The complete Consensus V3 loop peptide of the envelope protein gp120 of HIV-1 shows pronounced helical character in solution - Wikidata - awgldk - TriplyDB

The complete Consensus V3 loop peptide of the envelope protein gp120 of HIV-1 shows pronounced helical character in solution

The complete Consensus V3 loop peptide of the envelope protein gp120 of HIV-1 shows pronounced helical character in solution

http://www.wikidata.org/entity/Q27729741

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Structural and biophysical characterization of Staphylococcus aureus SaMazF shows conservation of functional dynamics Bioinformatic analysis of HIV-1 entry and pathogenesis.Inhibitory mechanism of the CXCR4 antagonist T22 against human immunodeficiency virus type 1 infection.Analysis of physicochemical and structural properties determining HIV-1 coreceptor usage Ab initio protein structure prediction with force field parameters derived from water-phase quantum chemical calculation.Solution structure, conformational dynamics, and CD4-induced activation in full-length, glycosylated, monomeric HIV gp120 Conformational preferences of the HIV-1 principal neutralizing determinant.Structural analysis of the HIV-1 gp120 V3 loop: application to the HIV-Haiti isolates.Conformational model for the consensus V3 loop of the envelope protein gp120 of HIV-1 in a 20% trifluoroethanol/water solution.An evolutionary-network model reveals stratified interactions in the V3 loop of the HIV-1 envelope.Accurate and efficient gp120 V3 loop structure based models for the determination of HIV-1 co-receptor usage.Computational methods for de novo protein design and its applications to the human immunodeficiency virus 1, purine nucleoside phosphorylase, ubiquitin specific protease 7, and histone demethylases.Short Communication: HIV-1 Variants That Use Mouse CCR5 Reveal Critical Interactions of gp120's V3 Crown with CCR5 Extracellular Loop 1 Conformational features of a synthetic cyclic peptide corresponding to the complete V3 loop of the RF HIV-1 strain in water and water/trifluoroethanol solutions.Protein dynamics and motions in relation to their functions: several case studies and the underlying mechanisms.On the Physicochemical and Structural Modifications Associated with HIV-1 Subtype B Tropism Transition.Crystal structures of human immunodeficiency virus type 1 (HIV-1) neutralizing antibody 2219 in complex with three different V3 peptides reveal a new binding mode for HIV-1 cross-reactivity.Simulations reveal that the HIV-1 gp120-CD4 complex dissociates via complex pathways and is a potential target of the polyamidoamine (PAMAM) dendrimer.Mimicking the structure of the V3 epitope bound to HIV-1 neutralizing antibodies Increased epitope complexity correlated with antibody affinity maturation and a novel binding mode revealed by structures of rabbit antibodies against the third variable loop (V3) of HIV-1 gp120.Global and local structural properties of the principal neutralizing determinant of the HIV-1 envelope protein gp120.

P2860

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P2860

The complete Consensus V3 loop peptide of the envelope protein gp120 of HIV-1 shows pronounced helical character in solution

http://www.wikidata.org/entity/Q27729741

description

1995 nî lūn-bûn

@nan

1995 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1995 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

1995年の論文

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1995年論文

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1995年論文

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1995年論文

@zh-hk

1995年論文

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1995年論文

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1995年论文

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name

The complete Consensus V3 loop ...... helical character in solution

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The complete Consensus V3 loop ...... helical character in solution

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The complete Consensus V3 loop ...... helical character in solution

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type

label

The complete Consensus V3 loop ...... helical character in solution

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The complete Consensus V3 loop ...... helical character in solution

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The complete Consensus V3 loop ...... helical character in solution

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prefLabel

The complete Consensus V3 loop ...... helical character in solution

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The complete Consensus V3 loop ...... helical character in solution

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The complete Consensus V3 loop ...... helical character in solution

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0014-5793(95)01086-T

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The complete Consensus V3 loop ...... helical character in solution

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Borremans FA

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

Boulez K

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Budesinsky M

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Fant F

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P2860

Crystal structure of the principal neutralization site of HIV-1

Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins

Solution conformation of a peptide corresponding to the principal neutralizing determinant of HIV-1IIIB: a two-dimensional NMR study.

Solution conformational preferences of immunogenic peptides derived from the principal neutralizing determinant of the HIV-1 envelope glycoprotein gp120.

Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix.

Studies of J-connectives and selective 1H-1H Overhauser effects in H2O solutions of biological macromolecules by two-dimensional NMR experiments.

'Random coil' 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG.

The CD4-gp120 interaction and AIDS pathogenesis.

Cell type-specific heterogeneity of the HIV-1 V3 loop in infected individuals: selection of virus in macrophages and plasma.

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117-121

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scholarly article

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10.1016/0014-5793(95)01086-T

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1

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1995-10-01T00:00:00Z

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7589496

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