about
Designing inhibitors of cytochrome c/cardiolipin peroxidase complexes: mitochondria-targeted imidazole-substituted fatty acidsOrigins of Structural Flexibility in Protein-Based Supramolecular Polymers Revealed by DEER SpectroscopyCysteine-specific Cu2+ chelating tags used as paramagnetic probes in double electron electron resonance.Cu²⁺ as an ESR Probe of Protein Structure and Function.Rotameric preferences of a protein spin label at edge-strand β-sheet sites.Simulating the dynamics and orientations of spin-labeled side chains in a protein-DNA complex.Binding of copper(II) to thyrotropin-releasing hormone (TRH) and its analogs.An ESR analysis of the mechanism of pericyclic reactions of bicyclobutaneESEEM analysis of multi-histidine Cu(II)-coordination in model complexes, peptides, and amyloid-βTunable, mixed-resolution modeling using library-based Monte Carlo and graphics processing units.Protein structural studies by paramagnetic solid-state NMR spectroscopy aided by a compact cyclen-type Cu(II) binding tagInsights into copper coordination in the EcoRI-DNA complex by ESR spectroscopy.Substantial contribution of the two imidazole rings of the His13-His14 dyad to Cu(II) binding in amyloid-β(1-16) at physiological pH and its significance.The double-histidine Cu²⁺-binding motif: a highly rigid, site-specific spin probe for electron spin resonance distance measurements.Conformational Changes Underlying Desensitization of the Pentameric Ligand-Gated Ion Channel ELIC.Cu(II)-Zn(II) Cross-Modulation in Amyloid-Beta Peptide Binding: An X-ray Absorption Spectroscopy Study.Sensitive Cu2+-Cu2+ distance measurements in a protein-DNA complex by double-quantum coherence ESR.Zn(II) ions substantially perturb Cu(II) ion coordination in amyloid-β at physiological pH.Nucleotide-Independent Copper(II)-Based Distance Measurements in DNA by Pulsed ESR Spectroscopy.A simple double quantum coherence ESR sequence that minimizes nuclear modulations in Cu(2+)-ion based distance measurements.Electron spin resonance shows common structural features for different classes of EcoRI-DNA complexesAn approach towards the measurement of nanometer range distances based on Cu2+ ions and ESR.The second Cu(II)-binding site in a proton-rich environment interferes with the aggregation of amyloid-beta(1-40) into amyloid fibrils.Resolution of (129)Xe chemical shifts at ultralow magnetic field.Direct evidence that all three histidine residues coordinate to Cu(II) in amyloid-beta1-16.The Cu2+-nitrilotriacetic acid complex improves loading of α-helical double histidine site for precise distance measurements by pulsed ESR.On the use of the Cu2+-iminodiacetic acid complex for double histidine based distance measurements by pulsed ESR.Analysis of Nitroxide-Based Distance Measurements in Cell Extracts and in Cells by Pulsed ESR Spectroscopy.ESR Resolves the C Terminus Structure of the Ligand-free Human Glutathione S-Transferase A1-1.The aggregated state of amyloid-beta peptide in vitro depends on Cu2+ ion concentration.Distance Distributions of End-Labeled Curved Bispeptide Oligomers by Electron Spin ResonanceOn the Use of Q-Band DEER to Resolve the Relative Orientations of Two Double Histidine Bound Cu-Ions in a ProteinA theoretical approach to the analysis of arbitrary pulses in magnetic resonanceUnfolding of alanine-based peptides using electron spin resonance distance measurementsSuppression of electron spin-echo envelope modulation peaks in double quantum coherence electron spin resonanceOn Cu(II)-Cu(II) distance measurements using pulsed electron electron double resonanceParamagnetic metal ions in pulsed ESR distance distribution measurementsProgrammable Topology in New Families of Heterobimetallic Metal-Organic Frameworks19F Paramagnetic Relaxation-Based NMR for Quaternary Structural Restraints of Ion ChannelsMolecular Dynamics Simulations Based on Newly Developed Force Field Parameters for Cu2+ Spin Labels Provide Insights into Double-Histidine-Based Double Electron-Electron Resonance
P50
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P50
description
hulumtues
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researcher
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wetenschapper
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հետազոտող
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name
Sunil Saxena
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Sunil Saxena
@en
Sunil Saxena
@es
Sunil Saxena
@nl
Sunil Saxena
@sl
সুনীল সাক্সেনা
@bn
type
label
Sunil Saxena
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Sunil Saxena
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Sunil Saxena
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Sunil Saxena
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Sunil Saxena
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সুনীল সাক্সেনা
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prefLabel
Sunil Saxena
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Sunil Saxena
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Sunil Saxena
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Sunil Saxena
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Sunil Saxena
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সুনীল সাক্সেনা
@bn
P106
P1153
7402626357
P21
P31
P496
0000-0001-9098-6114
P569
2000-01-01T00:00:00Z