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

https://doi.org/10.1021/bi300974y
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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/mabi.200900479openalex-snapshot
Self‐Association of Unfolded Outer Membrane Proteins
inferredcites →https://doi.org/10.1006/jmbi.1995.0590openalex-snapshot
An Integrated Kinetic Analysis of Intermediates and Transition States in Protein Folding Reactions
inferredcites →https://doi.org/10.1006/jmbi.2001.5039openalex-snapshot
A simple way to measure protein refolding rates in water
inferredcites →https://doi.org/10.1007/s00018-008-7517-4openalex-snapshot
A conformationally isoformic thermophilic protein with high kinetic unfolding barriers
inferredcites →https://doi.org/10.1016/0022-2836(92)90561-wopenalex-snapshot
The folding of an enzyme
inferredcites →https://doi.org/10.1016/b978-0-12-381268-1.00018-5openalex-snapshot
Using Tryptophan Fluorescence to Measure the Stability of Membrane Proteins Folded in Liposomes
inferredcites →https://doi.org/10.1016/j.abb.2007.09.024openalex-snapshot
The process of folding proteins into membranes: Challenges and progress
inferredcites →https://doi.org/10.1016/j.abb.2008.05.003openalex-snapshot
Assessment of the stability and unfolding pathways of azurin from Pseudomonas aeruginosa through the combination of denaturating osmolytes
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.bpc.2010.03.004openalex-snapshot
In vitro association of fragments of a β-sheet membrane protein
inferredcites →https://doi.org/10.1016/j.chemphyslip.2006.02.004openalex-snapshot
Folding kinetics of the outer membrane proteins OmpA and FomA into phospholipid bilayers
inferredcites →https://doi.org/10.1016/j.jmb.2005.10.060openalex-snapshot
The Major Outer Membrane Protein of Fusobacterium nucleatum (FomA) Folds and Inserts into Lipid Bilayers via Parallel Folding Pathways
inferredcites →https://doi.org/10.1016/j.jmb.2011.08.041openalex-snapshot
Overcoming Hysteresis to Attain Reversible Equilibrium Folding for Outer Membrane Phospholipase A in Phospholipid Bilayers
inferredcites →https://doi.org/10.1016/s0005-2736(01)00410-2openalex-snapshot
Escherichia coli OmpA retains a folded structure in the presence of sodium dodecyl sulfate due to a high kinetic barrier to unfolding
inferredcites →https://doi.org/10.1016/s0021-9258(19)77141-5openalex-snapshot
The Solubility of Amino Acids, Diglycine, and Triglycine in Aqueous Guanidine Hydrochloride Solutions
inferredcites →https://doi.org/10.1016/s0022-2836(02)01071-9openalex-snapshot
Secondary and Tertiary Structure Formation of the β-Barrel Membrane Protein OmpA is Synchronized and Depends on Membrane Thickness
inferredcites →https://doi.org/10.1016/s1359-0278(96)00003-xopenalex-snapshot
On-pathway versus off-pathway folding intermediates
inferredcites →https://doi.org/10.1021/bi00107a010openalex-snapshot
Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
inferredcites →https://doi.org/10.1021/bi00107a011openalex-snapshot
Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding
inferredcites →https://doi.org/10.1021/bi00693a026openalex-snapshot
Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
inferredcites →https://doi.org/10.1021/bi011494vopenalex-snapshot
Unfolding Rates of Barstar Determined in Native and Low Denaturant Conditions Indicate the Presence of Intermediates
inferredcites →https://doi.org/10.1021/bi020316eopenalex-snapshot
Protein Hydration, Thermodynamic Binding, and Preferential Hydration
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/bi061265eopenalex-snapshot
A Minimal Transmembrane β-Barrel Platform Protein Studied by Nuclear Magnetic Resonance,
inferredcites →https://doi.org/10.1021/bi961478bopenalex-snapshot
Folding Intermediates of a β-Barrel Membrane Protein. Kinetic Evidence for a Multi-Step Membrane Insertion Mechanism,
inferredcites →https://doi.org/10.1021/bi963095jopenalex-snapshot
A Method for Assessing the Stability of a Membrane Protein
inferredcites →https://doi.org/10.1021/bi980250gopenalex-snapshot
Folding of Circular and Permuted Chymotrypsin Inhibitor 2: Retention of the Folding Nucleus
inferredcites →https://doi.org/10.1021/bi9824644openalex-snapshot
Time-Resolved Distance Determination by Tryptophan Fluorescence Quenching: Probing Intermediates in Membrane Protein Folding
inferredcites →https://doi.org/10.1021/bi982465wopenalex-snapshot
Outer Membrane Protein A of Escherichia coli Inserts and Folds into Lipid Bilayers by a Concerted Mechanism
inferredcites →https://doi.org/10.1021/jp905553hopenalex-snapshot
How Chain Length and Charge Affect Surfactant Denaturation of Acyl Coenzyme A Binding Protein (ACBP)
inferredcites →https://doi.org/10.1038/346440a0openalex-snapshot
Transient folding intermediates characterized by protein engineering
inferredcites →https://doi.org/10.1038/nsb1297-965openalex-snapshot
Competing unfolding pathways
inferredcites →https://doi.org/10.1073/pnas.0400358101openalex-snapshot
Elastic coupling of integral membrane protein stability to lipid bilayer forces
inferredcites →https://doi.org/10.1073/pnas.0806953106openalex-snapshot
The transition state for integral membrane protein folding
inferredcites →https://doi.org/10.1073/pnas.0911904107openalex-snapshot
The transition state for folding of an outer membrane protein
inferredcites →https://doi.org/10.1073/pnas.1103979108openalex-snapshot
Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers
inferredcites →https://doi.org/10.1073/pnas.89.16.7457openalex-snapshot
Refolding and oriented insertion of a membrane protein into a lipid bilayer.
