Cell surface proteoglycans are necessary for A27L protein-mediated cell fusion: identification of the N-terminal region of A27L protein as the glycosaminoglycan-binding domain.
about
Vaccinia virus 4c (A26L) protein on intracellular mature virus binds to the extracellular cellular matrix lamininPoxvirus cell entry: how many proteins does it take?Large-plaque mutants of Sindbis virus show reduced binding to heparan sulfate, heightened viremia, and slower clearance from the circulationVaccinia virus L1 binds to cell surfaces and blocks virus entry independently of glycosaminoglycansA Turn-like Structure "KKPE" Segment Mediates the Specific Binding of Viral Protein A27 to Heparin and Heparan Sulfate on Cell SurfacesStructural and Biochemical Characterization of the Vaccinia Virus Envelope Protein D8 and Its Recognition by the Antibody LA5Poxvirus tropismDrosophila S2 cells are non-permissive for vaccinia virus DNA replication following entry via low pH-dependent endocytosis and early transcriptionVaccinia viral protein A27 is anchored to the viral membrane via a cooperative interaction with viral membrane protein A17A novel cellular protein, VPEF, facilitates vaccinia virus penetration into HeLa cells through fluid phase endocytosis.Disulfide bond formation at the C termini of vaccinia virus A26 and A27 proteins does not require viral redox enzymes and suppresses glycosaminoglycan-mediated cell fusion.Vaccinia virus exhibits cell-type-dependent entry characteristics.Vaccinia virus penetration requires cholesterol and results in specific viral envelope proteins associated with lipid raftsVaccinia virus H2 protein is an essential component of a complex involved in virus entry and cell-cell fusionGlycosaminoglycan sulfation requirements for respiratory syncytial virus infection.Vaccinia virus envelope H3L protein binds to cell surface heparan sulfate and is important for intracellular mature virion morphogenesis and virus infection in vitro and in vivoVaccinia virus envelope D8L protein binds to cell surface chondroitin sulfate and mediates the adsorption of intracellular mature virions to cellsVaccinia virus A21 virion membrane protein is required for cell entry and fusionThe product of the vaccinia virus L5R gene is a fourth membrane protein encoded by all poxviruses that is required for cell entry and cell-cell fusion.Proteome analysis of vaccinia virus IHD-W-infected HEK 293 cells with 2-dimensional gel electrophoresis and MALDI-PSD-TOF MS of on solid phase support N-terminally sulfonated peptides.The membrane fusion step of vaccinia virus entry is cooperatively mediated by multiple viral proteins and host cell componentsVaccinia virus J1R protein: a viral membrane protein that is essential for virion morphogenesis.Smallpox vaccines: targets of protective immunity.Crystal structure of vaccinia viral A27 protein reveals a novel structure critical for its function and complex formation with A26 proteinGlycosaminoglycans mediate retention of the poxvirus type I interferon binding protein at the cell surface to locally block interferon antiviral responses.The envelope G3L protein is essential for entry of vaccinia virus into host cellsVaccinia virus G9 protein is an essential component of the poxvirus entry-fusion complex.Lipid membranes in poxvirus replication.Identification of linear heparin-binding peptides derived from human respiratory syncytial virus fusion glycoprotein that inhibit infectivity.Vaccinia mature virus fusion regulator A26 protein binds to A16 and G9 proteins of the viral entry fusion complex and dissociates from mature virions at low pHVaccinia virus entry, exit, and interaction with differentiated human airway epithelia.Proteoglycans in host-pathogen interactions: molecular mechanisms and therapeutic implicationsOrthopoxvirus species and strain differences in cell entry.Linear Epitopes in Vaccinia Virus A27 Are Targets of Protective Antibodies Induced by Vaccination against Smallpox.The Vaccinia Virus H3 Envelope Protein, a Major Target of Neutralizing Antibodies, Exhibits a Glycosyltransferase Fold and Binds UDP-GlucoseVaccinia virus entry into cells is dependent on a virion surface protein encoded by the A28L gene.Protective effect of surfactant protein d in pulmonary vaccinia virus infection: implication of A27 viral protein.Engineering the vaccinia virus L1 protein for increased neutralizing antibody response after DNA immunization.Reprogramming antitumor immunity against chemoresistant ovarian cancer by a CXCR4 antagonist-armed viral oncotherapy.From crescent to mature virion: vaccinia virus assembly and maturation.
