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Detection and structural characterization of insulin prefibrilar oligomers using surface enhanced Raman spectroscopy

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What this work says

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

inferredcites →https://doi.org/10.1002/9783527619344openalex-snapshot
Amyloid Proteins
inferredcites →https://doi.org/10.1002/btpr.1812openalex-snapshot
Protein misfolding and aggregation research: Some thoughts on improving quality and utility
inferredcites →https://doi.org/10.1002/jbio.200710013openalex-snapshot
Hen egg white lysozyme fibrillation: a deep‐UV resonance Raman spectroscopic study
inferredcites →https://doi.org/10.1002/jrs.2359openalex-snapshot
Tip‐enhanced Raman scattering studies of histidine on novel silver substrates
inferredcites →https://doi.org/10.1002/prot.22169openalex-snapshot
A universal pathway for amyloid nucleus and precursor formation for insulin
inferredcites →https://doi.org/10.1002/prot.22417openalex-snapshot
Time‐dependent insulin oligomer reaction pathway prior to fibril formation: Cooling and seeding
inferredcites →https://doi.org/10.1006/jsbi.2000.4222openalex-snapshot
Review: Amyloidogenesis—Unquestioned Answers and Unanswered Questions
inferredcites →https://doi.org/10.1007/s00216-007-1667-3openalex-snapshot
SERS: a versatile tool in chemical and biochemical diagnostics
inferredcites →https://doi.org/10.1007/s00216-009-2702-3openalex-snapshot
Surface-enhanced Raman scattering for protein detection
inferredcites →https://doi.org/10.1016/0014-5793(83)80277-4openalex-snapshot
Biochemical Applications of Raman and Resonance Raman Spectroscopies
inferredcites →https://doi.org/10.1016/0022-2860(84)85077-2openalex-snapshot
Biochemical applications of Raman and resonance Raman spectroscopies
inferredcites →https://doi.org/10.1016/0924-2031(93)87032-oopenalex-snapshot
New developments in Raman spectroscopy of biological systems
inferredcites →https://doi.org/10.1016/j.bbapap.2010.04.001openalex-snapshot
Molecular mechanism of Thioflavin-T binding to amyloid fibrils
inferredcites →https://doi.org/10.1016/j.bbrc.2011.03.090openalex-snapshot
Serum amyloid A 2.2 refolds into a octameric oligomer that slowly converts to a more stable hexamer
inferredcites →https://doi.org/10.1016/j.bios.2011.12.056openalex-snapshot
Highly sensitive SERS detection of cancer proteins in low sample volume using hollow core photonic crystal fiber
inferredcites →https://doi.org/10.1016/j.bpj.2008.12.3957openalex-snapshot
Bovine Insulin Filaments Induced by Reducing Disulfide Bonds Show a Different Morphology, Secondary Structure, and Cell Toxicity from Intact Insulin Amyloid Fibrils
inferredcites →https://doi.org/10.1016/j.bpj.2010.10.010openalex-snapshot
Probing the Nucleus Model for Oligomer Formation during Insulin Amyloid Fibrillogenesis
inferredcites →https://doi.org/10.1016/j.cell.2007.10.014openalex-snapshot
Semen-Derived Amyloid Fibrils Drastically Enhance HIV Infection
inferredcites →https://doi.org/10.1016/s0006-3495(00)76359-4openalex-snapshot
Characterization of the Oligomeric States of Insulin in Self-Assembly and Amyloid Fibril Formation by Mass Spectrometry
inferredcites →https://doi.org/10.1016/s0014-5793(97)00076-8openalex-snapshot
Mechanochemical mechanism for peptidyl free radical generation by amyloid fibrils
inferredcites →https://doi.org/10.1016/s0022-2836(03)00536-9openalex-snapshot
Insulin Assembly Damps Conformational Fluctuations: Raman Analysis of Amide I Linewidths in Native States and Fibrils
inferredcites →https://doi.org/10.1021/bi002555copenalex-snapshot
