Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1 - Wikidata - awgldk - TriplyDB

Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1

Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1

http://www.wikidata.org/entity/Q24643931

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Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1 Infectivities of human and other primate lentiviruses are activated by desialylation of the virion surface Designed oligomers of cyanovirin-N show enhanced HIV neutralization Inhibition of human immunodeficiency virus (HIV) infection in vitro by anticarbohydrate monoclonal antibodies: peripheral glycosylation of HIV envelope glycoprotein gp120 may be a target for virus neutralization Inhibition of alpha-glucosidase I of the glycoprotein-processing enzymes by 6-O-butanoyl castanospermine (MDL 28,574) and its consequences in human immunodeficiency virus-infected T cells Nonrandom distribution of gp120 N-linked glycosylation sites important for infectivity of human immunodeficiency virus type 1 Effect of chloroquine on reducing HIV-1 replication in vitro and the DC-SIGN mediated transfer of virus to CD4+ T-lymphocytes.C-terminal tail of human immunodeficiency virus gp41: functionally rich and structurally enigmatic.Modulation of antigen-specific humoral responses in rhesus macaques by using cytokine cDNAs as DNA vaccine adjuvants Resistance of native, oligomeric envelope on simian immunodeficiency virus to digestion by glycosidases.N-linked glycosylation sites adjacent to and within the V1/V2 and the V3 loops of dualtropic human immunodeficiency virus type 1 isolate DH12 gp120 affect coreceptor usage and cellular tropism Analysis of genetic variability within the immunodominant epitopes of envelope gp41 from human immunodeficiency virus type 1 (HIV-1) group M and its impact on HIV-1 antibody detection.Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.Subtle evolutionary changes in the distribution of N-glycosylation sequons in the HIV-1 envelope glycoprotein 120 Glycosylation and disulfide bond analysis of transiently and stably expressed clade C HIV-1 gp140 trimers in 293T cells identifies disulfide heterogeneity present in both proteins and differences in O-linked glycosylation Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16.Partial enzymatic deglycosylation preserves the structure of cleaved recombinant HIV-1 envelope glycoprotein trimers.The tale of the long tail: the cytoplasmic domain of HIV-1 gp41.Transmitted/founder simian immunodeficiency virus envelope sequences in vesicular stomatitis and Semliki forest virus vector immunized rhesus macaques.Prime-boost immunization of rabbits with HIV-1 gp120 elicits potent neutralization activity against a primary viral isolate.HIV-1 envelope glycan moieties modulate HIV-1 transmission.Surfactant Protein D modulates HIV infection of both T-cells and dendritic cells.Role of N-linked glycans in a human immunodeficiency virus envelope glycoprotein: effects on protein function and the neutralizing antibody response.Glycomic analysis by glycoprotein immobilization for glycan extraction and liquid chromatography on microfluidic chip.Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron cryomicroscopy.HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation.Antiviral therapy for human immunodeficiency virus infections Processing of the envelope glycoprotein gp160 in immunotoxin-resistant cell lines chronically infected with human immunodeficiency virus type 1.Glycosylation of simian immunodeficiency virus influences immune-tissue targeting during primary infection, leading to immunodeficiency or viral control Proposed atomic structure of a truncated human immunodeficiency virus glycoprotein gp120 derived by molecular modeling: target CD4 recognition and docking mechanism.Neutralization sensitivity of human immunodeficiency virus type 1 is determined in part by the cell in which the virus is propagated.Complement-mediated binding of naturally glycosylated and glycosylation-modified human immunodeficiency virus type 1 to human CR2 (CD21).HIV-1 N-glycan composition governs a balance between dendritic cell-mediated viral transmission and antigen presentation.Strain-specific neutralizing determinant in the transmembrane protein of simian immunodeficiency virus.Mutational analysis of conserved N-linked glycosylation sites of human immunodeficiency virus type 1 gp41 Cloning and characterization of human immunodeficiency virus type 1 variants diminished in the ability to induce syncytium-independent cytolysis.Effects of individually silenced N-glycosylation sites and non-synonymous single-nucleotide polymorphisms on the fusogenic function of human syncytin-2.HIV-1 envelope glycoprotein signatures that correlate with the development of cross-reactive neutralizing activity.Two-dimensional gel-based approaches for the assessment of N-Linked and O-GlcNAc glycosylation in human and simian immunodeficiency viruses.Bitter-sweet symphony: glycan-lectin interactions in virus biology.

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Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1

http://www.wikidata.org/entity/Q24643931

description

1988 nî lūn-bûn

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1988 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1988 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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1988年の論文

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1988年論文

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1988年論文

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1988年論文

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1988年論文

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1988年論文

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1988年论文

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name

Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1

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Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1

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Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1

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Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1

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Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1

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Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1

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prefLabel

Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1

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Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1

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Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1

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Proceedings of the National Academy of Sciences of the United States of America

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Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1

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D C Montefiori

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W E Robinson

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W M Mitchell

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Isolation of a T-lymphotropic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS)

Inhibition of human immunodeficiency virus syncytium formation and virus replication by castanospermine

Complete nucleotide sequence of the AIDS virus, HTLV-III

The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus

Detection, isolation, and continuous production of cytopathic retroviruses (HTLV-III) from patients with AIDS and pre-AIDS

Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis

Binding of the human retrovirus HTLV-III/LAV/ARV/HIV to the CD4 (T4) molecule: conformation dependence, epitope mapping, antibody inhibition, and potential for idiotypic mimicry

Binding of HTLV-III/LAV to T4+ T cells by a complex of the 110K viral protein and the T4 molecule

Functional regions of the envelope glycoprotein of human immunodeficiency virus type 1

T-lymphocyte T4 molecule behaves as the receptor for human retrovirus LAV

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