ArticleVirology2011
Human polyomavirus JC small regulatory agnoprotein forms highly stable dimers and oligomers: implications for their roles in agnoprotein function.
Article in Virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 26 citations in OpenAlex.
- Recent advances in discovery and functional analysis of the small proteins and microRNA expressed by polyomaviruses.Virology · 2025Review
- Human neurotropic polyomavirus, JC virus, agnoprotein targets mitochondrion and modulates its functions.Virology · 2021Article
- Article
- Expression of novel proteins by polyomaviruses and recent advances in the structural and functional features of agnoprotein of JC virus, BK virus, and simian virus 40.Journal of cellular physiology · 2019Review
- Neuroimmune Regulation of JC Virus by Intracellular and Extracellular Agnoprotein.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2018Article
- Discovery and characterization of novel trans-spliced products of human polyoma JC virus late transcripts from PML patients.Journal of cellular physiology · 2018Article
- Structure-based release analysis of the JC virus agnoprotein regions: A role for the hydrophilic surface of the major alpha helix domain in release.Journal of cellular physiology · 2018Article
- Biology of the BKPyV: An Update.Viruses · 2017Review
- Nuclear Magnetic Resonance Structure of the Human Polyoma JC Virus Agnoprotein.Journal of cellular biochemistry · 2017Article
- Emerging From the Unknown: Structural and Functional Features of Agnoprotein of Polyomaviruses.Journal of cellular physiology · 2016Review
- Oligomerization of the microtubule-associated protein tau is mediated by its N-terminal sequences: implications for normal and pathological tau action.Journal of neurochemistry · 2016Article
- The agnoprotein of polyomavirus JC is released by infected cells: evidence for its cellular uptake by uninfected neighboring cells.Virology · 2014Article
- Nuclear magnetic resonance structure revealed that the human polyomavirus JC virus agnoprotein contains an α-helix encompassing the Leu/Ile/Phe-rich domain.Journal of virology · 2014Article
- Article
- Agnogene deletion in a novel pathogenic JC virus isolate impairs VP1 expression and virion production.PloS one · 2013Article
- Article
- Agnoprotein of mammalian polyomaviruses.Virology · 2012Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
JC virus (JCV) encodes a small basic phosphoprotein from the late coding region called agnoprotein, which has been shown to play important regulatory roles in the viral replication cycle. In this study, we report that agnoprotein forms highly stable dimers and higher order oligomer complexes. This was confirmed by immunoblotting and mass spectrometry studies. These complexes are extremely resistant to strong denaturing agents, including urea and SDS. Central portion of the protein, amino acids spanning from 17 to 42 is important for dimer/oligomer formation. Removal of 17 to 42 aa region from the viral background severely affected the efficiency of the JCV replication. Extracts prepared from JCV-infected cells showed a double banding pattern for agnoprotein in vivo. Collectively, these findings suggest that agnoprotein forms functionally active homodimer/oligomer complexes and these may be important for its function during viral propagation and thus for the progression of PML.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.