Structure-based release analysis of the JC virus agnoprotein regions: A role for the hydrophilic surface of the major alpha helix domain in release

Author:

Saribas A. Sami1,White Martyn K.1,Safak Mahmut1ORCID

Affiliation:

1. Laboratory of Molecular Neurovirology, Department of Neuroscience; Lewis Katz School of Medicine at Temple University; Philadelphia Pennsylvania

Funder

Temple University Drug Discovery Initiative

National Institute of Neurological Disorders and Stroke

Publisher

Wiley

Subject

Cell Biology,Clinical Biochemistry,Physiology

Reference58 articles.

1. Human polyomavirus JCV late leader peptide region contains important regulatory elements;Akan;Virology,2006

2. Blockade of chemokine activity by a soluble chemokine binding protein from vaccinia virus;Alcami;The Journal of Immunology,1998

3. Vaccinia virus complement control protein is capable of protecting xenoendothelial cells from antibody binding and killing by human complement and cytotoxic cells;Al-Mohanna;Transplantation,2001

4. Vaccinia virus complement control protein inhibits hyperacute xenorejection;Anderson;Transplantation Proceedings,2002

5. The basis for modeling progressive multifocal leukoencephalopathy pathogenesis;Berger;Current Opinion in Neurology,2011

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