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dc.contributor.authorChonticha Saisawangen_US
dc.contributor.authorPornpan Sillapeeen_US
dc.contributor.authorKwanhathai Sinsirimongkolen_US
dc.contributor.authorSukathida Ubolen_US
dc.contributor.authorDuncan R. Smithen_US
dc.contributor.authorAlbert J. Kettermanen_US
dc.contributor.otherMahidol Universityen_US
dc.identifier.citationBioscience Reports. Vol.35, (2015)en_US
dc.description.abstract© 2015 Authors. Alphavirus nsP2 proteins are multifunctional and essential for viral replication. The protease role of nsP2 is critical for virus replication as only the virus protease activity is used for processing of the viral non-structural polypeptide. Chikungunya virus is an emerging disease problem that is becoming a world-wide health issue. We have generated purified recombinant chikungunya virus nsP2 proteins, both full length and a truncated protease domain from the Cterminus of the nsP2 protein. Enzyme characterization shows that the protease domain alone has different properties compared with the full length nsP2 protease. We also show chikungunya nsP2 protease possesses different substrate specificity to the canonical alphavirus nsP2 polyprotein cleavage specificity. Moreover, the chikungunya nsP2 also appears to differ from other alphavirus nsP2 in its distinctive ability to recognize small peptide substrates.en_US
dc.rightsMahidol Universityen_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleFull length and protease domain activity of chikungunya virus nsP2 differ from other alphavirus nsP2 proteases in recognition of small peptide substratesen_US
Appears in Collections:Scopus 2011-2015

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