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Thermally induced denaturation and aggregation of BLG-A: effect of the Cu2+ and Zn2+ metal ions
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1006/bbrc.2001.5263openalex-snapshot
Inhibitory Effect of Copper(II) on Zinc(II)-Induced Aggregation of Amyloid β-Peptide
inferredcites →https://doi.org/10.1006/jmbi.2001.4661openalex-snapshot
Kidney dialysis-associated amyloidosis: a molecular role for copper in fiber formation
inferredcites →https://doi.org/10.1007/978-1-4615-7658-7openalex-snapshot
Principles of Fluorescence Spectroscopy
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Principles of Fluorescence Spectroscopy
inferredcites →https://doi.org/10.1007/s00018-003-3447-3openalex-snapshot
Investigation of the effects of copper ions on protein aggregation using a model system
inferredcites →https://doi.org/10.1007/s00249-005-0041-7openalex-snapshot
Metal binding in amyloid β-peptides shows intra- and inter-peptide coordination modes
inferredcites →https://doi.org/10.1016/0003-9861(74)90298-7openalex-snapshot
Structural implications derived from the analysis of electron paramagnetic resonance spectra of natural and artificial copper proteins
inferredcites →https://doi.org/10.1016/0167-4838(94)00225-6openalex-snapshot
Thermal denaturation of β-lactoglobulin: effect of protein concentration at pH 6.75 and 8.05
inferredcites →https://doi.org/10.1016/0260-8774(88)90038-6openalex-snapshot
Functional properties of food macromolecules
inferredcites →https://doi.org/10.1016/j.bbapap.2003.12.008openalex-snapshot
Conformational constraints for amyloid fibrillation: the importance of being unfolded
inferredcites →https://doi.org/10.1016/j.bbapap.2007.06.008openalex-snapshot
Aggregation and fibrillation of bovine serum albumin
inferredcites →https://doi.org/10.1016/j.bpc.2003.09.004openalex-snapshot
Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering
inferredcites →https://doi.org/10.1016/j.foodhyd.2006.07.007openalex-snapshot
Denaturation and aggregation processes in thermal gelation of whey proteins resolved by differential scanning calorimetry
inferredcites →https://doi.org/10.1016/s0022-2836(02)00856-2openalex-snapshot
Amyloidogenic Unfolding Intermediates Differentiate Sheep Prion Protein Variants
inferredcites →https://doi.org/10.1016/s0076-6879(99)09020-5openalex-snapshot
[18] Quantification of β-sheet amyloid fibril structures with thioflavin T
inferredcites →https://doi.org/10.1016/s0268-005x(98)00056-3openalex-snapshot
Heat induced aggregation and gelation of β-lactoglobulin in the presence of κ-carrageenan
inferredcites →https://doi.org/10.1016/s0301-4622(03)00134-0openalex-snapshot
Kinetics of heat- and acidification-induced aggregation of firefly luciferase
inferredcites →https://doi.org/10.1016/s0924-2244(02)00133-4openalex-snapshot
Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins
inferredcites →https://doi.org/10.1016/s0968-0004(99)01445-0openalex-snapshot
Protein misfolding, evolution and disease
inferredcites →https://doi.org/10.1016/s0969-2126(97)00205-0openalex-snapshot
Bovine β-lactoglobulin at 1.8 Å resolution — still an enigmatic lipocalin
inferredcites →https://doi.org/10.1016/s1359-0278(98)00002-9openalex-snapshot
Protein aggregation: folding aggregates, inclusion bodies and amyloid
inferredcites →https://doi.org/10.1017/s0022029900028235openalex-snapshot
Thermal gelation and denaturation of bovine β-lactoglobulins A and B
inferredcites →https://doi.org/10.1021/bi00367a014openalex-snapshot
Why does ribonuclease irreversibly inactivate at high temperatures?