inferredcites →https://doi.org/10.1073/pnas.96.21.11746openalex-snapshot
Salt-induced detour through compact regions of the protein folding landscape
inferredcites →https://doi.org/10.1074/jbc.270.47.28199openalex-snapshot
Kinetics of Folding and Membrane Insertion of a β-Barrel Membrane Protein
inferredcites →https://doi.org/10.1074/jbc.m802754200openalex-snapshot
β-Barrel Proteins That Reside in the Escherichia coli Outer Membrane in Vivo Demonstrate Varied Folding Behavior in Vitro
inferredcites →https://doi.org/10.1093/protein/gzq079openalex-snapshot
Mapping the folding pathway of the transmembrane protein DsbB by protein engineering
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/j.1365-2958.2003.03903.xopenalex-snapshot
Structure of the OmpA‐like domain of RmpM from Neisseria meningitidis
inferredcites →https://doi.org/10.1111/j.1365-2958.2005.04674.xopenalex-snapshot
Interactions between folding factors and bacterial outer membrane proteins
inferredcites →https://doi.org/10.1146/annurev.bi.60.070191.004051openalex-snapshot
DENATURED STATES OF PROTEINS

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/pro.70214openalex-snapshot
A high‐sensitivity stopped‐flow EPR system to monitor millisecond conformational kinetics in spin‐labeled proteins
inferred← citeshttps://doi.org/10.1007/8623_2016_4openalex-snapshot
Approaches for Preparation and Biophysical Characterization of Transmembrane β-Barrels
inferred← citeshttps://doi.org/10.1007/978-1-0716-5054-7_30openalex-snapshot
Mitochondrial Transmembrane β-Barrels: Deducing Thermodynamic Regulators of Folding and Stability
inferred← citeshttps://doi.org/10.1007/s00232-022-00238-wopenalex-snapshot
The Thermodynamic Stability of Membrane Proteins in Micelles and Lipid Bilayers Investigated with the Ferrichrom Receptor FhuA
inferred← citeshttps://doi.org/10.1007/s00249-013-0887-zopenalex-snapshot
Folding and stability of outer membrane protein A (OmpA) from Escherichia coli in an amphipathic polymer, amphipol A8-35
inferred← citeshttps://doi.org/10.1007/s00253-013-5123-3openalex-snapshot
Structural characteristics of thermostable immunogenic outer membrane protein from Salmonella enterica serovar Typhi
inferred← citeshttps://doi.org/10.1007/s12551-017-0324-0openalex-snapshot
Kinetic stability of membrane proteins
inferred← citeshttps://doi.org/10.1016/j.abb.2012.10.008openalex-snapshot
Folding of outer membrane proteins
inferred← citeshttps://doi.org/10.1016/j.abb.2014.02.011openalex-snapshot
Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: What have we learned to date?
