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How Chain Length and Charge Affect Surfactant Denaturation of Acyl Coenzyme A Binding Protein (ACBP)
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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/cbic.200300815openalex-snapshot
Membrane Protein–Lipid Interactions in Mixed Micelles Studied by NMR Spectroscopy with the Use of Paramagnetic Reagents
inferredcites →https://doi.org/10.1006/jmbi.1993.1240openalex-snapshot
Three-dimensional Structure of the Complex between Acyl-Coenzyme A Binding Protein and Palmitoyl-Coenzyme A
inferredcites →https://doi.org/10.1006/jmbi.1995.0409openalex-snapshot
Local Perturbations by Ligand Binding of Hydrogen Deuterium Exchange Kinetics in a Four-helix Bundle Protein, Acyl Coenzyme A Binding Protein (ACBP)
inferredcites →https://doi.org/10.1006/jmbi.2001.5300openalex-snapshot
Burst-phase expansion of native protein prior to global unfolding in SDS
inferredcites →https://doi.org/10.1007/978-1-4615-0557-0_7openalex-snapshot
Surfactant-Protein Interactions
inferredcites →https://doi.org/10.1016/0076-6879(86)31045-0openalex-snapshot
[14]Determination and analysis of urea and guanidine hydrochloride denaturation curves
inferredcites →https://doi.org/10.1016/0301-4622(94)00073-5openalex-snapshot
Detergent organisation in solutions and in crystals of membrane proteins
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.bbapap.2007.11.010openalex-snapshot
Aggregation of S6 in a quasi-native state by sub-micellar SDS
inferredcites →https://doi.org/10.1016/j.jmb.2003.10.041openalex-snapshot
Side-chain Contributions to Membrane Protein Structure and Stability
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/s0006-3495(02)73982-9openalex-snapshot
Protein Unfolding in Detergents: Effect of Micelle Structure, Ionic Strength, pH, and Temperature
inferredcites →https://doi.org/10.1016/s0022-2836(03)00624-7openalex-snapshot
Folding of DsbB in Mixed Micelles: A Kinetic Analysis of the Stability of a Bacterial Membrane Protein
inferredcites →https://doi.org/10.1016/s0065-3233(08)60005-4openalex-snapshot
The Interactions of Proteins and Synthetic Detergents
inferredcites →https://doi.org/10.1021/bi00021a037openalex-snapshot
Folding of a four-helix bundle: studies of acyl-coenzyme A binding protein
inferredcites →https://doi.org/10.1021/bi0358622openalex-snapshot
Elimination of a Misfolded Folding Intermediate by a Single Point Mutation
inferredcites →https://doi.org/10.1021/bi0491898openalex-snapshot
Structural Basis of Protein Kinetic Stability: Resistance to Sodium Dodecyl Sulfate Suggests a Central Role for Rigidity and a Bias Toward β-Sheet Structure
inferredcites →https://doi.org/10.1021/bi963095jopenalex-snapshot
A Method for Assessing the Stability of a Membrane Protein
inferredcites →https://doi.org/10.1021/bi982427copenalex-snapshot
Conserved Residues and Their Role in the Structure, Function, and Stability of Acyl-Coenzyme A Binding Protein
inferredcites →https://doi.org/10.1021/bp0501468openalex-snapshot
Surfactant-Induced Unfolding of Cellulase: Kinetic Studies
inferredcites →https://doi.org/10.1021/j100231a029openalex-snapshot
Influence of salt, detergent concentration, and temperature on the fluorescence quenching of 1-methylpyrene in sodium dodecyl sulfate with m-dicyanobenzene
inferredcites →https://doi.org/10.1021/ja00449a004openalex-snapshot
Environmental effects on vibronic band intensities in pyrene monomer fluorescence and their application in studies of micellar systems
inferredcites →https://doi.org/10.1021/ja808776jopenalex-snapshot
Mixing and Matching Detergents for Membrane Protein NMR Structure Determination
inferredcites →https://doi.org/10.1021/la702890yopenalex-snapshot
Global Study of Myoglobin−Surfactant Interactions
inferredcites →https://doi.org/10.1038/9384openalex-snapshot
The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP.
inferredcites →https://doi.org/10.1042/bj2760817openalex-snapshot
Gene synthesis, expression in Escherichia coli, purification and characterization of the recombinant bovine acyl-CoA-binding protein
inferredcites →https://doi.org/10.1073/pnas.0705067104openalex-snapshot
Combined kinetic and thermodynamic analysis of α-helical membrane protein unfolding
inferredcites →https://doi.org/10.1073/pnas.96.20.11008openalex-snapshot
Kinetic stability as a mechanism for protease longevity
inferredcites →https://doi.org/10.1110/ps.052031306openalex-snapshot
Thermodynamics of unfolding of an integral membrane protein in mixed micelles
inferredcites →https://doi.org/10.1529/biophysj.106.101238openalex-snapshot
Unfolding of β-Sheet Proteins in SDS
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Ubiquitin forms conventional decorated micelle structures with sodium dodecyl sulfate at saturation
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Mass Spectrometry—From Peripheral Proteins to Membrane Motors
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inferred← citeshttps://doi.org/10.1021/acsomega.3c07256openalex-snapshot
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inferred← citeshttps://doi.org/10.1021/acsomega.5c01998openalex-snapshot
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Structural Analysis of Protein Denaturation with Alkyl Perfluorinated Sulfonates
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