inferredcites →https://doi.org/10.1021/bi034879hopenalex-snapshot
Aggregation of Bovine Insulin Probed by DSC/PPC Calorimetry and FTIR Spectroscopy
inferredcites →https://doi.org/10.1021/bi0606748openalex-snapshot
Exothermic Effects Observed upon Heating of β2-Microglobulin Monomers in the Presence of Amyloid Seeds
inferredcites →https://doi.org/10.1021/bi602403vopenalex-snapshot
Heat-Triggered Conversion of Protofibrils into Mature Amyloid Fibrils of β2-Microglobulin
inferredcites →https://doi.org/10.1021/bi991518mopenalex-snapshot
Aggregation Events Occur Prior to Stable Intermediate Formation during Refolding of Interleukin 1β
inferredcites →https://doi.org/10.1021/jf960789qopenalex-snapshot
Heat-Induced Aggregation of β-Lactoglobulin: Role of the Free Thiol Group and Disulfide Bonds
inferredcites →https://doi.org/10.1023/a:1015277805345openalex-snapshot
Kinetics of Protein Aggregation. Quantitative Estimation of the Chaperone-Like Activity in Test-Systems Based on Suppression of Protein Aggregation
inferredcites →https://doi.org/10.1038/nature01891openalex-snapshot
Rationalization of the effects of mutations on peptide andprotein aggregation rates
inferredcites →https://doi.org/10.1038/nm1066openalex-snapshot
Protein aggregation and neurodegenerative disease
inferredcites →https://doi.org/10.1038/nrd1695openalex-snapshot
Protein drug stability: a formulation challenge
inferredcites →https://doi.org/10.1039/b314086eopenalex-snapshot
Hydration and structure—the two sides of the insulin aggregation process
inferredcites →https://doi.org/10.1039/b403014aopenalex-snapshot
Aggregation across the length-scales in β-lactoglobulin
inferredcites →https://doi.org/10.1039/b406180bopenalex-snapshot
The sulfinic acid switch in proteins
inferredcites →https://doi.org/10.1063/1.1622380openalex-snapshot
Effect of protein–protein interactions on protein aggregation kinetics
inferredcites →https://doi.org/10.1073/pnas.0407881102openalex-snapshot
Structural characterization of copper(II) binding to α-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease
inferredcites →https://doi.org/10.1073/pnas.77.8.4425openalex-snapshot
Observation of an exothermic process associated with the in vitro polymerization of brain tubulin.
inferredcites →https://doi.org/10.1074/jbc.273.21.12817openalex-snapshot
Dramatic Aggregation of Alzheimer Aβ by Cu(II) Is Induced by Conditions Representing Physiological Acidosis
inferredcites →https://doi.org/10.1097/00001756-199903170-00011openalex-snapshot
Oxidative stress induces amyloid-like aggregate formation of NACP/α-synuclein in vitro
inferredcites →https://doi.org/10.1110/ps.0217702openalex-snapshot
A kinetic study of β‐lactoglobulin amyloid fibril formation promoted by urea
inferredcites →https://doi.org/10.1110/ps.03445704openalex-snapshot
Increase in the conformational flexibility of β2‐microglobulin upon copper binding: A possible role for copper in dialysis‐related amyloidosis
inferredcites →https://doi.org/10.1110/ps.29002openalex-snapshot
The solution structure of human β2‐microglobulin reveals the prodromes of its amyloid transition
inferredcites →https://doi.org/10.1110/ps.42501openalex-snapshot
Conformational characterization of oligomeric intermediates and aggregates in β‐lactoglobulin heat aggregation
inferredcites →https://doi.org/10.1111/j.1471-4159.1993.tb03639.xopenalex-snapshot
Aluminum, Iron, and Zinc Ions Promote Aggregation of Physiological Concentrations of β‐Amyloid Peptide
inferredcites →https://doi.org/10.1126/science.8073293openalex-snapshot
Rapid induction of Alzheimer A beta amyloid formation by zinc
inferredcites →https://doi.org/10.1134/s000629790603014xopenalex-snapshot
Change in kinetic regime of protein aggregation with temperature increase. Thermal aggregation of rabbit muscle creatine kinase
inferredcites →https://doi.org/10.1146/annurev.biochem.66.1.385openalex-snapshot
