On the public citation graph
A pivotal role of serine 225 phosphorylation in the function of hepatitis C virus NS5A revealed with the application of a phosphopeptide antiserum and super-resolution microscopy
0 signed · 59 inferred · view as graph
Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.
Is this your work? Sign in with ORCID and put your name on the
claims that are yours.
Reference health. See whether every reference in this work resolves to a
known work and none has been retracted — and get a dated CiteStamped
badge you can embed.
What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/dvdy.22019openalex-snapshot
Regulation of Wnt/β‐catenin signaling by protein kinases
inferredcites →https://doi.org/10.1002/pro.2456openalex-snapshot
The crystal structure of NS5A domain 1 from genotype 1a reveals new clues to the mechanism of action for dimeric HCV inhibitors
inferredcites →https://doi.org/10.1016/j.bbalip.2017.07.009openalex-snapshot
The perilipin family of lipid droplet proteins: Gatekeepers of intracellular lipolysis
inferredcites →https://doi.org/10.1016/j.chom.2009.03.007openalex-snapshot
Composition and Three-Dimensional Architecture of the Dengue Virus Replication and Assembly Sites
inferredcites →https://doi.org/10.1016/j.jmb.2012.04.023openalex-snapshot
Transient Structure and SH3 Interaction Sites in an Intrinsically Disordered Fragment of the Hepatitis C Virus Protein NS5A
inferredcites →https://doi.org/10.1016/j.virol.2007.01.042openalex-snapshot
Phosphorylation of hepatitis C virus NS5A nonstructural protein: A new paradigm for phosphorylation-dependent viral RNA replication?
inferredcites →https://doi.org/10.1016/j.virol.2011.03.026openalex-snapshot
The hepatitis C virus NS5A inhibitor (BMS-790052) alters the subcellular localization of the NS5A non-structural viral protein
inferredcites →https://doi.org/10.1016/j.virol.2014.12.018openalex-snapshot
Daclatasvir inhibits hepatitis C virus NS5A motility and hyper-accumulation of phosphoinositides
inferredcites →https://doi.org/10.1016/s0021-9258(18)77295-5openalex-snapshot
Phosphate groups as substrate determinants for casein kinase I action.
inferredcites →https://doi.org/10.1038/nature03580openalex-snapshot
Structure of the zinc-binding domain of an essential component of the hepatitis C virus replicase
inferredcites →https://doi.org/10.1038/nature04078openalex-snapshot
Evasion of intracellular host defence by hepatitis C virus
inferredcites →https://doi.org/10.1038/nbt.3625openalex-snapshot
Protein-retention expansion microscopy of cells and tissues labeled using standard fluorescent proteins and antibodies
inferredcites →https://doi.org/10.1038/nbt.3892openalex-snapshot
Nanoscale imaging of clinical specimens using pathology-optimized expansion microscopy
inferredcites →https://doi.org/10.1038/ncb1631openalex-snapshot
The lipid droplet is an important organelle for hepatitis C virus production
inferredcites →https://doi.org/10.1038/nm.3248openalex-snapshot
Understanding the hepatitis C virus life cycle paves the way for highly effective therapies
inferredcites →https://doi.org/10.1038/nm1268openalex-snapshot
Production of infectious hepatitis C virus in tissue culture from a cloned viral genome
inferredcites →https://doi.org/10.1038/nprot.2006.209openalex-snapshot
A general user interface for prediction servers of proteins' post-translational modification sites
inferredcites →https://doi.org/10.1038/s41598-017-02648-6openalex-snapshot
Glycogen synthase kinase 3β inhibitors prevent hepatitis C virus release/assembly through perturbation of lipid metabolism
inferredcites →https://doi.org/10.1046/j.1365-2893.1999.00004.xopenalex-snapshot