Effect of Environmental Factors on the Kinetics of Insulin Fibril Formation: Elucidation of the Molecular Mechanism
inferredcites →https://doi.org/10.1021/cr200198aopenalex-snapshot
UV Resonance Raman Investigations of Peptide and Protein Structure and Dynamics
inferredcites →https://doi.org/10.1021/ja070038copenalex-snapshot
Probing a Fibrillation Nucleus Directly by Deep Ultraviolet Raman Spectroscopy
inferredcites →https://doi.org/10.1021/ja303263yopenalex-snapshot
Structure and Composition of Insulin Fibril Surfaces Probed by TERS
inferredcites →https://doi.org/10.1021/ja309300dopenalex-snapshot
Structure Enhancement Factor Relationships in Single Gold Nanoantennas by Surface-Enhanced Raman Excitation Spectroscopy
inferredcites →https://doi.org/10.1021/la049454qopenalex-snapshot
Effect of Surface Wettability on the Adhesion of Proteins
inferredcites →https://doi.org/10.1021/la1041794openalex-snapshot
Protein-Associated Water and Secondary Structure Effect Removal of Blood Proteins from Metallic Substrates
inferredcites →https://doi.org/10.1021/nl0808132openalex-snapshot
Nanofluidic Biosensing for β-Amyloid Detection Using Surface Enhanced Raman Spectroscopy
inferredcites →https://doi.org/10.1038/nature02261openalex-snapshot
Protein folding and misfolding
inferredcites →https://doi.org/10.1038/nm1782openalex-snapshot
Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
inferredcites →https://doi.org/10.1038/nrn2168openalex-snapshot
Intracellular amyloid-β in Alzheimer's disease
inferredcites →https://doi.org/10.1039/b708459popenalex-snapshot
SERS—a single-molecule and nanoscale tool for bioanalytics
inferredcites →https://doi.org/10.1039/c2an36478fopenalex-snapshot
Amide I vibrational mode suppression in surface (SERS) and tip (TERS) enhanced Raman spectra of protein specimens
inferredcites →https://doi.org/10.1042/bj20030422openalex-snapshot
Suppression by polycyclic compounds of the conversion of human amylin into insoluble amyloid
inferredcites →https://doi.org/10.1073/pnas.0904532106openalex-snapshot
Mechanism of amyloid plaque formation suggests an intracellular basis of Aβ pathogenicity
inferredcites →https://doi.org/10.1073/pnas.0910080106openalex-snapshot
Molecular basis for insulin fibril assembly
inferredcites →https://doi.org/10.1073/pnas.1218402110openalex-snapshot
Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
inferredcites →https://doi.org/10.1074/jbc.m109.069542openalex-snapshot
Fibrillar Oligomers Nucleate the Oligomerization of Monomeric Amyloid β but Do Not Seed Fibril Formation
inferredcites →https://doi.org/10.1074/jbc.m110.133108openalex-snapshot
Resveratrol Selectively Remodels Soluble Oligomers and Fibrils of Amyloid Aβ into Off-pathway Conformers
inferredcites →https://doi.org/10.1074/jbc.m305466200openalex-snapshot
Targeted Control of Kinetics of β-Amyloid Self-association by Surface Tension-modifying Peptides
inferredcites →https://doi.org/10.1074/jbc.r800016200openalex-snapshot
Structural Classification of Toxic Amyloid Oligomers
inferredcites →https://doi.org/10.1093/jb/mvi101openalex-snapshot
Improved Estimation of the Secondary Structures of Proteins by Vacuum-Ultraviolet Circular Dichroism Spectroscopy
inferredcites →https://doi.org/10.1101/cshperspect.a004507openalex-snapshot
Chemical and Biological Approaches for Adapting Proteostasis to Ameliorate Protein Misfolding and Aggregation Diseases-Progress and Prognosis
inferredcites →https://doi.org/10.1110/ps.062639307openalex-snapshot
The first step of hen egg white lysozyme fibrillation, irreversible partial unfolding, is a two‐state transition
inferredcites →https://doi.org/10.1111/j.1742-4658.2005.05022.xopenalex-snapshot
Mechanisms of amyloid fibril self‐assembly and inhibition
