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Peptidomimetic inhibitors of N-myristoyltransferase from human malaria and leishmaniasis parasites

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Peptidomimetic inhibitors of N-myristoyltransferase from human malaria and leishmaniasis parasites. / Olaleye, Tayo O.; Brannigan, James A.; Roberts, Shirley M.; Leatherbarrow, Robin J.; Wilkinson, Anthony J.; Tate, Edward W.

In: Organic and Biomolecular Chemistry, Vol. 12, No. 41, 07.11.2014, p. 8132-8137.

Research output: Contribution to journalArticle

Harvard

Olaleye, TO, Brannigan, JA, Roberts, SM, Leatherbarrow, RJ, Wilkinson, AJ & Tate, EW 2014, 'Peptidomimetic inhibitors of N-myristoyltransferase from human malaria and leishmaniasis parasites', Organic and Biomolecular Chemistry, vol. 12, no. 41, pp. 8132-8137. https://doi.org/10.1039/c4ob01669f

APA

Olaleye, T. O., Brannigan, J. A., Roberts, S. M., Leatherbarrow, R. J., Wilkinson, A. J., & Tate, E. W. (2014). Peptidomimetic inhibitors of N-myristoyltransferase from human malaria and leishmaniasis parasites. Organic and Biomolecular Chemistry, 12(41), 8132-8137. https://doi.org/10.1039/c4ob01669f

Vancouver

Olaleye TO, Brannigan JA, Roberts SM, Leatherbarrow RJ, Wilkinson AJ, Tate EW. Peptidomimetic inhibitors of N-myristoyltransferase from human malaria and leishmaniasis parasites. Organic and Biomolecular Chemistry. 2014 Nov 7;12(41):8132-8137. https://doi.org/10.1039/c4ob01669f

Author

Olaleye, Tayo O. ; Brannigan, James A. ; Roberts, Shirley M. ; Leatherbarrow, Robin J. ; Wilkinson, Anthony J. ; Tate, Edward W. / Peptidomimetic inhibitors of N-myristoyltransferase from human malaria and leishmaniasis parasites. In: Organic and Biomolecular Chemistry. 2014 ; Vol. 12, No. 41. pp. 8132-8137.

Bibtex - Download

@article{39152f28bc5b463cbe150c50f2435c76,
title = "Peptidomimetic inhibitors of N-myristoyltransferase from human malaria and leishmaniasis parasites",
abstract = "N-Myristoyltransferase (NMT) has been shown to be essential in Leishmania and subsequently validated as a drug target in Plasmodium. Herein, we discuss the use of antifungal NMT inhibitors as a basis for inhibitor development resulting in the first sub-micromolar peptidomimetic inhibitors of Plasmodium and Leishmania NMTs. High-resolution structures of these inhibitors with Plasmodium and Leishmania NMTs permit a comparative analysis of binding modes, and provide the first crystal structure evidence for a ternary NMT-Coenzyme A/myristoylated peptide product complex. This journal is",
author = "Olaleye, {Tayo O.} and Brannigan, {James A.} and Roberts, {Shirley M.} and Leatherbarrow, {Robin J.} and Wilkinson, {Anthony J.} and Tate, {Edward W.}",
year = "2014",
month = "11",
day = "7",
doi = "10.1039/c4ob01669f",
language = "English",
volume = "12",
pages = "8132--8137",
journal = "Organic and Biomolecular Chemistry",
issn = "1477-0520",
publisher = "The Royal Society of Chemistry",
number = "41",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Peptidomimetic inhibitors of N-myristoyltransferase from human malaria and leishmaniasis parasites

AU - Olaleye, Tayo O.

AU - Brannigan, James A.

AU - Roberts, Shirley M.

AU - Leatherbarrow, Robin J.

AU - Wilkinson, Anthony J.

AU - Tate, Edward W.

PY - 2014/11/7

Y1 - 2014/11/7

N2 - N-Myristoyltransferase (NMT) has been shown to be essential in Leishmania and subsequently validated as a drug target in Plasmodium. Herein, we discuss the use of antifungal NMT inhibitors as a basis for inhibitor development resulting in the first sub-micromolar peptidomimetic inhibitors of Plasmodium and Leishmania NMTs. High-resolution structures of these inhibitors with Plasmodium and Leishmania NMTs permit a comparative analysis of binding modes, and provide the first crystal structure evidence for a ternary NMT-Coenzyme A/myristoylated peptide product complex. This journal is

AB - N-Myristoyltransferase (NMT) has been shown to be essential in Leishmania and subsequently validated as a drug target in Plasmodium. Herein, we discuss the use of antifungal NMT inhibitors as a basis for inhibitor development resulting in the first sub-micromolar peptidomimetic inhibitors of Plasmodium and Leishmania NMTs. High-resolution structures of these inhibitors with Plasmodium and Leishmania NMTs permit a comparative analysis of binding modes, and provide the first crystal structure evidence for a ternary NMT-Coenzyme A/myristoylated peptide product complex. This journal is

UR - http://www.scopus.com/inward/record.url?scp=84907638369&partnerID=8YFLogxK

U2 - 10.1039/c4ob01669f

DO - 10.1039/c4ob01669f

M3 - Article

VL - 12

SP - 8132

EP - 8137

JO - Organic and Biomolecular Chemistry

T2 - Organic and Biomolecular Chemistry

JF - Organic and Biomolecular Chemistry

SN - 1477-0520

IS - 41

ER -