Hepatitis C virus (HCV) NS5A protein: role in HCV replication and resistance to interferon‐α
inferredcites →https://doi.org/10.1053/j.gastro.2014.04.021openalex-snapshot
Kinetic Analyses Reveal Potent and Early Blockade of Hepatitis C Virus Assembly by NS5A Inhibitors
inferredcites →https://doi.org/10.1053/j.gastro.2014.07.019openalex-snapshot
Daclatasvir-Like Inhibitors of NS5A Block Early Biogenesis of Hepatitis C Virus–Induced Membranous Replication Factories, Independent of RNA Replication
inferredcites →https://doi.org/10.1053/j.gastro.2016.11.047openalex-snapshot
Daclatasvir Prevents Hepatitis C Virus Infectivity by Blocking Transfer of the Viral Genome to Assembly Sites
inferredcites →https://doi.org/10.1073/pnas.1500265112openalex-snapshot
Characterization of nonprimate hepacivirus and construction of a functional molecular clone
inferredcites →https://doi.org/10.1074/jbc.m115.675413openalex-snapshot
Phosphoproteomics Identified an NS5A Phosphorylation Site Involved in Hepatitis C Virus Replication
inferredcites →https://doi.org/10.1074/jbc.m210900200openalex-snapshot
The Hepatitis C Virus Non-structural NS5A Protein Inhibits Activating Protein–1 Function by Perturbing Ras-ERK Pathway Signaling
inferredcites →https://doi.org/10.1074/jbc.m305684200openalex-snapshot
Hepatitis C Virus Non-structural Proteins in the Probable Membranous Compartment Function in Viral Genome Replication
inferredcites →https://doi.org/10.1099/jgv.0.000975openalex-snapshot
Regulation of hepatitis C virus replication via threonine phosphorylation of the NS5A protein
inferredcites →https://doi.org/10.1099/vir.0.050633-0openalex-snapshot
The C terminus of NS5A domain II is a key determinant of hepatitis C virus genome replication, but is not required for virion assembly and release
inferredcites →https://doi.org/10.1099/vir.0.81334-0openalex-snapshot
Development and characterization of a transient-replication assay for the genotype 2a hepatitis C virus subgenomic replicon
inferredcites →https://doi.org/10.1111/j.1469-0691.2010.03432.xopenalex-snapshot
Evolving epidemiology of hepatitis C virus
inferredcites →https://doi.org/10.1111/j.1478-3231.2011.02494.xopenalex-snapshot
Hepatitis C virus infection in USA: an estimate of true prevalence
inferredcites →https://doi.org/10.1128/jvi.00068-10openalex-snapshot
Polo-Like Kinase 1 Is Involved in Hepatitis C Virus Replication by Hyperphosphorylating NS5A
inferredcites →https://doi.org/10.1128/jvi.00194-17openalex-snapshot
Serine 235 Is the Primary NS5A Hyperphosphorylation Site Responsible for Hepatitis C Virus Replication
inferredcites →https://doi.org/10.1128/jvi.00616-10openalex-snapshot
All Three Domains of the Hepatitis C Virus Nonstructural NS5A Protein Contribute to RNA Binding
inferredcites →https://doi.org/10.1128/jvi.00805-17openalex-snapshot
Phosphorylation of Serine 225 in Hepatitis C Virus NS5A Regulates Protein-Protein Interactions
inferredcites →https://doi.org/10.1128/jvi.00826-16openalex-snapshot
Release of Infectious Hepatitis C Virus from Huh7 Cells Occurs via a trans -Golgi Network-to-Endosome Pathway Independent of Very-Low-Density Lipoprotein Secretion
inferredcites →https://doi.org/10.1128/jvi.02352-08openalex-snapshot
Crystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C Virus
inferredcites →https://doi.org/10.1128/jvi.02490-13openalex-snapshot
Dynamic Imaging of the Hepatitis C Virus NS5A Protein during a Productive Infection
inferredcites →https://doi.org/10.1128/jvi.02995-14openalex-snapshot
Serine Phosphorylation of the Hepatitis C Virus NS5A Protein Controls the Establishment of Replication Complexes
