ArticleGenes & development1999
Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16.
Article in Genes & development, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
29 citing papers in PubMed, 58 citations in OpenAlex.
- Co-Regulation Mechanism of Host p53 and Fos in Transcriptional Activation of ILTV Immediate-Early GeneMicroorganisms · 2024Article
- Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression.Communications biology · 2022Article
- Host factors associated with either VP16 or VP16-induced complex differentially affect HSV-1 lytic infection.Reviews in medical virology · 2022Review
- The Role of Pyrazolopyridine Derivatives on Different Steps of Herpes Simplex Virus Type-1International journal of molecular sciences · 2022Article
- Antimicrobial Peptides: An Update on Classifications and Databases.International journal of molecular sciences · 2021Review
- Aptamers in Virology-A Consolidated Review of the Most Recent Advancements in Diagnosis and Therapy.Pharmaceutics · 2021Review
- Article
- Single-cell RNA-sequencing analysis identifies host long noncoding RNA MAMDC2-AS1 as a co-factor for HSV-1 nuclear transport.International journal of biological sciences · 2020Article
- The Role of VP16 in the Life Cycle of Alphaherpesviruses.Frontiers in microbiology · 2020Review
- Heat-shock protein 90α is involved in maintaining the stability of VP16 and VP16-mediated transactivation of α genes from herpes simplex virus-1.Molecular medicine (Cambridge, Mass.) · 2018Article
- A comparison of herpes simplex virus type 1 and varicella-zoster virus latency and reactivation.The Journal of general virology · 2015Review
- Proteomic analysis of the herpes simplex virus 1 virion protein 16 transactivator protein in infected cells.Proteomics · 2015Article
- Biologically active and antimicrobial peptides from plants.BioMed research international · 2015Review
- Crystal structure of the herpesvirus inner tegument protein UL37 supports its essential role in control of viral trafficking.Journal of virology · 2014Article
- Antimicrobial peptides.Pharmaceuticals (Basel, Switzerland) · 2013Article
- Herpes simplex virus 1-encoded tegument protein VP16 abrogates the production of beta interferon (IFN) by inhibiting NF-κB activation and blocking IFN regulatory factor 3 to recruit its coactivator CBP.Journal of virology · 2013Article
- Octamer-binding transcription factors: genomics and functions.Frontiers in bioscience (Landmark edition) · 2013Review
- Analysis of the interaction between the essential herpes simplex virus 1 tegument proteins VP16 and VP1/2.Journal of virology · 2012Article
- Structure and VP16 binding of the Mediator Med25 activator interaction domain.Nature structural & molecular biology · 2011Article
- The major determinant for addition of tegument protein pUL48 (VP16) to capsids in herpes simplex virus type 1 is the presence of the major tegument protein pUL36 (VP1/2).Journal of virology · 2010Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
Abstract
On infection, the herpes simplex virus (HSV) virion protein VP16 (Vmw65; alphaTIF) forms a transcriptional regulatory complex-the VP16-induced complex-with two cellular proteins, HCF and Oct-1, on VP16-responsive cis-regulatory elements in HSV immediate-early promoters called TAATGARAT. Comparison of different HSV VP16 sequences reveals a conserved core region that is sufficient for VP16-induced complex formation. The crystal structure of the VP16 core has been determined at 2.1 A resolution. The results reveal a novel, seat-like protein structure. Together with the activity of mutant VP16 proteins, the structure of free VP16 suggests that it contains (1) a disordered carboxy-terminal region that associates with HCF, Oct-1, and DNA in the VP16-induced complex, and (2) a structured region involved in virion assembly and possessing a novel DNA-binding surface that differentiates among TAATGARAT VP16-response elements.
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Registered trials
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.