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Analysis of protein palmitoylation reveals a pervasive role in Plasmodium development and pathogenesis.


ABSTRACT: PRIDE ID: 17889. Data published as part of Cell Host Microbe. 2012 Aug 16;12(2):246-58 [[http://www.ncbi.nlm.nih.gov/pubmed/22901544 PubMed]]. From the Abstract: {{i}} ... sing complementary palmitoyl protein purification approaches and quantitative mass spectrometry, we examined protein palmitoylation in asexual-stage P. falciparum parasites and identified over 400 palmitoylated proteins, including those involved in cytoadherence, drug resistance, signaling, development, and invasion ...{{/i}}

INSTRUMENT(S): Instrument

ORGANISM(S): Human, Plasmodium_falciparum_refseq

DISEASE(S): Not Available

SUBMITTER: Jones ML, et al.  

PROVIDER: GPM11210004611 | GPMDB |

REPOSITORIES: GPMDB

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Analysis of protein palmitoylation reveals a pervasive role in Plasmodium development and pathogenesis.

Jones Matthew L ML   Collins Mark O MO   Goulding David D   Choudhary Jyoti S JS   Rayner Julian C JC  

Cell host & microbe 20120801 2


Asexual stage Plasmodium falciparum replicates and undergoes a tightly regulated developmental process in human erythrocytes. One mechanism involved in the regulation of this process is posttranslational modification (PTM) of parasite proteins. Palmitoylation is a PTM in which cysteine residues undergo a reversible lipid modification, which can regulate target proteins in diverse ways. Using complementary palmitoyl protein purification approaches and quantitative mass spectrometry, we examined p  ...[more]

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