Binding of human collectins (SP-A and MBP) to influenza virus
about
An Insight into the Diverse Roles of Surfactant Proteins, SP-A and SP-D in Innate and Adaptive ImmunityCrystallographic Complexes of Surfactant Protein A and Carbohydrates Reveal Ligand-induced Conformational ChangeCompounds with anti-influenza activity: present and future of strategies for the optimal treatment and management of influenza. Part II: Future compounds against influenza virusCollectins and pulmonary host defenseSurfactant protein A binding to cytomegalovirus proteins enhances virus entry into rat lung cells.Protective role of the lung collectins surfactant protein A and surfactant protein D in airway inflammation.Critical role of airway macrophages in modulating disease severity during influenza virus infection of mice.Distinct roles for lung collectins in pulmonary host defense.Effect of lung surfactant collectins on bronchoalveolar macrophage interaction with Blastomyces dermatitidis: inhibition of tumor necrosis factor alpha production by surfactant protein DCollectin-mediated antiviral host defense of the lung: evidence from influenza virus infection of miceSoluble host defense lectins in innate immunity to influenza virusPulmonary collectins in innate immunity of the lung.Protective effect of surfactant protein d in pulmonary vaccinia virus infection: implication of A27 viral protein.Bitter-sweet symphony: glycan-lectin interactions in virus biology.Inhibition of influenza viral neuraminidase activity by collectins.Mechanism of binding of surfactant protein D to influenza A viruses: importance of binding to haemagglutinin to antiviral activity.Surfactant protein A, but not surfactant protein D, is an opsonin for influenza A virus phagocytosis by rat alveolar macrophages.Recombinant bovine conglutinin, lacking the N-terminal and collagenous domains, has less conglutination activity but is able to inhibit haemagglutination by influenza A virus.Inhibition of lectin-mediated innate host defences in vivo modulates disease severity during influenza virus infection.Molecular structures and interactions of pulmonary surfactant components.Human lung surfactant protein A exists in several different oligomeric states: oligomer size distribution varies between patient groups.Structure of a truncated human surfactant protein D is less effective in agglutinating bacteria than the native structure and fails to inhibit haemagglutination by influenza A virus.Specific interaction of hepatitis C virus glycoproteins with mannan binding lectin inhibits virus entry.Human mannan-binding lectin inhibits the infection of influenza A virus without complement.Alterations in lung collectins in an adaptive allergic immune response.
P2860
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P2860
Binding of human collectins (SP-A and MBP) to influenza virus
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Binding of human collectins (SP-A and MBP) to influenza virus
@en
Binding of human collectins
@nl
type
label
Binding of human collectins (SP-A and MBP) to influenza virus
@en
Binding of human collectins
@nl
prefLabel
Binding of human collectins (SP-A and MBP) to influenza virus
@en
Binding of human collectins
@nl
P2093
P2860
P356
P1433
P1476
Binding of human collectins (SP-A and MBP) to influenza virus
@en
P2093
P2860
P304
P356
10.1042/BJ3040455
P407
P478
304 ( Pt 2)
P577
1994-12-01T00:00:00Z