Preparation and characterization of purified amyloid fibrils.

No abstract is available for this paper.

• Publication year

  2001

• Venue

  Journal of the American Chemical Society

• Publication date

  2001-08-22

• Fields of study

  Medicine, Chemistry

• Identifiers
  DOI 10.1021/JA016229BPMID 11506581
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid

  2001cited by this paper
• Protofilaments, filaments, ribbons, and fibrils from peptidomimetic self-assembly:  implications for amyloid fibril formation and materials science.

  2000cited by this paper
• Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy

  2000cited by this paper
• Protein engineering as a strategy to avoid formation of amyloid fibrils

  2000cited by this paper
• Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils.

  2000cited by this paper
• Cryo‐electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing

  1999cited by this paper
• Propagating structure of Alzheimer's beta-amyloid(10-35) is parallel beta-sheet with residues in exact register.

  1998cited by this paper
• The structure of amyloid fibrils by electron microscopy and X-ray diffraction.

  1997cited by this paper
• Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide

  1995cited by this paper
• The Alzheimer A beta peptide develops protease resistance in association with its polymerization into fibrils.

  1994cited by this paper
• Amyloidosis

  1994cited by this paper
• Amyloidosis: a final common pathway for protein deposition in tissues.

  1990cited by this paper
• Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins.

  1986cited by this paper

• Gaining insight into protein structure via ATR-FTIR spectroscopy

  2024cites this paper
• Cell-Penetrating Peptides: Promising Therapeutics and Drug-Delivery Systems for Neurodegenerative Diseases.

  2024cites this paper
• Plant-based protein amyloid fibrils: Origins, formation, extraction, applications, and safety.

  2024cites this paper
• Lysozyme Interaction with Phospholipid Nanodroplets Probed by Sum Frequency Scattering Vibrational Spectroscopy.

  2023cites this paper
• Sulfated Polysaccharides as a Fighter with Protein Non-Physiological Aggregation: The Role of Polysaccharide Flexibility and Charge Density

  2023cites this paper
• Wheat gluten amyloid fibrils: Conditions, mechanism, characterization, application, and future perspectives.

  2023cites this paper
• Raman spectroscopy and its plasmon-enhanced counterparts: A toolbox to probe protein dynamics and aggregation.

  2023cites this paper
• An Approach for In-Situ Detection of Gold Colloid Aggregates Amyloid Formations Within The Hippocampus of The Cohen's Alzheimer's Disease Rat Model By Surface Enhanced Raman Scattering Methods.

  2023cites this paper
• The Ability of Some Polysaccharides to Disaggregate Lysozyme Amyloid Fibrils and Renature the Protein

  2023cites this paper
• Synthetic, Cell-Derived, Brain-Derived, and Recombinant β-Amyloid: Modelling Alzheimer’s Disease for Research and Drug Development

  2022cites this paper
• Heat accelerates degradation of β-lactoglobulin fibrils at neutral pH

  2021cites this paper
• Glucosylceramide Associated with Gaucher Disease Forms Amyloid-like Twisted Ribbon Fibrils That Induce α-Synuclein Aggregation

  2021cites this paper
• Inhibition of fibrillation of human γd-crystallin by a flavonoid morin

  2020cites this paper
• Molecular Spectroscopic Markers of Abnormal Protein Aggregation

  2020influential citation
• Enhanced purification coupled with biophysical analyses shows cross-β structure as a core building block for Streptococcus mutans functional amyloids

  2020cites this paper
• Study of Nanofibrils Formation of Fibroin Protein in Specific Thermal and Acidity Conditions

  2020cites this paper
• Biological Functions of Prokaryotic Amyloids in Interspecies Interactions: Facts and Assumptions

  2020cites this paper
• Docking interactions determine early cleavage events in insulin proteolysis by pepsin: Experiment and simulation.

  2020cites this paper
• Structure-Function Relationship of Inclusion Bodies of a Multimeric Protein

  2020cites this paper
• Dissolution of Amyloid Aggregates in Aqueous Ionic Liquid Solutions: A Case Study of Insulin Amyloid

  2019cites this paper
• Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation.

  2019cites this paper
• Protein Nanofibrils as Storage Forms of Peptide Drugs and Hormones.

  2019cites this paper
• Identification of Amyloidogenic Regions in the Spine of Insulin Fibrils

  2019cites this paper
• Revisiting the conformational state of albumin conjugated to gold nanoclusters: A self-assembly pathway to giant superstructures unraveled

  2019cites this paper
• Recovery and cryopreservation of insulin amyloid using ionic liquids

  2018cites this paper
• Global transition of human serum albumin to prefibrillar aggregates induced by temsirolimus: Insight into implications of anti‐renal cancer drug

  2018cites this paper
• Amyloids Are Novel Cell-Adhesive Matrices.

