Title : HSP90 Chaperoning in Addition to Phosphoprotein Required for Folding but Not for Supporting Enzymatic Activities of Measles and Nipah Virus L Polymerases.

Pub. Date : 2016 Aug 1

PMID : 27170753






2 Functional Relationships(s)
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1 By using NVP-AUY922 and/or 17-dimethylaminoethylamino-17-demethoxygeldanamycin as specific inhibitors of cellular heat shock protein 90 (HSP90), we found that efficient chaperoning of L by HSP90 requires P in the measles, Nipah, and vesicular stomatitis viruses. 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin heat shock protein 90 alpha family class A member 1 Homo sapiens
2 By using NVP-AUY922 and/or 17-dimethylaminoethylamino-17-demethoxygeldanamycin as specific inhibitors of cellular heat shock protein 90 (HSP90), we found that efficient chaperoning of L by HSP90 requires P in the measles, Nipah, and vesicular stomatitis viruses. 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin heat shock protein 90 alpha family class A member 1 Homo sapiens