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Myoglobin and α-Lactalbumin Form Smaller Complexes with the Biosurfactant Rhamnolipid Than with SDS
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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/mrc.1260301019openalex-snapshot
Proton NMR study on rhamnolipids produced by Pseudomonas aeruginosa
inferredcites →https://doi.org/10.1007/bf00180159openalex-snapshot
The aggregation behavior of zinc-free insulin studied by small-angle neutron scattering
inferredcites →https://doi.org/10.1007/s002530051648openalex-snapshot
Potential commercial applications of microbial surfactants
inferredcites →https://doi.org/10.1016/j.bbamem.2016.09.024openalex-snapshot
Biosurfactants and surfactants interacting with membranes and proteins: Same but different?
inferredcites →https://doi.org/10.1016/j.bbapap.2011.03.003openalex-snapshot
Protein–surfactant interactions: A tale of many states
inferredcites →https://doi.org/10.1016/j.bbapap.2014.10.005openalex-snapshot
Denaturation of α-lactalbumin and myoglobin by the anionic biosurfactant rhamnolipid
inferredcites →https://doi.org/10.1016/j.biotechadv.2008.06.002openalex-snapshot
Reversed micelle solvents as tools of enzyme purification and enzyme-catalyzed conversion
inferredcites →https://doi.org/10.1016/j.bpj.2017.03.013openalex-snapshot
Refolding of SDS-Unfolded Proteins by Nonionic Surfactants
inferredcites →https://doi.org/10.1016/j.febslet.2014.04.004openalex-snapshot
Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid
inferredcites →https://doi.org/10.1016/j.foodhyd.2016.07.031openalex-snapshot
α-Lactalbumin and sodium dodecyl sulfate aggregates: Denaturation, complex formation and time stability
inferredcites →https://doi.org/10.1016/j.jbiotec.2012.05.022openalex-snapshot
Rhamnolipids—Next generation surfactants?
inferredcites →https://doi.org/10.1016/j.jcis.2008.09.012openalex-snapshot
A small-angle X-ray scattering study of the structure of lysozyme–sodium dodecyl sulfate complexes
inferredcites →https://doi.org/10.1016/j.jcis.2008.10.021openalex-snapshot
α-Lactalbumin is unfolded by all classes of surfactants but by different mechanisms
inferredcites →https://doi.org/10.1016/j.jmb.2009.06.019openalex-snapshot
The Role of Decorated SDS Micelles in Sub-CMC Protein Denaturation and Association
inferredcites →https://doi.org/10.1016/j.jmb.2010.05.060openalex-snapshot
SDS-Induced Fibrillation of α-Synuclein: An Alternative Fibrillation Pathway
inferredcites →https://doi.org/10.1016/j.physb.2007.05.003openalex-snapshot
Structure of protein–surfactant complexes as studied by small-angle neutron scattering and dynamic light scattering
inferredcites →https://doi.org/10.1016/s0001-8686(97)00312-6openalex-snapshot
Analysis of small-angle scattering data from colloids and polymer solutions: modeling and least-squares fitting
inferredcites →https://doi.org/10.1016/s0021-9797(03)00109-7openalex-snapshot
A systematic study of bovine serum albumin (BSA) and sodium dodecyl sulfate (SDS) interactions by surface tension and small angle X-ray scattering
inferredcites →https://doi.org/10.1016/s1359-0294(02)00044-4openalex-snapshot
Scattering from block copolymer micelles
inferredcites →https://doi.org/10.1021/ac0608826openalex-snapshot
Determination of the Acid Dissociation Constant of the Biosurfactant Monorhamnolipid in Aqueous Solution by Potentiometric and Spectroscopic Methods
inferredcites →https://doi.org/10.1021/acs.biochem.6b01009openalex-snapshot
Human Lysozyme Peptidase Resistance Is Perturbed by the Anionic Glycolipid Biosurfactant Rhamnolipid Produced by the Opportunistic Pathogen Pseudomonas aeruginosa
inferredcites →https://doi.org/10.1021/acs.biochem.7b00420openalex-snapshot
Glycolipid Biosurfactants Activate, Dimerize, and Stabilize Thermomyces lanuginosus Lipase in a pH-Dependent Fashion
inferredcites →https://doi.org/10.1021/j100354a053openalex-snapshot
Sodium alkyl sulfate apparent molar volumes in normal and heavy water: connection with micellar structure
inferredcites →https://doi.org/10.1021/j100617a012openalex-snapshot
Theory of micelle formation in aqueous solutions
inferredcites →https://doi.org/10.1021/la00060a012openalex-snapshot
Theory of surfactant self-assembly: a predictive molecular thermodynamic approach
inferredcites →https://doi.org/10.1021/la1031834openalex-snapshot