  2018cites this paper
• Amyloid Fibrils: Versatile Biomaterials for Cell Adhesion and Tissue Engineering Applications.

  2018cites this paper
• Spectroscopic Signature for Stable β-Amyloid Fibrils versus β-Sheet-Rich Oligomers.

  2018cites this paper
• Global Protein Stabilization Does Not Suffice to Prevent Amyloid Fibril Formation.

  2018cites this paper
• A Free Energy Barrier Caused by the Refolding of an Oligomeric Intermediate Controls the Lag Time of Amyloid Formation by hIAPP.

  2017cites this paper
• Mellitate: A multivalent anion with extreme charge density causes rapid aggregation and misfolding of wild type lysozyme at neutral pH

  2017cites this paper
• High-Pressure-Driven Reversible Dissociation of α-Synuclein Fibrils Reveals Structural Hierarchy.

  2017cites this paper
• Assessment of structural properties of amyloid aggregates and their application potential

  2016cites this paper
• Suppression Effect on the Formation of Insulin Amyloid by the Use of Ionic Liquids

  2016cites this paper
• Highly Amyloidogenic Two-chain Peptide Fragments Are Released upon Partial Digestion of Insulin with Pepsin*♦

  2015cites this paper
• The role of proline‐containing peptide triads in β‐sheet formation: A kinetic study

  2015cites this paper
• From sequence to structure determinants of functional and non-functional protein aggregation /

  2015cites this paper
• Anesthetic 2,2,2-trifluoroethanol induces amyloidogenesis and cytotoxicity in human serum albumin.

  2015cites this paper
• Formation of lysozyme oligomers at model cell membranes monitored with sum frequency generation spectroscopy.

  2014cites this paper
• The role of protein hydrophobicity in conformation change and self-assembly into large amyloid fibers.

  2014cites this paper
• Protein aggregation and partial globular state in aqueous 1-alkyl-3-methylimidazolium nitrate solutions

  2014cites this paper
• Molecular Interaction between the Chaperone Hsc70 and the N-terminal Flank of Huntingtin Exon 1 Modulates Aggregation*

  2014cites this paper
• Methods for Studying and Structure–Function Relationships of Non-Fibrillar Protein Assemblies in Alzheimer's Disease and Related Disorders

  2014cites this paper
• Hydrophobic enhancement of Dopa-mediated adhesion in a mussel foot protein.

  2013cites this paper
• Evolution of the amyloid fiber over multiple length scales.

  2013cites this paper
• Application of Functional Amyloids in Morphological Control and in Self-assembled Composites

  2013cites this paper
• Lysine functionalised amyloid fibrils: the design and assembly of a TTR1-based peptide

  2013cites this paper
• IR spectroscopic analyses of amyloid fibril formation of β2-microglobulin using a simplified procedure for its in vitro generation at neutral pH.

  2013cites this paper
• Characterization of Large Amyloid Fibers and Tapes with Fourier Transform Infrared (FT-IR) and Raman Spectroscopy

  2013cites this paper
• Amyloid‐Like Fibrils: Origin, Structure, Properties, and Potential Technological Applications

  2013cites this paper
• Preparation, processing and applications of protein nanofibers

  2013cites this paper
• ATR-FTIR: a "rejuvenated" tool to investigate amyloid proteins.

  2013cites this paper
• Amyloid fibril formation from human and bovine serum albumin followed by quasi-simultaneous Fourier-transform infrared (FT-IR) spectroscopy and static light scattering (SLS)

  2012cites this paper
• Proteins Fibrils from a Polymer Physics Perspective

  2012cites this paper
• Millisecond-to-Minute Protein Folding/Misfolding Events Monitored by FTIR Spectroscopy

  2012cites this paper
• Native structure protects SUMO proteins from aggregation into amyloid fibrils.

  2012cites this paper
• Yeast Prions: Their Assembly into Protein Fibrils and the Role of Assembly Modulators

  2012cites this paper
• Hexafluoroisopropanol induces self‐assembly of β‐amyloid peptides into highly ordered nanostructures

  2012cites this paper
• Overview of Fibrillar and Oligomeric Assemblies of Amyloidogenic Proteins

  2012cites this paper
• Biophysical characterisation of thermal-induced precipitates of recombinant anthrax protective antigen: evidence for kinetically trapped unfolding domains in solid-state.