inferredcites →https://doi.org/10.1111/j.1742-4658.2009.07307.xopenalex-snapshot
The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds
inferredcites →https://doi.org/10.1126/science.1079469openalex-snapshot
Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis
inferredcites →https://doi.org/10.1146/annurev.anchem.1.031207.112814openalex-snapshot
Surface-Enhanced Raman Spectroscopy
inferredcites →https://doi.org/10.1186/1750-1326-2-18openalex-snapshot
Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers
inferredcites →https://doi.org/10.1186/1750-1326-5-57openalex-snapshot
Conformation dependent monoclonal antibodies distinguish different replicating strains or conformers of prefibrillar Aβ oligomers
inferredcites →https://doi.org/10.1371/journal.pbio.0050134openalex-snapshot
A Helical Structural Nucleus Is the Primary Elongating Unit of Insulin Amyloid Fibrils
inferredcites →https://doi.org/10.1371/journal.pone.0020072openalex-snapshot
Evaluating Nuclei Concentration in Amyloid Fibrillation Reactions Using Back-Calculation Approach
inferredcites →https://doi.org/10.1371/journal.pone.0036989openalex-snapshot
Disulfide Bridges Remain Intact while Native Insulin Converts into Amyloid Fibrils
inferredcites →https://doi.org/10.1529/biophysj.104.048843openalex-snapshot
Amyloidogenic Self-Assembly of Insulin Aggregates Probed by High Resolution Atomic Force Microscopy
inferredcites →https://doi.org/10.1529/biophysj.106.098608openalex-snapshot
A Three-Stage Kinetic Model of Amyloid Fibrillation
inferredcites →https://doi.org/10.2174/092986606775338362openalex-snapshot
Protein Aggregation and Its Consequences for Human Disease
inferredcites →https://doi.org/10.2174/138920309789352038openalex-snapshot
Formation Mechanism of Insulin Fibrils and Structural Aspects of the Insulin Fibrillation Process
inferredcites →https://doi.org/10.2217/nnm.11.117openalex-snapshot
Advances in Localized Surface Plasmon Resonance Spectroscopy Biosensing
inferredcites →https://doi.org/10.55782/ane-2003-1463openalex-snapshot
Alzheimer's β-amyloid peptide as a source of neurotoxic free radicals: the role of structural effects

What points at this work

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

inferred← citeshttps://doi.org/10.2139/ssrn.4815261openalex-extracted
Developing a Biosensing Prototype Utilising 7cb Liquid Crystal for Human Insulin Detection
inferred← citeshttps://doi.org/10.1002/9780470027318.a9574openalex-snapshot
Surface‐Enhanced R aman Scattering of Biological Materials
inferred← citeshttps://doi.org/10.1002/ange.202010331openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/anie.202010331openalex-snapshot
Nanoscale Hyperspectral Imaging of Amyloid Secondary Structures in Liquid
inferred← citeshttps://doi.org/10.1002/cbic.201900394openalex-snapshot
Nanoscale Structural Organization of Insulin Fibril Polymorphs Revealed by Atomic Force Microscopy–Infrared Spectroscopy (AFM‐IR)
inferred← citeshttps://doi.org/10.1002/cnma.201900035openalex-snapshot
Spot‐on SERS Detection of Biomolecules with Laser‐Patterned Dot Arrays of Assembled Silver Nanowires
inferred← citeshttps://doi.org/10.1016/b978-0-323-99127-8.00016-7openalex-snapshot
Spectroscopic methods to detect and analyze protein oligomerization, aggregation, and fibrillation
inferred← citeshttps://doi.org/10.1016/j.apsusc.2019.144991openalex-snapshot
Amyloid aggregation at solid-liquid interfaces: Perspectives of studies using model surfaces
inferred← citeshttps://doi.org/10.1016/j.pdpdt.2023.103796openalex-snapshot
Characterization of structural changes occurring in insulin at different time intervals at room temperature by surface-enhanced Raman spectroscopy
