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Proteins in a brave new surfactant world

https://doi.org/10.1016/j.cocis.2015.07.003

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What this work says

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

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A Fluorinated Detergent for Membrane‐Protein Applications

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Low‐Resolution Structures of OmpA⋅DDM Protein–Detergent Complexes

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Generic Structures of Cytotoxic Liprotides: Nano‐Sized Complexes with Oleic Acid Cores and Shells of Disordered Proteins

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Identifying kinetically stable proteins with capillary electrophoresis

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Revisiting the folding kinetics of bacteriorhodopsin

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Molecular Engineering Aspects for the Production of New and Modified Biosurfactants

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Folding and stability of outer membrane protein A (OmpA) from Escherichia coli in an amphipathic polymer, amphipol A8-35

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Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels

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The relative effectiveness of guanidinium and some biguanide slats as denaturants Assessment against penicillinase

inferredcites →https://doi.org/10.1016/j.abb.2014.10.013openalex-snapshot

Folding and stability of integral membrane proteins in amphipols

inferredcites →https://doi.org/10.1016/j.bbamem.2005.08.006openalex-snapshot

Using micellar mole fractions to assess membrane protein stability in mixed micelles

inferredcites →https://doi.org/10.1016/j.bbamem.2015.05.004openalex-snapshot

Folding of β -barrel membrane proteins in lipid bilayers — Unassisted and assisted folding and insertion

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.febslet.2014.04.004openalex-snapshot

Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid

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.jfluchem.2008.10.007openalex-snapshot

Study on the Langmuir aggregation of fluorinated surfactants on protein

inferredcites →https://doi.org/10.1016/j.jmb.2007.11.026openalex-snapshot

Refolding SDS-Denatured Proteins by the Addition of Amphipathic Cosolvents

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.2010.03.012openalex-snapshot

The Interaction of Equine Lysozyme:Oleic Acid Complexes with Lipid Membranes Suggests a Cargo Off-Loading Mechanism

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SDS-Induced Fibrillation of α-Synuclein: An Alternative Fibrillation Pathway

inferredcites →https://doi.org/10.1016/j.jmb.2011.12.037openalex-snapshot

Thermodynamic Measurements of Bilayer Insertion of a Single Transmembrane Helix Chaperoned by Fluorinated Surfactants

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Hemifluorinated surfactants: a non‐dissociating environment for handling membrane proteins in aqueous solutions?

inferredcites →https://doi.org/10.1016/s0021-9258(17)30602-6openalex-snapshot

Refolding of an integral membrane protein. OmpA of Escherichia coli.

inferredcites →https://doi.org/10.1016/s0021-9258(18)62831-5openalex-snapshot

The Gross Conformation of Protein-Sodium Dodecyl Sulfate Complexes

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Effect of the nature of the counterion on the interaction between cesium and tetraalkylammonium dodecylsulfates and poly(ethylene oxide) or poly(vinylpyrolidone)

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The Use of Liprotides To Stabilize and Transport Hydrophobic Molecules

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Crystallographic studies of protein denaturation and renaturation. 2. Sodium dodecyl sulfate induced structural changes in triclinic lysozyme

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Quantifying the Kinetic Stability of Hyperstable Proteins via Time-Dependent SDS Trapping

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A Kinetic Analysis of the Folding and Unfolding of OmpA in Urea and Guanidinium Chloride: Single and Parallel Pathways

inferredcites →https://doi.org/10.1021/bi301258eopenalex-snapshot

pH Regulation of the Kinetic Stability of the Lipase fromThermomyces lanuginosus

inferredcites →https://doi.org/10.1021/bi400643sopenalex-snapshot

Structural Characterization of More Potent Alternatives to HAMLET, a Tumoricidal Complex of α-Lactalbumin and Oleic Acid

inferredcites →https://doi.org/10.1021/bi7007596openalex-snapshot

Dynamics of Membrane Protein/Amphipol Association Studied by Förster Resonance Energy Transfer: Implications for in Vitro Studies of Amphipol-Stabilized Membrane Proteins

inferredcites →https://doi.org/10.1021/bi963095jopenalex-snapshot

A Method for Assessing the Stability of a Membrane Protein

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The Anomalous Behavior of Fluorocarbon Solutions

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Complexes of Native Ubiquitin and Dodecyl Sulfate Illustrate the Nature of Hydrophobic and Electrostatic Interactions in the Binding of Proteins and Surfactants

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Modeling Detergent Organization around Aquaporin-0 Using Small-Angle X-ray Scattering

inferredcites →https://doi.org/10.1021/ja3079863openalex-snapshot

Effect of Surfactant Hydrophobicity on the Pathway for Unfolding of Ubiquitin

inferredcites →https://doi.org/10.1021/ja508359nopenalex-snapshot

Bacteriorhodopsin Folds through a Poorly Organized Transition State

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Dodine as a Protein Denaturant: The Best of Two Worlds?