inferredcites →https://doi.org/10.1128/jvi.03017-13openalex-snapshot
Insights into the Complexity and Functionality of Hepatitis C Virus NS5A Phosphorylation
inferredcites →https://doi.org/10.1128/jvi.03404-13openalex-snapshot
Dengue Virus- and Hepatitis C Virus-Induced Replication and Assembly Compartments: the Enemy Inside—Caught in the Web
inferredcites →https://doi.org/10.1128/jvi.78.23.13306-13314.2004openalex-snapshot
Reduction of Hepatitis C Virus NS5A Hyperphosphorylation by Selective Inhibition of Cellular Kinases Activates Viral RNA Replication in Cell Culture
inferredcites →https://doi.org/10.1371/journal.pone.0078195openalex-snapshot
GPS2 Is Required for the Association of NS5A with VAP-A and Hepatitis C Virus Replication
inferredcites →https://doi.org/10.1371/journal.pone.0170461openalex-snapshot
Nonstructural 5A Protein of Hepatitis C Virus Interferes with Toll-Like Receptor Signaling and Suppresses the Interferon Response in Mouse Liver
inferredcites →https://doi.org/10.1371/journal.ppat.1000032openalex-snapshot
Regulation of Hepatitis C Virion Production via Phosphorylation of the NS5A Protein
inferredcites →https://doi.org/10.1371/journal.ppat.1000035openalex-snapshot
Essential Role of Domain III of Nonstructural Protein 5A for Hepatitis C Virus Infectious Particle Assembly
inferredcites →https://doi.org/10.1371/journal.ppat.1003359openalex-snapshot
The Lipid Kinase Phosphatidylinositol-4 Kinase III Alpha Regulates the Phosphorylation Status of Hepatitis C Virus NS5A
inferredcites →https://doi.org/10.1371/journal.ppat.1003513openalex-snapshot
Rab18 Binds to Hepatitis C Virus NS5A and Promotes Interaction between Sites of Viral Replication and Lipid Droplets
inferredcites →https://doi.org/10.1371/journal.ppat.1006834openalex-snapshot
A role for domain I of the hepatitis C virus NS5A protein in virus assembly
inferredcites →https://doi.org/10.14348/molcells.2017.2299openalex-snapshot
Hepatitis C Virus Nonstructural 5A Protein (HCV-NS5A) Inhibits Hepatocyte Apoptosis through the NF-κb/miR-503/bcl-2 Pathway
inferredcites →https://doi.org/10.3390/v8050142openalex-snapshot
Mechanisms of Cellular Membrane Reorganization to Support Hepatitis C Virus Replication
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1099/jgv.0.001486openalex-snapshot
Insights into the unique characteristics of hepatitis C virus genotype 3 revealed by development of a robust sub-genomic DBN3a replicon
inferred← citeshttps://doi.org/10.1101/660217openalex-snapshot
Recombinant rotaviruses rescued by reverse genetics reveal the role of NSP5 hyperphosphorylation in the assembly of viral factories
inferred← citeshttps://doi.org/10.1128/jvi.00107-22openalex-snapshot
Sequential Phosphorylation of Hepatitis C Virus NS5A Protein Requires the ATP-Binding Domain of NS3 Helicase
inferred← citeshttps://doi.org/10.1128/jvi.01110-19openalex-snapshot
Recombinant Rotaviruses Rescued by Reverse Genetics Reveal the Role of NSP5 Hyperphosphorylation in the Assembly of Viral Factories
inferred← citeshttps://doi.org/10.1146/annurev-cellbio-100818-125320openalex-snapshot
Expansion Microscopy: Scalable and Convenient Super-Resolution Microscopy
inferred← citeshttps://doi.org/10.1186/s12876-021-01988-yopenalex-snapshot
First report on molecular docking analysis and drug resistance substitutions to approved HCV NS5A and NS5B inhibitors amongst Iranian patients
Editorial review for independent work. ICSAC — the Institute for Complexity
Science and Advanced Computing — runs a structured editorial panel for researchers
publishing outside journals, and publishes on CiteStamp rails. Submission is free
and goes through ORCID: icsacinstitute.org/submit.