Extracellular Toxoplasma gondii tachyzoites metabolize and incorporate unnatural sugars into cellular proteins.

scientific article published on 11 December 2015

Extracellular Toxoplasma gondii tachyzoites metabolize and incorporate unnatural sugars into cellular proteins. is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1016/J.MICINF.2015.11.004
P932PMC publication ID5337115
P698PubMed publication ID26687036

P50authorJennifer A PrescherQ67221954
Krysten A JonesQ83942089
Naomi S MorrissetteQ87723648
P2093author name stringLidia A Nazarova
Roxanna J Ochoa
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Probing glycosyltransferase activities with the Staudinger ligationQ44716470
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High-level expression of the Toxoplasma gondii STT3 gene is required for suppression of the yeast STT3 gene mutation.Q54485097
A family of glycolipids from Toxoplasma gondii. Identification of candidate glycolipid precursor(s) for Toxoplasma gondii glycosylphosphatidylinositol membrane anchorsQ68056838
Effects of extracellular potassium on acid release and motility initiation in Toxoplasma gondiiQ69402867
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Highly polymorphic family of glycosylphosphatidylinositol-anchored surface antigens with evidence of developmental regulation in Toxoplasma gondii.Q31133187
O-glycosylation in Toxoplasma gondii: identification and analysis of a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferasesQ33198875
Proteomics and glycomics analyses of N-glycosylated structures involved in Toxoplasma gondii--host cell interactionsQ33314196
Targeted metabolic labeling of yeast N-glycans with unnatural sugarsQ33733096
The surface of Toxoplasma tachyzoites is dominated by a family of glycosylphosphatidylinositol-anchored antigens related to SAG1.Q33753940
ToxoDB: accessing the Toxoplasma gondii genomeQ33963616
HSP60 is transported through the secretory pathway of 3-MCA-induced fibrosarcoma tumour cells and undergoes N-glycosylationQ34225839
Surface antigens of Toxoplasma gondii: variations on a themeQ34375964
Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1Q35002612
A chemical approach for identifying O-GlcNAc-modified proteins in cellsQ35242785
Unusual N-glycan structures required for trafficking Toxoplasma gondii GAP50 to the inner membrane complex regulate host cell entry through parasite motilityQ35264695
The Skp1 protein from Toxoplasma is modified by a cytoplasmic prolyl 4-hydroxylase associated with oxygen sensing in the social amoeba DictyosteliumQ36127067
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Detection of cytoplasmic glycosylation associated with hydroxyprolineQ36667150
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Analysis of the glycoproteome of Toxoplasma gondii using lectin affinity chromatography and tandem mass spectrometryQ39517645
Direct evidence of O-GlcNAcylation in the apicomplexan Toxoplasma gondii: a biochemical and bioinformatic studyQ39675387
The dual origin of Toxoplasma gondii N-glycansQ39922809
Identification of new O-GlcNAc modified proteins using a click-chemistry-based taggingQ39998103
P4510describes a project that usesImageJQ1659584
P433issue3
P921main subjectToxoplasma gondiiQ131003
P304page(s)199-210
P577publication date2015-12-11
P1433published inMicrobes and InfectionQ15760242
P1476titleExtracellular Toxoplasma gondii tachyzoites metabolize and incorporate unnatural sugars into cellular proteins
P478volume18

Reverse relations

cites work (P2860)
Q58735681Apart From Rhoptries, Identification of -GlcNAcylated Proteins Reinforces the Universality of the -GlcNAcome
Q38964632Reexamining Chronic Toxoplasma gondii Infection: Surprising Activity for a "Dormant" Parasite
Q92381191Stage-Specific and Selective Delivery of Caged Azidosugars into the Intracellular Parasite Toxoplasma gondii by Using an Esterase-Ester Pair Technique

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