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Tilted, Uninterrupted, Monomeric HIV-1 gp41 Transmembrane Helix from Residual Dipolar Couplings

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Trimerization of the HIV Transmembrane Domain in Lipid Bilayers Modulates Broadly Neutralizing Antibody Binding

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Molecular Symmetry as an Aid to Geometry Determination in Ligand Protein Complexes

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Tilt Angle of a Trans-membrane Helix is Determined by Hydrophobic Mismatch

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Recent progress in the study of biomolecular structure and dynamics in solution from residual dipolar couplings

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Magnetic susceptibility in paramagnetic NMR

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Dipolar Waves as NMR maps of helices in proteins

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NMR structures of biomolecules using field oriented media and residual dipolar couplings

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Conditional Trimerization and Lytic Activity of HIV-1 gp41 Variants Containing the Membrane-Associated Segments

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Alignment of Biopolymers in Strained Gels: A New Way To Create Detectable Dipole−Dipole Couplings in High-Resolution Biomolecular NMR

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An Empirical Backbone−Backbone Hydrogen-Bonding Potential in Proteins and Its Applications to NMR Structure Refinement and Validation

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Whole-Body Rocking Motion of a Fusion Peptide in Lipid Bilayers from Size-Dispersed 15N NMR Relaxation

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DOTA-M8: An Extremely Rigid, High-Affinity Lanthanide Chelating Tag for PCS NMR Spectroscopy

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Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a Dilute Liquid Crystalline Phase

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R -factor, Free R , and Complete Cross-Validation for Dipolar Coupling Refinement of NMR Structures

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Isotropic solutions of phospholipid bicelles: A new membrane mimetic for high-resolution NMR studies of polypeptides

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Charged acrylamide copolymer gels as media for weak alignment

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Distribution and three-dimensional structure of AIDS virus envelope spikes

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Capture of an early fusion-active conformation of HIV-1 gp41

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Viral membrane fusion

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Prefusion structure of trimeric HIV-1 envelope glycoprotein determined by cryo-electron microscopy

inferredcites →https://doi.org/10.1074/jbc.m113.514554openalex-snapshot

Trimeric Transmembrane Domain Interactions in Paramyxovirus Fusion Proteins

inferredcites →https://doi.org/10.1074/jbc.r112.406272openalex-snapshot

HIV Entry and Envelope Glycoprotein-mediated Fusion

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Weak alignment offers new NMR opportunities to study protein structure and dynamics

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Cryo-EM Structure of a Fully Glycosylated Soluble Cleaved HIV-1 Envelope Trimer

inferredcites →https://doi.org/10.1126/science.278.5340.1111openalex-snapshot

Direct Measurement of Distances and Angles in Biomolecules by NMR in a Dilute Liquid Crystalline Medium

inferredcites →https://doi.org/10.1126/science.aad2450openalex-snapshot

Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer

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Structural basis for membrane anchoring of HIV-1 envelope spike

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Insights into the Conformation of the Membrane Proximal Regions Critical to the Trimerization of the HIV-1 gp41 Ectodomain Bound to Dodecyl Phosphocholine Micelles

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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HIV ‐1 gp41 transmembrane oligomerization monitored by FRET and FCS

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Mechanochemical Transformation of CF3 Group: Synthesis of Amides and Schiff Bases

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Structure, interactions and membrane topology of HIV gp41 ectodomain sequences

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Interactions of HIV gp41's membrane-proximal external region and transmembrane domain with phospholipid membranes from 31P NMR

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A large HIV gp41 construct with trimer-of-hairpins structure exhibits V2E mutation-dominant attenuation of vesicle fusion and helicity very similar to V2E attenuation of HIV fusion and infection and supports: (1) hairpin stabilization of membrane apposition with larger distance for V2E; and (2)…

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HIV-1 Env gp41 Transmembrane Domain Dynamics Are Modulated by Lipid, Water, and Ion Interactions

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Structural Basis for Broad HIV-1 Neutralization by the MPER-Specific Human Broadly Neutralizing Antibody LN01

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Cholesterol Interaction with the Trimeric HIV Fusion Protein gp41 in Lipid Bilayers Investigated by Solid-State NMR Spectroscopy and Molecular Dynamics Simulations

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Cholesterol-Mediated Clustering of the HIV Fusion Protein gp41 in Lipid Bilayers

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N-Glycans modulate tilting of HIV-1 envelope glycoprotein

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Conformational plasticity underlies membrane fusion induced by an HIV sequence juxtaposed to the lipid envelope

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Influenza hemagglutinin membrane anchor

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Topological analysis of the gp41 MPER on lipid bilayers relevant to the metastable HIV-1 envelope prefusion state

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Solution NMR: A powerful tool for structural and functional studies of membrane proteins in reconstituted environments

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N-Glycans Modulate HIV-1 Env Conformational Plasticity

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The Conserved Positive Charge in the Transmembrane Domain of HIV Gp41 Contributes to Its Intrinsic Preference for Trimerization

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Molecular Modeling of the HR2 and Transmembrane Domains of the SARS-CoV-2 S Protein in the Prefusion State

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