MODELS OF AMYLOID SEEDING IN ALZHEIMER'S DISEASE AND SCRAPIE: Mechanistic Truths and Physiological Consequences of the Time-Dependent Solubility of Amyloid Proteins
inferredcites →https://doi.org/10.3168/jds.s0022-0302(04)73222-1openalex-snapshot
Invited Review: β-Lactoglobulin: Binding Properties, Structure, and Function
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1002/admi.202001060openalex-snapshot
Amyloid‐Mediated Fabrication of Organic–Inorganic Hybrid Materials and Their Biomedical Applications
inferred← citeshttps://doi.org/10.1002/ange.202204787openalex-snapshot
Water‐Soluble Melanin–Protein–Fe/Cu Conjugates Derived from Norepinephrine as Reliable Models for Neuromelanin of Human Brain Locus Coeruleus
inferred← citeshttps://doi.org/10.1002/anie.202204787openalex-snapshot
Water‐Soluble Melanin–Protein–Fe/Cu Conjugates Derived from Norepinephrine as Reliable Models for Neuromelanin of Human Brain Locus Coeruleus
inferred← citeshttps://doi.org/10.1002/biof.1121openalex-snapshot
Correlation between Al3+‐induced thermal stability and inhibition of fibrillation of N‐terminal domain of the hydrogenase maturation factor
inferred← citeshttps://doi.org/10.1002/chem.201402690openalex-snapshot
Multifunctional 8‐Hydroxyquinoline‐Appended Cyclodextrins as New Inhibitors of Metal‐Induced Protein Aggregation
inferred← citeshttps://doi.org/10.1002/jps.23076openalex-snapshot
Comparison of High-Throughput Biophysical Methods to Identify Stabilizing Excipients for a Model IgG2 Monoclonal Antibody: Conformational Stability and Kinetic Aggregation Measurements
inferred← citeshttps://doi.org/10.1002/smll.201000210openalex-snapshot
Microfluidic Rheometer for Characterization of Protein Unfolding and Aggregation in Microflows
inferred← citeshttps://doi.org/10.1007/s10953-017-0612-0openalex-snapshot
Thermal Aggregation of Bovine Serum Albumin in Conventional Buffers: An Insight into Molecular Level Interactions
inferred← citeshttps://doi.org/10.1007/s12551-012-0098-3openalex-snapshot
Application and use of differential scanning calorimetry in studies of thermal fluctuation associated with amyloid fibril formation
inferred← citeshttps://doi.org/10.1016/j.bmcl.2009.11.132openalex-snapshot
Chaperone-like activity of the acute-phase component human serum α1-acid glycoprotein: Inhibition of thermal- and chemical-induced aggregation of various proteins
inferred← citeshttps://doi.org/10.1016/j.chemosphere.2022.137088openalex-snapshot
Aggregation Behaviour of Black Carbon in Aquatic Solution: Effect of Ionic Strength and Coexisting Metals
inferred← citeshttps://doi.org/10.1016/j.clay.2022.106746openalex-snapshot
Insight into mechanisms of heavy metal-induced natural clay aggregation
inferred← citeshttps://doi.org/10.1016/j.envpol.2019.01.007openalex-snapshot
Systematic studies on the binding of metal ions in aggregates of humic acid: Aggregation kinetics, spectroscopic analyses and MD simulations
inferred← citeshttps://doi.org/10.1016/j.foodchem.2009.03.043openalex-snapshot
Copper modulates the heat-induced sulfhydryl/disulfide interchange reactions of β-Lactoglobulin
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2013.06.024openalex-snapshot
Effect of hydrolysis of soy β-conglycinin on the oxidative stability of O/W emulsions
inferred← citeshttps://doi.org/10.1016/j.foodres.2022.112298openalex-snapshot
Insights into the trace Sr2+ impact on the gel properties and spatial structure of mutton myofibrillar proteins
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2011.05.011openalex-snapshot
Early stage aggregation of human serum albumin in the presence of metal ions
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2012.04.024openalex-snapshot
Fibrillation of hen egg white lysozyme triggers reduction of copper(II)
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2015.02.014openalex-snapshot
