Pages that link to "Q34065509"

The following pages link to Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy (Q34065509):

Displaying 40 items.

• Quenched hydrogen/deuterium exchange NMR characterization of amyloid-beta peptide aggregates formed in the presence of Cu2 or Zn2 (Q24338939) (← links)
• Mechanisms of amyloid formation revealed by solution NMR (Q26797492) (← links)
• Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils (Q28388148) (← links)
• Aβ Peptide Fibrillar Architectures Controlled by Conformational Constraints of the Monomer (Q28744420) (← links)
• Induced beta-barrel formation of the Alzheimer's Abeta25-35 oligomers on carbon nanotube surfaces: implication for amyloid fibril inhibition (Q30157126) (← links)
• Effect of the amyloid β hairpin's structure on the handedness of helices formed by its aggregates. (Q30352016) (← links)
• Effect of benzyl alcohol on recombinant human interleukin-1 receptor antagonist structure and hydrogen-deuterium exchange (Q30402475) (← links)
• Interprotofilament interactions between Alzheimer's Abeta1-42 peptides in amyloid fibrils revealed by cryoEM (Q30438461) (← links)
• NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126. (Q30885520) (← links)
• Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level (Q34098577) (← links)
• Probing the Conformation of a Prion Protein Fibril with Hydrogen Exchange (Q34186501) (← links)
• The stability of monomeric intermediates controls amyloid formation: Abeta25-35 and its N27Q mutant (Q34546859) (← links)
• Human pancreatitis-associated protein forms fibrillar aggregates with a native-like conformation (Q34564980) (← links)
• NMR-based detection of hydrogen/deuterium exchange in liposome-embedded membrane proteins (Q35398997) (← links)
• Molecular alignment within beta-sheets in Abeta(14-23) fibrils: solid-state NMR experiments and theoretical predictions (Q35545486) (← links)
• Enhanced correction methods for hydrogen exchange-mass spectrometric studies of amyloid fibrils (Q36559830) (← links)
• Structural models of amyloid-like fibrils (Q36693082) (← links)
• Early stages of amyloid fibril formation studied by liquid-state NMR: the peptide hormone glucagon (Q36717607) (← links)
• The use of spin desalting columns in DMSO-quenched H/D-exchange NMR experiments. (Q36722239) (← links)
• Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR. (Q36925198) (← links)
• Structure-activity relationship of amyloid fibrils. (Q37549331) (← links)
• Controlling {beta}-amyloid oligomerization by the use of naphthalene sulfonates: trapping low molecular weight oligomeric species (Q40393792) (← links)
• Conserved core of amyloid fibrils of wild type and A30P mutant α‐synuclein (Q41845690) (← links)
• Increase in the conformational flexibility of beta 2-microglobulin upon copper binding: a possible role for copper in dialysis-related amyloidosis (Q41849521) (← links)
• Amide solvent protection analysis demonstrates that amyloid-beta(1-40) and amyloid-beta(1-42) form different fibrillar structures under identical conditions (Q42034358) (← links)
• Ca(2 ) enhances Aβ polymerization rate and fibrillar stability in a dynamic manner (Q43876883) (← links)
• Characterization of Amyloid Fibrils of Human β‐2‐Microglobulin by High‐Resolution Magic‐Angle Spinning NMR (Q44199195) (← links)
• Identification of a novel high affinity copper binding site in the APP(145-155) fragment of amyloid precursor protein. (Q45051155) (← links)
• Influence of Au nanoparticles on the aggregation of amyloid-β-(25-35) peptides (Q45173042) (← links)
• The polyphenol piceid destabilizes preformed amyloid fibrils and oligomers in vitro: hypothesis on possible molecular mechanisms (Q46230541) (← links)
• Lipid-induced conformational transition of the amyloid core fragment Abeta(28-35) and its A30G and A30I mutants (Q46636201) (← links)
• Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology (Q48175839) (← links)
• Suppression and dissolution of amyloid aggregates using ionic liquids. (Q52562272) (← links)
• A left-handed 3(1) helical conformation in the Alzheimer Abeta(12-28) peptide. (Q53258738) (← links)
• The solvent protection of alzheimer amyloid-beta-(1-42) fibrils as determined by solution NMR spectroscopy. (Q53272801) (← links)
• Study of the interaction between the amyloid beta peptide (1-40) and antioxidant compounds by nuclear magnetic resonance spectroscopy. (Q53314320) (← links)
• Probing Solvent Accessibility of Transthyretin Amyloid by Solution NMR Spectroscopy (Q57188082) (← links)
• Hydrogen/deuterium exchange mass spectrometry analysis of protein aggregates (Q79258627) (← links)
• Isotope-assisted vibrational circular dichroism investigations of amyloid β peptide fragment, Aβ(16–22) (Q84797817) (← links)
• Disordered versus Fibril-like Amyloid β (25−35) Dimers in Water: Structure and Thermodynamics (Q85235252) (← links)