly designed, would be converted to toxic products in organisms that contain MTR kinase but not in mammalian cells, which lack this enzyme.",
author = "Michael Riscoe and Ferro, {A. J.} and Fitchen, {J. H.}",
year = "1989",
doi = "10.1016/0169-4758(89)90128-2",
language = "English (US)",
volume = "5",
pages = "330--333",
journal = "Trends in Parasitology",
issn = "1471-4922",
publisher = "Elsevier Limited",
number = "10",

}

TY - JOUR

T1 - Methionine recycling as a target for antiprotozoal drug development

AU - Riscoe, Michael

AU - Ferro, A. J.

AU - Fitchen, J. H.

PY - 1989

Y1 - 1989

N2 - The development of new and effective ontiprotozool drugs has been difficult because of the close metabolic relationship between protozoa and mammalian cells. In this article, Michael Riscoe, Al Ferro and john Fitchen present their hypothesis for chemotherapeutic exploitation of methylthioribose (MTR) kinase, an enzyme critical to methionine salvage in certain protozoa. They propose that analogues of MTR if properly designed, would be converted to toxic products in organisms that contain MTR kinase but not in mammalian cells, which lack this enzyme.

AB - The development of new and effective ontiprotozool drugs has been difficult because of the close metabolic relationship between protozoa and mammalian cells. In this article, Michael Riscoe, Al Ferro and john Fitchen present their hypothesis for chemotherapeutic exploitation of methylthioribose (MTR) kinase, an enzyme critical to methionine salvage in certain protozoa. They propose that analogues of MTR if properly designed, would be converted to toxic products in organisms that contain MTR kinase but not in mammalian cells, which lack this enzyme.

UR - http://www.scopus.com/inward/record.url?scp=0024416959&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024416959&partnerID=8YFLogxK

U2 - 10.1016/0169-4758(89)90128-2

DO - 10.1016/0169-4758(89)90128-2

M3 - Article

VL - 5

SP - 330

EP - 333

JO - Trends in Parasitology

JF - Trends in Parasitology

SN - 1471-4922

IS - 10

ER -