Evidence of two oxidation states of copper during aggregation of hen egg white lysozyme (HEWL)
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2016.08.014openalex-snapshot
Resveratrol induces thermal stabilization of human serum albumin and modulates the early aggregation stage
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2009.10.021openalex-snapshot
Dual role of Zn2+ in maintaining structural integrity and suppressing deacetylase activity of SIRT1
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2014.04.003openalex-snapshot
Metal ions modulate thermal aggregation of beta-lactoglobulin: A joint chemical and physical characterization
inferred← citeshttps://doi.org/10.1016/j.lwt.2021.112557openalex-snapshot
Effects of divalent cations on the physical, conformational and immunological properties of bovine allergen β-lactoglobulin aggregates
inferred← citeshttps://doi.org/10.1016/j.patbio.2014.02.001openalex-snapshot
Conformational and thermal characterization of a synthetic peptidic fragment inspired from human tropoelastin: Signature of the amyloid fibers
inferred← citeshttps://doi.org/10.1021/acs.biomac.5b00371openalex-snapshot
Ferric Ions Inhibit the Amyloid Fibrillation of β-Lactoglobulin at High Temperature
inferred← citeshttps://doi.org/10.1021/acs.jafc.3c03192openalex-snapshot
New Perspectives on Food Matrix Modulation of Food Allergies: Immunomodulation and Component Interactions
inferred← citeshttps://doi.org/10.1021/acs.jpcb.9b09925openalex-snapshot
Effects of Polar Head Nature and Tail Length of Single-Chain Lipids on the Conformational Stability of β-Lactoglobulin
inferred← citeshttps://doi.org/10.1021/acsnano.9b01392openalex-snapshot
Sn-Triggered Two-Dimensional Fast Protein Assembly with Emergent Functions
inferred← citeshttps://doi.org/10.1021/jp103876popenalex-snapshot
Fibrillation in Human Serum Albumin Is Enhanced in the Presence of Copper(II)
inferred← citeshttps://doi.org/10.1039/c1sm06643aopenalex-snapshot
Inhibiting, promoting, and preserving stability of functional proteinfibrils
inferred← citeshttps://doi.org/10.1039/c2sm27408fopenalex-snapshot
Catalytic activity of copper ions in the amyloid fibrillation of β-lactoglobulin
inferred← citeshttps://doi.org/10.1039/c6ra24570fopenalex-snapshot
Curcumin inhibits the Al( iii ) and Zn( ii ) induced amyloid fibrillation of β-lactoglobulin in vitro
inferred← citeshttps://doi.org/10.1039/d0en00373eopenalex-snapshot
Aggregation and deposition behaviors of dissolved black carbon with coexisting heavy metals in aquatic solution
inferred← citeshttps://doi.org/10.1080/07391102.2013.819300openalex-snapshot
Fibrillation of human serum albumin shows nonspecific coordination on stoichiometric increment of Copper(II)
inferred← citeshttps://doi.org/10.1080/07391102.2014.921864openalex-snapshot
Copper(II) directs formation of toxic amorphous aggregates resulting in inhibition of hen egg white lysozyme fibrillation under alkaline salt-mediated conditions
inferred← citeshttps://doi.org/10.1080/19476337.2015.1023359openalex-snapshot
Characterization of protease activities in a crude extract of germinated cacao
inferred← citeshttps://doi.org/10.1093/mtomcs/mfac098openalex-snapshot
Analysis of copper-induced protein precipitation across the E. coli proteome
inferred← citeshttps://doi.org/10.2174/157018081604190220100304openalex-snapshot
Meet Our Associate Editorial Board Member
inferred← citeshttps://doi.org/10.3390/w12113200openalex-snapshot
Molecular Dynamics Simulation of the Interaction between Common Metal Ions and Humic Acids
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Peroxydation des lipides émulsionnés et transfert d'ions fer à l'interface huile / eau stabilisée par des protéines de lait : influence des résidus phosphates et de la stabilité du chélate de fer
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