N-linked glycosylation facilitates sialic acid-independent attachment and entry of influenza A viruses into cells expressing DC-SIGN or L-SIGN - Wikidata - awgldk - TriplyDB

N-linked glycosylation facilitates sialic acid-independent attachment and entry of influenza A viruses into cells expressing DC-SIGN or L-SIGN

N-linked glycosylation facilitates sialic acid-independent attachment and entry of influenza A viruses into cells expressing DC-SIGN or L-SIGN

http://www.wikidata.org/entity/Q34742902

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Antigen-specific B-cell receptor sensitizes B cells to infection by influenza virus Modulating the Innate Immune Response to Influenza A Virus: Potential Therapeutic Use of Anti-Inflammatory Drugs Dendritic cells and influenza A virus infection CLEC5A-Mediated Enhancement of the Inflammatory Response in Myeloid Cells Contributes to Influenza Virus Pathogenicity In Vivo Influenza A virus polymerase is a site for adaptive changes during experimental evolution in bat cells Playing hide and seek: how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection.Innate immune sensing and response to influenza.Efficient generation of influenza virus with a mouse RNA polymerase I-driven all-in-one plasmid Avian and Human Seasonal Influenza Hemagglutinin Proteins Elicit CD4 T Cell Responses That Are Comparable in Epitope Abundance and Diversity High doses of recombinant mannan-binding lectin inhibit the binding of influenza A(H1N1)pdm09 virus with cells expressing DC-SIGN.Developing the IVIG biomimetic, hexa-Fc, for drug and vaccine applications Binding of DC-SIGN to the hemagglutinin of influenza A viruses supports virus replication in DC-SIGN expressing cells.Efficient sensing of avian influenza viruses by porcine plasmacytoid dendritic cells Endogenous Murine BST-2/Tetherin Is Not a Major Restriction Factor of Influenza A Virus Infection.Cell receptors for influenza a viruses and the innate immune response Dendritic cells: microbial clearance via autophagy and potential immunobiological consequences for periodontal disease Soluble host defense lectins in innate immunity to influenza virus Susceptibility of bone marrow-derived macrophages to influenza virus infection is dependent on macrophage phenotype.Entry of influenza A Virus with a α2,6-linked sialic acid binding preference requires host fibronectin.The C-type Lectin Langerin Functions as a Receptor for Attachment and Infectious Entry of Influenza A Virus Endocytic function is critical for influenza A virus infection via DC-SIGN and L-SIGN.Towards multiscale modeling of influenza infection Absolute quantitation of immunoglobulin G and its glycoforms using multiple reaction monitoring.The macrophage galactose-type lectin can function as an attachment and entry receptor for influenza virus.Cell-surface receptors on macrophages and dendritic cells for attachment and entry of influenza virus.DC-SIGN, DC-SIGNR and LSECtin: C-type lectins for infection.The amazing innate immune response to influenza A virus infection.Marine viruses: the beneficial side of a threat.Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR protein reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments Measuring Attachment and Internalization of Influenza A Virus in A549 Cells by Flow Cytometry.α2-3- and α2-6- N-linked sialic acids allow efficient interaction of Newcastle Disease Virus with target cells.DC-SIGN and L-SIGN Are Attachment Factors That Promote Infection of Target Cells by Human Metapneumovirus in the Presence or Absence of Cellular Glycosaminoglycans.Optimized protocol for expression and purification of membrane-bound PglB, a bacterial oligosaccharyl transferase.Effect of receptor binding specificity on the immunogenicity and protective efficacy of influenza virus A H1 vaccines.Interaction of L-SIGN with hepatitis C virus envelope protein E2 up-regulates Raf-MEK-ERK pathway.The Role and Molecular Mechanism of Action of Surfactant Protein D in Innate Host Defense Against Influenza A Virus.Protein glycosylation in infectious disease pathobiology and treatment

P2860

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P2860

N-linked glycosylation facilitates sialic acid-independent attachment and entry of influenza A viruses into cells expressing DC-SIGN or L-SIGN

http://www.wikidata.org/entity/Q34742902

description

2010 nî lūn-bûn

@nan

2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年学术文章

@wuu

2010年学术文章

@zh-cn

2010年学术文章

@zh-hans

2010年学术文章

@zh-my

2010年学术文章

@zh-sg

2010年學術文章

@yue

name

N-linked glycosylation facilit ...... s expressing DC-SIGN or L-SIGN

@ast

N-linked glycosylation facilit ...... s expressing DC-SIGN or L-SIGN

@en

N-linked glycosylation facilit ...... s expressing DC-SIGN or L-SIGN

@nl

type

label

N-linked glycosylation facilit ...... s expressing DC-SIGN or L-SIGN

@ast

N-linked glycosylation facilit ...... s expressing DC-SIGN or L-SIGN

@en

N-linked glycosylation facilit ...... s expressing DC-SIGN or L-SIGN

@nl

prefLabel

N-linked glycosylation facilit ...... s expressing DC-SIGN or L-SIGN

@ast

N-linked glycosylation facilit ...... s expressing DC-SIGN or L-SIGN

@en

N-linked glycosylation facilit ...... s expressing DC-SIGN or L-SIGN

@nl

P1433

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P2860

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Journal of Virology

P1476

N-linked glycosylation facilit ...... s expressing DC-SIGN or L-SIGN

@en

P2093

Stuart G Turville

http://www.w3.org/2001/XMLSchema#string

P2860

HIV-1 Entry Cofactor: Functional cDNA Cloning of a Seven-Transmembrane, G Protein-Coupled Receptor

Sialobiology of Influenza: Molecular Mechanism of Host Range Variation of Influenza Viruses

DC-SIGN and L-SIGN are high affinity binding receptors for hepatitis C virus glycoprotein E2

CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome coronavirus

C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola virus in cis and in trans

Differential N-linked glycosylation of human immunodeficiency virus and Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR

DC-SIGNR, a DC-SIGN homologue expressed in endothelial cells, binds to human and simian immunodeficiency viruses and activates infection in trans

Dynamic populations of dendritic cell-specific ICAM-3 grabbing nonintegrin-positive immature dendritic cells and liver/lymph node-specific ICAM-3 grabbing nonintegrin-positive endothelial cells in the outer zones of the paracortex of human lymph nod

DC-SIGN (CD209) mediates dengue virus infection of human dendritic cells

West Nile Virus Discriminates between DC-SIGN and DC-SIGNR for Cellular Attachment and Infection

P304

2990-3000

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scholarly article

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10.1128/JVI.01705-10

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P433

6

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85

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Michelle D. Tate

Andrew G Brooks

Sarah L. Londrigan

Patrick C Reading

P577

2010-12-29T00:00:00Z

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49714340

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21191006

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P932

3067946

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