Mixing Behavior of the Biosurfactant, Rhamnolipid, with a Conventional Anionic Surfactant, Sodium Dodecyl Benzene Sulfonate
inferredcites →https://doi.org/10.1021/la2020226openalex-snapshot
Self-Assembly of Hydrophobin and Hydrophobin/Surfactant Mixtures in Aqueous Solution
inferredcites →https://doi.org/10.1021/la3028379openalex-snapshot
Numerical Validation of IFT in the Analysis of Protein–Surfactant Complexes with SAXS and SANS
inferredcites →https://doi.org/10.1021/la400432vopenalex-snapshot
Influence of Calcium Ions on Rhamnolipid and Rhamnolipid/Anionic Surfactant Adsorption and Self-Assembly
inferredcites →https://doi.org/10.1021/la803797xopenalex-snapshot
Physicochemical and Conformational Studies on BSA−Surfactant Interaction in Aqueous Medium
inferredcites →https://doi.org/10.1021/ma00139a013openalex-snapshot
Hard-sphere interactions between spherical domains in diblock copolymers
inferredcites →https://doi.org/10.1039/c5sm01231gopenalex-snapshot
Unfolding and folding pathway of lysozyme induced by sodium dodecyl sulfate
inferredcites →https://doi.org/10.1063/1.1665752openalex-snapshot
Small-angle neutron scattering study of structural changes in temperature sensitive microgel colloids
inferredcites →https://doi.org/10.1088/0953-8984/19/32/326102openalex-snapshot
Surfactant-induced protein unfolding as studied by small-angle neutron scattering and dynamic light scattering
inferredcites →https://doi.org/10.1107/s0021889804004170openalex-snapshot
A flux- and background-optimized version of the NanoSTAR small-angle X-ray scattering camera for solution scattering
inferredcites →https://doi.org/10.1107/s0021889808031129openalex-snapshot
Scatterless hybrid metal–single-crystal slit for small-angle X-ray scattering and high-resolution X-ray diffraction
inferredcites →https://doi.org/10.1107/s0021889877013879openalex-snapshot
A new method for the evaluation of small-angle scattering data
inferredcites →https://doi.org/10.1107/s0021889895007047openalex-snapshot
CRYSOL– a Program to Evaluate X-ray Solution Scattering of Biological Macromolecules from Atomic Coordinates
inferredcites →https://doi.org/10.1111/j.1472-765x.2007.02197.xopenalex-snapshot
Potential application of cyclic lipopeptide biosurfactants produced by Bacillus subtilis strains in laundry detergent formulations
inferredcites →https://doi.org/10.3389/fmicb.2015.00292openalex-snapshot
The anionic biosurfactant rhamnolipid does not denature industrial enzymes
inferredcites →https://doi.org/10.3389/fmicb.2016.01711openalex-snapshot
Weak and Saturable Protein–Surfactant Interactions in the Denaturation of Apo-α-Lactalbumin by Acidic and Lactonic Sophorolipid
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.4730416openalex-extracted
Dramatic Increase in Unfolding Rate of Ubiquitin at High Sds Concentrations: A Threshold Value for Sds Penetration?
inferred← citeshttps://doi.org/10.1002/9781119854395.ch10openalex-snapshot
Interaction of Glycolipid Biosurfactants with Model Membranes and Proteins
inferred← citeshttps://doi.org/10.1002/adhm.202302596openalex-snapshot
Biocompatible Rhamnolipid Self‐Assemblies with pH‐Responsive Antimicrobial Activity
inferred← citeshttps://doi.org/10.1007/s10930-023-10095-8openalex-snapshot
Effects of Sodium Dodecyl Sulfate on the Enzyme Catalysis and Conformation of a Recombinant γ-Glutamyltranspeptidase from Bacillus licheniformis
inferred← citeshttps://doi.org/10.1016/b978-0-443-15742-4.00044-2openalex-snapshot
Bio-Based Surfactants and Green Soft Materials
inferred← citeshttps://doi.org/10.1016/b978-0-443-29116-6.00021-7openalex-snapshot
Model Fitting and Simulation Techniques in Small-Angle Scattering Data Analysis
inferred← citeshttps://doi.org/10.1016/j.bbagen.2019.129434openalex-snapshot
Unfolding and partial refolding of a cellulase from the SDS-denatured state: From β-sheet to α-helix and back
inferred← citeshttps://doi.org/10.1016/j.bbapap.2019.140263openalex-snapshot
Bacterial amphiphiles as amyloid inducers: Effect of Rhamnolipid and Lipopolysaccharide on FapC fibrillation
inferred← citeshttps://doi.org/10.1016/j.bbapap.2020.140505openalex-snapshot
Structures and mechanisms of formation of liprotides
inferred← citeshttps://doi.org/10.1016/j.bpj.2018.10.022openalex-snapshot
Can a Charged Surfactant Unfold an Uncharged Protein?
inferred← citeshttps://doi.org/10.1016/j.cis.2022.102754openalex-snapshot
How do surfactants unfold and refold proteins?