inferred← citeshttps://doi.org/10.1016/j.snb.2018.06.029openalex-snapshot
A self-calibrated 2D nanoarchitecture for label-free SERS quantitation and distribution imaging of target
inferred← citeshttps://doi.org/10.1016/j.snb.2020.128519openalex-snapshot
Three-dimensional ordered Ag/ZnO/Si hierarchical nanoflower arrays for spatially uniform and ultrasensitive SERS detection
inferred← citeshttps://doi.org/10.1016/j.xphs.2015.10.023openalex-snapshot
Characterization of Sizes of Aggregates of Insulin Analogs and the Conformations of the Constituent Protein Molecules: A Concomitant Dynamic Light Scattering and Raman Spectroscopy Study
inferred← citeshttps://doi.org/10.1021/acs.chemrev.3c00494openalex-snapshot
Advanced Techniques for Detecting Protein Misfolding and Aggregation in Cellular Environments
inferred← citeshttps://doi.org/10.1021/acs.jpcc.7b04787openalex-snapshot
Unraveling the Near- and Far-Field Relationship of 2D Surface-Enhanced Raman Spectroscopy Substrates Using Wavelength-Scan Surface-Enhanced Raman Excitation Spectroscopy
inferred← citeshttps://doi.org/10.1021/acsnano.6b07523openalex-snapshot
Site-Selective Surface-Enhanced Raman Detection of Proteins
inferred← citeshttps://doi.org/10.1039/c4nr05704jopenalex-snapshot
Concave gold nanocube assemblies as nanotraps for surface-enhanced Raman scattering-based detection of proteins
inferred← citeshttps://doi.org/10.1039/c5an00342copenalex-snapshot
Exploring the structure and formation mechanism of amyloid fibrils by Raman spectroscopy: a review
inferred← citeshttps://doi.org/10.1039/c7cp06838gopenalex-snapshot
Electrochemical surface-enhanced Raman spectroscopy (EC-SERS) study of the interaction between protein aggregates and biomimetic membranes
inferred← citeshttps://doi.org/10.1039/d4cp03205eopenalex-snapshot
Developing a biosensing prototype utilising a 7CB liquid crystal for human insulin detection
inferred← citeshttps://doi.org/10.1080/05704928.2024.2367450openalex-snapshot
Fabrication method of colloidal dispersions and substrates for detection of pesticide, veterinary drug, and biomolecule using surfaced-enhanced Raman spectroscopy: a review
inferred← citeshttps://doi.org/10.1101/2020.08.26.267799openalex-snapshot
Mechanistic Studies of the Stabilization of Insulin Helical Structure by Coomassie Brilliant Blue
inferred← citeshttps://doi.org/10.1364/aop.479884openalex-snapshot
Advances in Raman spectroscopy and imaging for biomedical research
inferred← citeshttps://doi.org/10.1515/ntrev-2025-0279openalex-snapshot
Nanoparticles as SERS substrates: recent progress in hormone sensing
inferred← citeshttps://doi.org/10.17879/freeneuropathology-2022-4210openalex-snapshot
From Research to Diagnostic Application of Raman Spectroscopy in Neurosciences: Past and Perspectives
inferred← citeshttps://doi.org/10.3390/ijms22126435openalex-snapshot
Amyloid Prefibrillar Oligomers: The Surprising Commonalities in Their Structure and Activity
inferred← citeshttps://doi.org/10.3390/ijms232415811openalex-snapshot
Current Insights on the Use of Insulin and the Potential Use of Insulin Mimetics in Targeting Insulin Signalling in Alzheimer’s Disease
inferred← citeshttps://doi.org/10.3390/molecules25112498openalex-snapshot
Molecular Spectroscopic Markers of Abnormal Protein Aggregation
inferred← citeshttps://doi.org/10.3390/nano13172391openalex-snapshot
Tin/Tin Oxide Nanostructures: Formation, Application, and Atomic and Electronic Structure Peculiarities
inferred← citeshttps://doi.org/10.5281/zenodo.30874openalex-snapshot
The Utilization Of Genetic Approaches For Effective Conservation Of Endangered Species Congress Project, Regional Workshop, Zvolen, January 25– 27, 2012
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