Structural Characterization of an Intrinsically Unfolded Mini-HBX Protein from Hepatitis B Virus
Open Access
- 1 August 2012
- journal article
- Published by Elsevier in Molecules and Cells
- Vol. 34 (2) , 165-170
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Understanding protein non-foldingBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2010
- NF-κB signaling mediates the induction of MTA1 by hepatitis B virus transactivator protein HBxOncogene, 2009
- High‐level expression and large‐scale preparation of soluble HBx antigen from Escherichia coliBiotechnology and Applied Biochemistry, 2009
- Structural Polymorphism of 441-Residue Tau at Single Residue ResolutionPLOS Biology, 2009
- Intrinsically Disordered Proteins in Human Diseases: Introducing the D2ConceptAnnual Review of Biophysics, 2008
- Pre‐structured motifs in the natively unstructured preS1 surface antigen of hepatitis B virusProtein Science, 2007
- IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy contentBioinformatics, 2005
- The cysteine residues of the hepatitis B virus onco-protein HBx are not required for its interaction with RNA or with human p53Virus Research, 2005
- Expression of deletion mutants of the hepatitis B virus protein HBx in E. coli and characterization of their RNA binding activitiesVirus Research, 2001
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995