inferred← citeshttps://doi.org/10.1016/j.cocis.2023.101766openalex-snapshot
The adsorption and self-assembly of biosurfactants and biosurfactant / surfactant mixtures using neutron scattering techniques
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2025.149069openalex-snapshot
Divergent effects of anionic surfactants on laundry enzymes: Structural stability, activity modulation, and self-cleavage mechanisms
inferred← citeshttps://doi.org/10.1016/j.jbc.2022.101569openalex-snapshot
Induction, inhibition, and incorporation: Different roles for anionic and zwitterionic lysolipids in the fibrillation of the functional amyloid FapC
inferred← citeshttps://doi.org/10.1016/j.jcis.2020.08.027openalex-snapshot
The intriguing role of rhamnolipids on plasma membrane remodelling: From lipid rafts to membrane budding
inferred← citeshttps://doi.org/10.1016/j.jcis.2021.03.110openalex-snapshot
Ubiquitin forms conventional decorated micelle structures with sodium dodecyl sulfate at saturation
inferred← citeshttps://doi.org/10.1016/j.jcis.2021.12.188openalex-snapshot
The changing face of SDS denaturation: Complexes of Thermomyces lanuginosus lipase with SDS at pH 4.0, 6.0 and 8.0
inferred← citeshttps://doi.org/10.1016/j.jcis.2023.08.002openalex-snapshot
The evolution of equilibrium poly(styrene sulfonate) and dodecyl trimethylammonium bromide supramolecular structure in dilute aqueous solution with increasing surfactant binding
inferred← citeshttps://doi.org/10.1016/j.jcis.2024.10.060openalex-snapshot
Investigating the interactions between an industrial lipase and anionic (bio)surfactants
inferred← citeshttps://doi.org/10.1016/j.jcis.2025.137572openalex-snapshot
Balance of hydrophobic and electrostatic interaction of polymers and surfactants: Case of anionic surfactant and hydrophobically modified polymer
inferred← citeshttps://doi.org/10.1016/j.jcis.2026.141662openalex-snapshot
Critical role of electrostatic interactions in protein kinetic stability: Kinetic studies of unfolding ubiquitin using SDS at varying pH values
inferred← citeshttps://doi.org/10.1016/j.jmb.2023.168194openalex-snapshot
Tau Fibrillation Induced by Heparin or a Lysophospholipid Show Different Initial Oligomer Formation
inferred← citeshttps://doi.org/10.1016/j.molliq.2022.120791openalex-snapshot
Lipid nanoparticles with erythrocyte cell-membrane proteins
inferred← citeshttps://doi.org/10.1021/acs.analchem.8b05416openalex-snapshot
Analytical Evaluation of Low-Field 31P NMR Spectroscopy for Lipid Analysis
inferred← citeshttps://doi.org/10.1021/acs.langmuir.2c00172openalex-snapshot
The Amphoteric Surfactant N,N-Dimethyldodecylamine N-Oxide Unfolds β-Lactoglobulin above the Critical Micelle Concentration
inferred← citeshttps://doi.org/10.1021/acs.langmuir.3c00336openalex-snapshot
Self-Assembly of Rhamnolipid Bioamphiphiles: Understanding the Structure–Property Relationship Using Small-Angle X-ray Scattering
inferred← citeshttps://doi.org/10.1021/acs.langmuir.5c05353openalex-snapshot
Influence of Sugar Headgroup on the Self-Assembly of Bioinspired Anionic Glycolipids
inferred← citeshttps://doi.org/10.1021/acsomega.5c08922openalex-snapshot
Effect of the Chemical Structure of Ionic Glycolipids on Their Lyotropic Aqueous Phase Behavior
inferred← citeshttps://doi.org/10.1039/c9nr09135aopenalex-snapshot
Protein unfolding by SDS: the microscopic mechanisms and the properties of the SDS-protein assembly
inferred← citeshttps://doi.org/10.1039/c9sc04831fopenalex-snapshot
A complete picture of protein unfolding and refolding in surfactants
inferred← citeshttps://doi.org/10.1039/d0sc02100hopenalex-snapshot
SDS-induced multi-stage unfolding of a small globular protein through different denatured states revealed by single-molecule fluorescence
inferred← citeshttps://doi.org/10.1039/d1gc00097gopenalex-snapshot
Self-assembly, interfacial properties, interactions with macromolecules and molecular modelling and simulation of microbial bio-based amphiphiles (biosurfactants). A tutorial review
inferred← citeshttps://doi.org/10.1107/s1600576718014462openalex-snapshot
Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument
inferred← citeshttps://doi.org/10.3389/fmolb.2020.00125openalex-snapshot
Multi-Step Unfolding and Rearrangement of α-Lactalbumin by SDS Revealed by Stopped-Flow SAXS
inferred← citeshttps://doi.org/10.3389/frsfm.2022.1081877openalex-snapshot
Recent advances in biosurfactant-based association colloids—Self-assembly in water
inferred← citeshttps://doi.org/10.3390/biom8040126openalex-snapshot
Heme Dissociation from Myoglobin in the Presence of the Zwitterionic Detergent N,N-Dimethyl-N-Dodecylglycine Betaine: Effects of Ionic Liquids
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