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Dynamic allostery governs cyclophilin A-HIV capsid interplay

Dynamic allostery governs cyclophilin A-HIV capsid interplay

http://www.wikidata.org/entity/Q36332027

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HIV Genome-Wide Protein Associations: a Review of 30 Years of Research Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site.Improving dipolar recoupling for site-specific structural and dynamics studies in biosolids NMR: windowed RN-symmetry sequences All-Atom Molecular Dynamics of Virus Capsids as Drug Targets Major Variations in HIV-1 Capsid Assembly Morphologies Involve Minor Variations in Molecular Structures of Structurally Ordered Protein Segments.Toward Closing the Gap: Quantum Mechanical Calculations and Experimentally Measured Chemical Shifts of a Microcrystalline Lectin.Computational Methodologies for Real-Space Structural Refinement of Large Macromolecular Complexes.Enzyme Selectivity Fine-Tuned through Dynamic Control of a Loop Molecular Architecture of the Retroviral Capsid.Contributions of Charged Residues in Structurally Dynamic Capsid Surface Loops to Rous Sarcoma Virus Assembly.Solid-State NMR Provides Evidence for Small-Amplitude Slow Domain Motions in a Multispanning Transmembrane α-Helical Protein.Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.Capsid-Dependent Host Factors in HIV-1 Infection.Enhancing NMR Sensitivity of Natural-Abundance Low-γ Nuclei by Ultrafast Magic-Angle-Spinning Solid-State NMR Spectroscopy.Physical properties of the HIV-1 capsid from all-atom molecular dynamics simulations.Characterization of Protein-Protein Interfaces in Large Complexes by Solid-State NMR Solvent Paramagnetic Relaxation Enhancements.Protein conformational dynamics studied by 15N and 1H R1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals.Quenching protein dynamics interferes with HIV capsid maturation.Microsecond Timescale Protein Dynamics: a Combined Solid-State NMR Approach.A suite of pulse sequences based on multiple sequential acquisitions at one and two radiofrequency channels for solid-state magic-angle spinning NMR studies of proteins.Segmental isotopic labeling of HIV-1 capsid protein assemblies for solid state NMR.Expanding the horizons for structural analysis of fully protonated protein assemblies by NMR spectroscopy at MAS frequencies above 100 kHz.

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P2860

Dynamic allostery governs cyclophilin A-HIV capsid interplay

http://www.wikidata.org/entity/Q36332027

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2015 nî lūn-bûn

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2015年の論文

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2015年学术文章

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Dynamic allostery governs cyclophilin A-HIV capsid interplay

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Dynamic allostery governs cyclophilin A-HIV capsid interplay

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type

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Dynamic allostery governs cyclophilin A-HIV capsid interplay

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Dynamic allostery governs cyclophilin A-HIV capsid interplay

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Dynamic allostery governs cyclophilin A-HIV capsid interplay

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Dynamic allostery governs cyclophilin A-HIV capsid interplay

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PNAS.1516920112

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

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Dynamic allostery governs cyclophilin A-HIV capsid interplay

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Christopher Aiken

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Christopher J Langmead

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Christopher L Suiter

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Guangjin Hou

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Huilan Zhang

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In-Ja L Byeon

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Jinwoo Ahn

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

Manman Lu

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

Peijun Zhang

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

Peter L Gor'kov

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

P2860

Cyclophilin A is required for TRIM5{alpha}-mediated resistance to HIV-1 in Old World monkey cells

Virus assembly and maturation: auto-regulation through allosteric molecular switches

Structural Convergence between Cryo-EM and NMR Reveals Intersubunit Interactions Critical for HIV-1 Capsid Function

Structure of the HIV-1 Full-Length Capsid Protein in a Conformationally Trapped Unassembled State Induced by Small-Molecule Binding

Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics

HIV-1 capsid undergoes coupled binding and isomerization by the nuclear pore protein NUP358

Structure and Dynamics of Full-Length HIV-1 Capsid Protein in Solution

Structure of a kinesin-tubulin complex and implications for kinesin motility

The structure of apo-kinesin bound to tubulin links the nucleotide cycle to movement

Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid

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scholarly article

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47

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112

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Angela M Gronenborn

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2015-11-09T00:00:00Z

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283648966

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