  2012cites this paper
• SERDP WP-1756

  2012cites this paper
• Oligomeric intermediates in amyloid formation: structure determination and mechanisms of toxicity.

  2012cites this paper
• Scaling up the production of protein nanofibres

  2011cites this paper
• Imaging secondary structure of individual amyloid fibrils of a β2-microglobulin fragment using near-field infrared spectroscopy.

  2011cites this paper
• Bovine Serum Albumin protofibril-like aggregates formation: solo but not simple mechanism.

  2011cites this paper
• Metastability of native proteins and the phenomenon of amyloid formation.

  2011cites this paper
• Functional fibrils derived from the peptide TTR1-cycloRGDfK that target cell adhesion and spreading.

  2011cites this paper
• Self-folding and aggregation of amyloid nanofibrils.

  2011cites this paper
• Nanomaterials: amyloids reflect their brighter side

  2011cites this paper
• Peptide mixtures can self-assemble into large amyloid fibers of varying size and morphology.

  2011cites this paper
• Specific mutations alter fibrillation kinetics, fiber morphologies, and membrane interactions of pentapeptides derived from human calcitonin.

  2010cites this paper
• Isolation of short peptide fragments from alpha-synuclein fibril core identifies a residue important for fibril nucleation: a possible implication for diagnostic applications.

  2010cites this paper
• Three‐Dimensional Characterization of Helical Silver Nanochains Mediated by Protein Assemblies

  2010cites this paper
• Characterization of amyloidogenic intermediate states through a combined use of CD and NMR spectroscopy.

  2010cites this paper
• Atomistic simulation of nanomechanical properties of Alzheimer's Abeta(1-40) amyloid fibrils under compressive and tensile loading.

  2010cites this paper
• Formation of amyloid fibrils in vitro from partially unfolded intermediates of human gammaC-crystallin.

  2010cites this paper
• Études biophysiques d'un peptide amyloïde et de ses interactions avec des membranes modèles

  2010cites this paper
• Failure of Alzheimer’s Aβ(1–40) amyloid nanofibrils under compressive loading

  2010cites this paper
• High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure .

  2010cites this paper
• Peptide Self-Assembly from the Molecular to the Macroscopic Scale at Standard Conditions

  2010influential citation
• Aggregation of Alzheimer amyloid beta peptide (1-42) on the multivalent sulfonated sugar interface.

  2010cites this paper
• Enzyme-mediated self-assembly of highly ordered structures from disordered proteins

  2009cites this paper
• Incorporating glucose oxidase activity into amyloid fibrils

  2009influential citation
• Self-assembly of Bacteriophage-associated Hyaluronate Lyase (HYLP2) into an Enzymatically Active Fibrillar Film*

  2009cites this paper
• Protein nanofibres of defined morphology prepared from mixtures of crude crystallins

  2009cites this paper
• Characterization of oligomeric species on the aggregation pathway of human lysozyme.

  2009cites this paper
• Surface- and Solution-Based Assembly of Amyloid Fibrils for Biomedical and Nanotechnology Applications

  2009cites this paper
• Structure and sequence determinants of aggregation investigated with molecular dynamics.

  2009influential citation
• Cutting edge structural protein from the jaws of Nereis virens.

  2008cites this paper
• Formation of amyloid fibrils in vitro by human γD-crystallin and its isolated domains

  2008cites this paper
• Investigating the mechanism of peptide aggregation: insights from mixed monte carlo-molecular dynamics simulations.

  2008cites this paper
• Assembly of the asparagine- and glutamine-rich yeast prions into protein fibrils.

  2008cites this paper
• Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders.

  2008cites this paper
• Early stages of misfolding and association of beta2-microglobulin: insights from infrared spectroscopy and dynamic light scattering.

  2008cites this paper
• Fibril formation of hsp10 homologue proteins and determination of fibril core regions: differences in fibril core regions dependent on subtle differences in amino acid sequence.

  2008cites this paper
• A Common β-Sheet Architecture Underlies in Vitro and in Vivo β2-Microglobulin Amyloid Fibrils*S⃞

  2008cites this paper
• Amyloid Fibrils: From Disease to Design. New Biomaterial Applications for Self-Assembling Cross-β Fibrils

  2007cites this paper
• The Yeast Prion Proteins Sup35p and Ure2p

  2007cites this paper
• Alpha-sheet: The toxic conformer in amyloid diseases?

  2006cites this paper