Research graph
References from Proximity labelling of internalizing influenza A viruses reveals a role for neogenin in virus uptake. Local targets link to admitted publications; unresolved targets remain external evidence.
Unresolved reference
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Influenza virus uses mGluR2 as an endocytic receptor to enter cells
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A sialylated voltage-dependent Ca2+ channel binds hemagglutinin and mediates influenza A virus entry into mammalian cells
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Breaking the convention: sialoglycan variants, coreceptors, and alternative receptors for influenza A virus entry
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A genome-wide CRISPR/Cas9 gene knockout screen identifies immunoglobulin superfamily DCC subclass member 4 as a key host factor that promotes influenza virus endocytosis
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The epidermal growth factor receptor (EGFR) promotes uptake of influenza A viruses (IAV) into host cells
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Hemagglutinin of influenza A virus binds specifically to cell surface nucleolin and plays a role in virus internalization
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The G protein-coupled receptor FFAR2 promotes internalization during influenza A virus entry
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Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus
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Assembly of endocytic machinery around individual influenza viruses during viral entry
10.1038/nsmb769 · 2004 · External reference
Influenza virus can enter and infect cells in the absence of clathrin-mediated endocytosis
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Infectious entry pathway of influenza virus in a canine kidney cell line
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The Ras-PI3K signaling pathway is involved in clathrin-independent endocytosis and the internalization of influenza viruses
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Filamentous influenza virus enters cells via macropinocytosis
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Dissection of the influenza A virus endocytic routes reveals macropinocytosis as an alternative entry pathway
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Epsin 1 is involved in recruitment of ubiquitinated EGF receptors into clathrin-coated pits
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Interaction with epsin 1 regulates the constitutive clathrin-dependent internalization of ErbB3
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Proximity labeling in mammalian cells with TurboID and split-TurboID
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Entry of influenza A virus into host cells - recent progress and remaining challenges
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Role of clathrin-mediated endocytosis during vesicular stomatitis virus entry into host cells
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Timing is everything: fine-tuned molecular machines orchestrate paramyxovirus entry
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SAINTexpress: improvements and additional features in significance analysis of INTeractome software
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Combined proximity labeling and affinity purification-mass spectrometry workflow for mapping and visualizing protein interaction networks
10.1038/s41596-020-0365-x · 2020 · External reference
Meta- and orthogonal integration of influenza “OMICs” data defines a role for UBR4 in virus budding
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DeepTMHMM predicts alpha and beta transmembrane proteins using deep neural networks
2022 · External reference
The epsin protein family: coordinators of endocytosis and signaling
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The STRING database in 2023: protein-protein association networks and functional enrichment analyses for any sequenced genome of interest
10.1093/nar/gkac1000 · 2023 · External reference
Monitoring cell-surface N-glycoproteome dynamics by quantitative proteomics reveals mechanistic insights into macrophage differentiation
10.1074/mcp.m116.063859 · 2017 · External reference
MHC class II proteins mediate sialic acid independent entry of human and avian H2N2 influenza A viruses
10.1038/s41564-024-01771-1 · 2024 · External reference
Comparison of different aminofunctionalization strategies for attachment of single antibodies to AFM cantilevers
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Linking of sensor molecules with amino groups to amino-functionalized AFM tips
10.1021/bc200099t · 2011 · External reference
Determination of the kinetic on- and off-rate of single virus-cell interactions
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Nanomechanical mapping of first binding steps of a virus to animal cells