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How Chain Length and Charge Affect Surfactant Denaturation of Acyl Coenzyme A Binding Protein (ACBP)

inferredcites →https://doi.org/10.1021/la103495kopenalex-snapshot

Structural Analysis of Protein Complexes with Sodium Alkyl Sulfates by Small-Angle Scattering and Polyacrylamide Gel Electrophoresis

inferredcites →https://doi.org/10.1021/la201832dopenalex-snapshot

Denaturation of Proteins by SDS and Tetraalkylammonium Dodecyl Sulfates

inferredcites →https://doi.org/10.1021/la203879topenalex-snapshot

Interaction of a Rhodococcus sp. Trehalose Lipid Biosurfactant with Model Proteins: Thermodynamic and Structural Changes

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Numerical Validation of IFT in the Analysis of Protein–Surfactant Complexes with SAXS and SANS

inferredcites →https://doi.org/10.1021/la303944topenalex-snapshot

Structural Analysis of Protein Denaturation with Alkyl Perfluorinated Sulfonates

inferredcites →https://doi.org/10.1021/la4013747openalex-snapshot

Impact of Urea on Detergent Micelle Properties

inferredcites →https://doi.org/10.1021/la404392topenalex-snapshot

Anionic Branched Surfactants as Alternative Denaturing Agents for Protein Separations

inferredcites →https://doi.org/10.1021/la800636sopenalex-snapshot

Thermodynamic and Structural Changes Associated with the Interaction of a Dirhamnolipid Biosurfactant with Bovine Serum Albumin

inferredcites →https://doi.org/10.1021/la9018772openalex-snapshot

Thermodynamic Characterization of the Exchange of Detergents and Amphipols at the Surfaces of Integral Membrane Proteins

inferredcites →https://doi.org/10.1038/nature06977openalex-snapshot

Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins

inferredcites →https://doi.org/10.1073/pnas.0705417104openalex-snapshot

Identifying the subproteome of kinetically stable proteins via diagonal 2D SDS/PAGE

inferredcites →https://doi.org/10.1073/pnas.1012594108openalex-snapshot

Stable folding core in the folding transition state of an α-helical integral membrane protein

inferredcites →https://doi.org/10.1073/pnas.1424751112openalex-snapshot

Cooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus and nonnative loops

inferredcites →https://doi.org/10.1073/pnas.97.8.4221openalex-snapshot

Conversion of α-lactalbumin to a protein inducing apoptosis

inferredcites →https://doi.org/10.1110/ps.0231103openalex-snapshot

Lipids as cofactors in protein folding: Stereo‐specific lipid–protein interactions are required to form HAMLET (human α‐lactalbumin made lethal to tumor cells)

inferredcites →https://doi.org/10.1110/ps.035154.108openalex-snapshot

Lysine acetylation can generate highly charged enzymes with increased resistance toward irreversible inactivation

inferredcites →https://doi.org/10.1110/ps.8.10.2065openalex-snapshot

Outer membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent

inferredcites →https://doi.org/10.1111/febs.12772openalex-snapshot

Weak protein–ligand interactions studied by small‐angle X ‐ray scattering

inferredcites →https://doi.org/10.1146/annurev-biophys-042910-155219openalex-snapshot

Amphipols From A to Z

inferredcites →https://doi.org/10.1201/9780367803094openalex-snapshot

Surface Activity of Proteins

inferredcites →https://doi.org/10.1201/9781439822548.ch8openalex-snapshot

Protein-Surfactant Interactions

inferredcites →https://doi.org/10.1529/biophysj.106.101238openalex-snapshot

Unfolding of β-Sheet Proteins in SDS

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Amyloid Formation in Surfactants and Alcohols: Membrane Mimetics or Structural Switchers?

inferredcites →https://doi.org/10.3389/fmicb.2015.00292openalex-snapshot

The anionic biosurfactant rhamnolipid does not denature industrial enzymes

What points at this work

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

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Étude structurale et fonctionnelle de l'appareil de recombinaison homologue chez Streptococcus pneumoniae

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