Replacement of Leishmania N-acetylglucosamine-1-phosphate transferase gene requires episomal rescue

被引：5

作者：

Chen, DQ ^{[1
]}

Lu, HG ^{[1
]}

Chang, KP ^{[1
]}

机构：

[1] Finch Univ Hlth Sci Chicago Med Sch, Dept Microbiol & Immunol, N Chicago, IL 60064 USA

来源：

MOLECULAR AND BIOCHEMICAL PARASITOLOGY | 1999年 / 100卷 / 02期

关键词：

Leishmania; NAGT; knockout mutants;

D O I：

10.1016/S0166-6851(99)00038-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

[No abstract available]

引用

页码：223 / 227

页数：5

共 12 条

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[7] N-ACETYLGLUCOSAMINE-1-PHOSPHATE TRANSFERASE GENE IS CONSERVED IN 5 LEISHMANIA SPP AND OVEREXPRESSED DUE TO ITS AMPLIFICATION IN THEIR TUNICAMYCIN-RESISTANT VARIANTS
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[8] THE 63-KILOBASE CIRCULAR AMPLICON OF TUNICAMYCIN-RESISTANT LEISHMANIA-AMAZONENSIS CONTAINS A FUNCTIONAL N-ACETYLGLUCOSAMINE-1-PHOSPHATE TRANSFERASE GENE THAT CAN BE USED AS A DOMINANT SELECTABLE MARKER IN TRANSFECTION
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[J]. MOLECULAR AND CELLULAR BIOLOGY, 1992, 12 (09) : 4112 - 4122
[9] EXTRACHROMOSOMAL GENETIC COMPLEMENTATION OF SURFACE METALLOPROTEINASE (GP63)-DEFICIENT LEISHMANIA INCREASES THEIR BINDING TO MACROPHAGES
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[10] Posttranslational regulation of a Leishmania HEXXH metalloprotease (gp63) - The effects of site-specific mutagenesis of catalytic, zinc binding, N-glycosylation, and glycosyl phosphatidylinositol addition sites on N-terminal end cleavage, intracellular stability, and extracellular exit
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