10.1038/nnano.2016.228 · 2017 · External reference
Single-molecule analysis of SARS-CoV-2 binding to C-type lectin receptors
10.1021/acs.nanolett.2c04931 · 2023 · External reference
Application of a biologically contained reporter system to study gain-of-function H5N1 influenza A viruses with pandemic potential
10.1128/msphere.00423-20 · 2020 · External reference
Requirement for vacuolar proton-ATPase activity during entry of influenza virus into cells
10.1128/jvi.69.4.2306-2312.1995 · 1995 · External reference
Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
10.1006/meth.2001.1262 · 2001 · External reference
Comparative application of BioID and TurboID for protein-proximity biotinylation
10.3390/cells9051070 · 2020 · External reference
Role of the actin cytoskeleton during influenza virus internalization into polarized epithelial cells
10.1111/j.1462-5822.2007.00900.x · 2007 · External reference
Netrins and neogenin promote myotube formation
10.1083/jcb.200405039 · 2004 · External reference
Interaction of hemojuvelin with neogenin results in iron accumulation in human embryonic kidney 293 cells
10.1074/jbc.m506207200 · 2005 · External reference
Neogenin mediates the action of repulsive guidance molecule
10.1038/ncb1156 · 2004 · External reference
Neogenin, a receptor for bone morphogenetic proteins
10.1074/jbc.m110.180919 · 2011 · External reference
Neogenin-RGMa signaling at the growth cone is bone morphogenetic protein-independent and involves RhoA, ROCK, and PKC
10.1074/jbc.m610901200 · 2007 · External reference
A Ca(2 )-dependent signalling circuit regulates influenza A virus internalization and infection
10.1038/ncomms3763 · 2013 · External reference
Neogenin interacts with RGMa and netrin-1 to guide axons within the embryonic vertebrate forebrain
10.1016/j.ydbio.2006.06.018 · 2006 · External reference
Hepatocyte neogenin is required for hemojuvelin-mediated hepcidin expression and iron homeostasis in mice
10.1182/blood.2020009485 · 2021 · External reference
The Netrin-1-Neogenin-1 signaling axis controls neuroblastoma cell migration via integrin-β1 and focal adhesion kinase activation
10.1080/19336918.2021.1892397 · 2021 · External reference
PLC-γ1 signaling plays a subtype-specific role in postbinding cell entry of influenza A virus
10.1128/jvi.02591-13 · 2014 · External reference
New world bats harbor diverse influenza A viruses
10.1371/journal.ppat.1003657 · 2013 · External reference
Hemagglutinin homologue from H17N10 bat influenza virus exhibits divergent receptor-binding and pH-dependent fusion activities
10.1073/pnas.1218509110 · 2013 · External reference
Bat-derived influenza hemagglutinin H17 does not bind canonical avian or human receptors and most likely uses a unique entry mechanism
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MHC class II proteins mediate cross-species entry of bat influenza viruses
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Junction adhesion molecule is a receptor for reovirus
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Utilization of sialic acid as a coreceptor enhances reovirus attachment by multistep adhesion strengthening
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Beta1 integrin mediates internalization of mammalian reovirus
10.1128/jvi.80.6.2760-2770.2006 · 2006 · External reference
Single-virus tracking with quantum dots in live cells
10.1038/s41596-022-00775-7 · 2023 · External reference
Revealing different pathways for influenza A virus to reach microtubules after endocytosis by quantum dot-based single-virus tracking
10.1021/acsnano.4c05261 · 2024 · External reference
A “driver switchover” mechanism of influenza virus transport from microfilaments to microtubules
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Proximal protein landscapes of the type I interferon signaling cascade reveal negative regulation by PJA2
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B-Fabric: the Swiss Army Knife for life sciences
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The PRIDE database and related tools and resources in 2019: improving support for quantification data
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MSFragger: ultrafast and comprehensive peptide identification in mass spectrometry-based proteomics
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Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis
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g:Profiler-interoperable web service for functional enrichment analysis and gene identifier mapping (2023 update)
10.1093/nar/gkad347 · 2023 · External reference
Reovirus directly engages integrin to recruit clathrin for entry into host cells
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Combining confocal and atomic force microscopy to quantify single-virus binding to mammalian cell surfaces
10.1038/nprot.2017.112 · 2017 · External reference
Metabotropic glutamate receptor subtype 2 is a cellular receptor for rabies virus
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