Dimerization of the hepatitis C virus nonstructural protein 4B depends on the integrity of an aminoterminal basic leucine zipper

The hepatitis C virus (HCV) nonstructural (NS) protein 4B is known for protein–protein interactions with virus and host cell factors. Only little is known about the corresponding protein binding sites and underlying molecular mechanisms. Recently, we have predicted a putative basic leucine zipper (b...

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Main Authors: Welker, Martin-Walter, Welsch, Christoph, Meyer, Aline, Antes, Iris, Albrecht, Mario, Forestier, Nicole, Kronenberger, Bernd, Lengauer, Thomas, Piiper, Albrecht, Zeuzem, Stefan, Sarrazin, Christoph
Format: Artigo
Language:Inglês
Published: Wiley Subscription Services, Inc., A Wiley Company 2010
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Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC2974824/
https://ncbi.nlm.nih.gov/pubmed/20506268
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.409
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