ArticleThe Journal of biological chemistry2008
Analysis of a membrane interacting region of herpes simplex virus type 1 glycoprotein H.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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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
30 citing papers in PubMed, 56 citations in OpenAlex.
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- Synergistic Cancer Metabolic Therapy via Co-Delivery of 3-Bromopyruvate and Temozolomide with a Supramolecular Shuttle.ACS applied materials & interfaces · 2025Article
- Review
- Association Mechanism of Peptide-Coated Metal Nanoparticles with Model Membranes: A Coarse-Grained Study.Journal of chemical theory and computation · 2021Article
- Peptides and Dendrimers: How to Combat Viral and Bacterial Infections.Pharmaceutics · 2021Review
- Stunning symmetries involved in the self-assembly of the HSV-1 capsid.The journal of the Korean Physical Society · 2021Review
- Enhanced uptake of gH625 by blood brain barrier compared to liver in vivo: characterization of the mechanism by an in vitro model and implications for delivery.Scientific reports · 2018Article
- Infectivity inhibition by overlapping synthetic peptides derived from the gH/gL heterodimer of herpes simplex virus type 1.Journal of peptide science : an official publication of the European Peptide Society · 2017Article
- Review
- Liposome armed with herpes virus-derived gH625 peptide to overcome doxorubicin resistance in lung adenocarcinoma cell lines.Oncotarget · 2016Article
- Membranotropic Cell Penetrating Peptides: The Outstanding Journey.International journal of molecular sciences · 2015Review
- Dissociation of HSV gL from gH by αvβ6- or αvβ8-integrin promotes gH activation and virus entry.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- gH625: a milestone in understanding the many roles of membranotropic peptides.Biochimica et biophysica acta · 2015Review
- Peptide gH625 enters into neuron and astrocyte cell lines and crosses the blood-brain barrier in rats.International journal of nanomedicine · 2015Article
- Exploitation of viral properties for intracellular delivery.Journal of peptide science : an official publication of the European Peptide Society · 2014Review
- Elucidation of the interaction mechanism with liposomes of gH625-peptide functionalized dendrimers.PloS one · 2014Article
- Peptide-lipid interactions: experiments and applications.International journal of molecular sciences · 2013Article
- Interaction domain of glycoproteins gB and gH of Marek's disease virus and identification of an antiviral peptide with dual functions.PloS one · 2013Article
- gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins.International journal of nanomedicine · 2013Article
- Dendrimers functionalized with membrane-interacting peptides for viral inhibition.International journal of nanomedicine · 2013Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycoprotein H (gH) of herpes simplex virus type I (HSV-1) is involved in the complex mechanism of membrane fusion of the viral envelope with the host cell. Membrane interacting regions and potential fusion peptides have been identified in HSV-1 gH as well as glycoprotein B (gB). Because of the complex fusion mechanism of HSV-1, which requires four viral glycoproteins, and because there are only structural data for gB and glycoprotein D, many questions regarding the mechanism by which HSV-1 fuses its envelope with the host cell membrane remain unresolved. Previous studies have shown that peptides derived from certain regions of gH have the potential to interact with membranes, and based on these findings we have generated a set of peptides containing mutations in one of these domains, gH-(626-644), to investigate further the functional role of this region. Using a combination of biochemical, spectroscopic, and nuclear magnetic resonance techniques, we showed that the alpha-helical nature of this stretch of amino acids in gH is important for membrane interaction and that the aromatic residues, tryptophan and tyrosine, are critical for induction of fusion.
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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.