P2860
Q24336532-1A78F545-5C25-4671-A5E2-8695AFA116AAQ27002455-6CF89DB3-E990-4B06-AB71-A37D98DFB45AQ27469619-71B91C42-68C1-4214-A083-71EB17F450A5Q27488704-4FDAD946-20A0-4EAF-969A-CECDB9D7C8B3Q27490518-A510BAE0-C5E9-4451-9E60-EF09D15B705EQ27679281-F27045D8-7504-4CC3-BD2A-D35CA2EF218AQ28237434-159DF74A-03AE-444D-8408-A78D9CD5EF6FQ28477161-E43040B7-D16A-4903-BBF2-F04A567718C8Q30358168-9497F28E-5298-4B2C-B3CE-31A11ADD77FDQ30483178-E1149CF4-2B05-4E72-82EF-A98C62D1B217Q30488301-9B7C956F-70BE-4EB2-B636-711CFC3A9072Q33698769-06E96A58-034F-4A33-8AF0-2F842EA9F7CDQ33718427-62427F95-C0D3-4B87-BD9C-D18977B5B254Q33724218-D972E5AD-9AF3-47C0-81C0-38A7FF612623Q33787265-4A58DF09-83FB-4D4D-92BB-F57CFA9F6867Q33801656-452320F2-AAE4-4122-997A-7AA62A5304F3Q33821117-CBB4B109-80D4-4A48-9444-AA71DF487AC9Q33908798-4B62990F-13B9-41AB-A091-CC841DEFD276Q33930439-E51B784C-E47E-4475-8940-429DA1922100Q33977645-C7973078-D4CF-405F-AC8F-6CDC4879FD8DQ34109783-2538BEB1-DAEB-4A2A-9763-591D3144BD39Q34347131-52A2BFD7-A138-475E-B3F0-68AAFCBC9C3EQ34780607-B6FBB31E-0825-43D6-B2FC-41AB531451FFQ34976944-53607227-4D54-4F65-9113-C17B296D262DQ35003207-3992D037-8895-40D2-8BE9-9F3510705459Q35024119-8FCBC614-DB64-43CA-BF63-FB55856B4CF2Q35101454-B2C5D8C1-B68A-4DAF-8724-0A0B9D448A0EQ35260919-962CB33C-947C-4267-A618-AFDDB8DD9992Q35634327-7998EFD5-1691-414A-9BEC-0D061EAF4FEEQ35826881-E02D817E-3BBB-4958-B401-9D8439AADA6AQ36098912-F99EEE21-4DD1-422D-A923-0A212B8B07F2Q36253322-0361833D-8011-4EC9-B97A-8963D74E805FQ36315941-828A7F1E-D995-47AE-8386-1ADAD7FC87A2Q36811880-D225B26F-9687-4B7A-B8FC-EE01F0592495Q36878858-24BBAA27-46E5-4C0C-A175-330E3F94F1D6Q36954883-8F23AB58-5071-421D-BE5C-E8A220BF07B5Q36993944-4B2D48CA-5A34-4CE9-A200-CF7555791A05Q37125302-ABDEBFAF-7C8A-4CD3-A901-DD16178227DEQ37502464-744E4099-600E-473E-8100-12B6237827DCQ38258150-99752BC2-CE8F-4861-B8F9-0D3E1C298142
P2860
Cell surface proteoglycans are necessary for A27L protein-mediated cell fusion: identification of the N-terminal region of A27L protein as the glycosaminoglycan-binding domain.
description
1998 nî lūn-bûn
@nan
1998 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Cell surface proteoglycans are ...... cosaminoglycan-binding domain.
@ast
Cell surface proteoglycans are ...... cosaminoglycan-binding domain.
@en
type
label
Cell surface proteoglycans are ...... cosaminoglycan-binding domain.
@ast
Cell surface proteoglycans are ...... cosaminoglycan-binding domain.
@en
prefLabel
Cell surface proteoglycans are ...... cosaminoglycan-binding domain.
@ast
Cell surface proteoglycans are ...... cosaminoglycan-binding domain.
@en
P2093
P2860
P1433
P1476
Cell surface proteoglycans are ...... ycosaminoglycan-binding domain
@en
P2093
P2860
P304
P577
1998-10-01T00:00:00Z