Home > Research > Publications & Outputs > Probing enzymes late in the trypanosomal glycos...

Research

Electronic data

  • Urbaniak_ACSChemBiol2008

    Rights statement: ACS Author Choice CC-BY

    Final published version, 5.14 MB, PDF document

    Available under license: CC BY

Links

Text available via DOI:

Keywords

View graph of relations

Probing enzymes late in the trypanosomal glycosylphosphatidylinositol biosynthetic pathway with synthetic glycosylphosphatidylinositol analogues

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Published

Standard

Probing enzymes late in the trypanosomal glycosylphosphatidylinositol biosynthetic pathway with synthetic glycosylphosphatidylinositol analogues. / Urbaniak, Michael D.; Yashunsky, Dmitry V.; Crossman, Arthur et al.
In: ACS Chemical Biology, Vol. 3, No. 10, 17.10.2008, p. 625-634.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Urbaniak, MD, Yashunsky, DV, Crossman, A, Nikolaev, AV & Ferguson, MAJ 2008, 'Probing enzymes late in the trypanosomal glycosylphosphatidylinositol biosynthetic pathway with synthetic glycosylphosphatidylinositol analogues', ACS Chemical Biology, vol. 3, no. 10, pp. 625-634. https://doi.org/10.1021/cb800143w

APA

Urbaniak, M. D., Yashunsky, D. V., Crossman, A., Nikolaev, A. V., & Ferguson, M. A. J. (2008). Probing enzymes late in the trypanosomal glycosylphosphatidylinositol biosynthetic pathway with synthetic glycosylphosphatidylinositol analogues. ACS Chemical Biology, 3(10), 625-634. https://doi.org/10.1021/cb800143w

Vancouver

Urbaniak MD, Yashunsky DV, Crossman A, Nikolaev AV, Ferguson MAJ. Probing enzymes late in the trypanosomal glycosylphosphatidylinositol biosynthetic pathway with synthetic glycosylphosphatidylinositol analogues. ACS Chemical Biology. 2008 Oct 17;3(10):625-634. doi: 10.1021/cb800143w

Author

Urbaniak, Michael D. ; Yashunsky, Dmitry V. ; Crossman, Arthur et al. / Probing enzymes late in the trypanosomal glycosylphosphatidylinositol biosynthetic pathway with synthetic glycosylphosphatidylinositol analogues. In: ACS Chemical Biology. 2008 ; Vol. 3, No. 10. pp. 625-634.

Bibtex

@article{ca9b255a1140492aabe1b9ff3dd956b6,
title = "Probing enzymes late in the trypanosomal glycosylphosphatidylinositol biosynthetic pathway with synthetic glycosylphosphatidylinositol analogues",
abstract = "Glycosylphosphatidylinositol (GPI)-anchored proteins are abundant in the protozoan parasite Trypanosoma brucei, the causative agent of African sleeping sickness in humans and the related disease Nagana in cattle, and disruption of GPI biosynthesis is genetically and chemically validated as a drug target. Here, we examine the ability of enzymes of the trypanosomal GPI biosynthetic pathway to recognize and process a series of synthetic dimannosyl-glucosaminylphosphatidylinositol analogues containing systematic modifications on the mannose residues. The data reveal which portions of the natural substrate are important for recognition, explain why mannosylation occurs prior to inositol acylation in the trypanosomal pathway, and identify the first inhibitor of the third alpha-mannosyltransferase of the GPI biosynthetic pathway.",
keywords = "Animals, Enzyme Inhibitors, Glycosylphosphatidylinositols, Humans, Mannosyltransferases, Trypanocidal Agents, Trypanosoma brucei brucei, Trypanosomiasis, African",
author = "Urbaniak, {Michael D.} and Yashunsky, {Dmitry V.} and Arthur Crossman and Nikolaev, {Andrei V.} and Ferguson, {Michael A. J.}",
note = "ACS Author Choice CC-BY",
year = "2008",
month = oct,
day = "17",
doi = "10.1021/cb800143w",
language = "English",
volume = "3",
pages = "625--634",
journal = "ACS Chemical Biology",
issn = "1554-8929",
publisher = "American Chemical Society",
number = "10",

}

RIS

TY - JOUR

T1 - Probing enzymes late in the trypanosomal glycosylphosphatidylinositol biosynthetic pathway with synthetic glycosylphosphatidylinositol analogues

AU - Urbaniak, Michael D.

AU - Yashunsky, Dmitry V.

AU - Crossman, Arthur

AU - Nikolaev, Andrei V.

AU - Ferguson, Michael A. J.

N1 - ACS Author Choice CC-BY

PY - 2008/10/17

Y1 - 2008/10/17

N2 - Glycosylphosphatidylinositol (GPI)-anchored proteins are abundant in the protozoan parasite Trypanosoma brucei, the causative agent of African sleeping sickness in humans and the related disease Nagana in cattle, and disruption of GPI biosynthesis is genetically and chemically validated as a drug target. Here, we examine the ability of enzymes of the trypanosomal GPI biosynthetic pathway to recognize and process a series of synthetic dimannosyl-glucosaminylphosphatidylinositol analogues containing systematic modifications on the mannose residues. The data reveal which portions of the natural substrate are important for recognition, explain why mannosylation occurs prior to inositol acylation in the trypanosomal pathway, and identify the first inhibitor of the third alpha-mannosyltransferase of the GPI biosynthetic pathway.

AB - Glycosylphosphatidylinositol (GPI)-anchored proteins are abundant in the protozoan parasite Trypanosoma brucei, the causative agent of African sleeping sickness in humans and the related disease Nagana in cattle, and disruption of GPI biosynthesis is genetically and chemically validated as a drug target. Here, we examine the ability of enzymes of the trypanosomal GPI biosynthetic pathway to recognize and process a series of synthetic dimannosyl-glucosaminylphosphatidylinositol analogues containing systematic modifications on the mannose residues. The data reveal which portions of the natural substrate are important for recognition, explain why mannosylation occurs prior to inositol acylation in the trypanosomal pathway, and identify the first inhibitor of the third alpha-mannosyltransferase of the GPI biosynthetic pathway.

KW - Animals

KW - Enzyme Inhibitors

KW - Glycosylphosphatidylinositols

KW - Humans

KW - Mannosyltransferases

KW - Trypanocidal Agents

KW - Trypanosoma brucei brucei

KW - Trypanosomiasis, African

U2 - 10.1021/cb800143w

DO - 10.1021/cb800143w

M3 - Journal article

C2 - 18928250

VL - 3

SP - 625

EP - 634

JO - ACS Chemical Biology

JF - ACS Chemical Biology

SN - 1554-8929

IS - 10

ER -