inferred← citeshttps://doi.org/10.1016/j.abb.2014.10.013openalex-snapshot
Folding and stability of integral membrane proteins in amphipols
inferred← citeshttps://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
inferred← citeshttps://doi.org/10.1016/j.bbamem.2017.09.020openalex-snapshot
Transmembrane β-barrels: Evolution, folding and energetics
inferred← citeshttps://doi.org/10.1016/j.bbamem.2019.183097openalex-snapshot
Reversible folding energetics of Yersinia Ail barrel reveals a hyperfluorescent intermediate
inferred← citeshttps://doi.org/10.1016/j.bbamem.2020.183512openalex-snapshot
Breakdown of classical paradigms in relation to membrane structure and functions
inferred← citeshttps://doi.org/10.1016/j.bbapap.2025.141072openalex-snapshot
Role of electrostatics in cold adaptation: A comparative study of eury- and stenopsychrophilic triose phosphate isomerase
inferred← citeshttps://doi.org/10.1016/j.cocis.2015.07.003openalex-snapshot
Proteins in a brave new surfactant world
inferred← citeshttps://doi.org/10.1016/j.febslet.2014.04.004openalex-snapshot
Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid
inferred← citeshttps://doi.org/10.1016/j.febslet.2014.10.017openalex-snapshot
Juxtamembrane tryptophans have distinct roles in defining the OmpX barrel–micelle boundary and facilitating protein–micelle association
inferred← citeshttps://doi.org/10.1016/j.jbc.2023.102899openalex-snapshot
Apo-metallothionein-3 cooperatively forms tightly compact structures under physiological conditions
inferred← citeshttps://doi.org/10.1016/j.molliq.2017.02.099openalex-snapshot
Biophysical insight into the binding of triprolidine hydrochloride to human serum albumin: Calorimetric, spectroscopy and molecular docking approaches
inferred← citeshttps://doi.org/10.1021/acs.biochem.6b01153openalex-snapshot
Concatemers of Outer Membrane Protein A Take Detours in the Folding Landscape
inferred← citeshttps://doi.org/10.1021/acs.biochem.8b00012openalex-snapshot
Folding Determinants of Transmembrane β-Barrels Using Engineered OMP Chimeras
inferred← citeshttps://doi.org/10.1021/jacs.1c05964openalex-snapshot
Engineering a Hyperstable Yersinia pestis Outer Membrane Protein Ail Using Thermodynamic Design
inferred← citeshttps://doi.org/10.1021/la4013747openalex-snapshot
Impact of Urea on Detergent Micelle Properties
inferred← citeshttps://doi.org/10.1038/s41467-021-24432-xopenalex-snapshot
The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding
inferred← citeshttps://doi.org/10.1038/s41557-023-01319-6openalex-snapshot
Protein–lipid charge interactions control the folding of outer membrane proteins into asymmetric membranes
inferred← citeshttps://doi.org/10.1038/srep06508openalex-snapshot
Differential Contribution of Tryptophans to the Folding and Stability of the Attachment Invasion Locus Transmembrane β-Barrel from Yersinia pestis
inferred← citeshttps://doi.org/10.1039/c4ra11207eopenalex-snapshot
Thermodynamic, structural and functional properties of membrane protein inclusion bodies are analogous to purified counterparts: case study from bacteria and humans
inferred← citeshttps://doi.org/10.1039/c5sc00618jopenalex-snapshot
Hydration of guanidinium depends on its local environment
inferred← citeshttps://doi.org/10.1039/d4fd00180jopenalex-snapshot
Protein-induced membrane asymmetry modulates OMP folding kinetics and stability
inferred← citeshttps://doi.org/10.1042/bst20160020openalex-snapshot
A growing toolbox of techniques for studying β-barrel outer membrane protein folding and biogenesis
inferred← citeshttps://doi.org/10.1073/pnas.2514687122openalex-snapshot
A fluorescent reporter and single-turnover kinetics reveal insight into BAM complex function
inferred← citeshttps://doi.org/10.1074/jbc.ra120.013396openalex-snapshot
Quantitating denaturation by formic acid: imperfect repeats are essential to the stability of the functional amyloid protein FapC
inferred← citeshttps://doi.org/10.1074/jbc.rev120.011473openalex-snapshot
Role of the lipid bilayer in outer membrane protein folding in Gram-negative bacteria
inferred← citeshttps://doi.org/10.1101/2023.04.20.537663openalex-snapshot
Protein-lipid charge interactions control the folding of OMPs into asymmetric membranes
inferred← citeshttps://doi.org/10.1186/s12915-017-0464-5openalex-snapshot
Outer membrane protein folding from an energy landscape perspective
inferred← citeshttps://doi.org/10.1371/journal.pone.0079351openalex-snapshot
Methionine Mutations of Outer Membrane Protein X Influence Structural Stability and Beta-Barrel Unfolding
inferred← citeshttps://doi.org/10.1371/journal.pone.0087701openalex-snapshot
Influence of Protein – Micelle Ratios and Cysteine Residues on the Kinetic Stability and Unfolding Rates of Human Mitochondrial VDAC-2
inferred← citeshttps://doi.org/10.1371/journal.pone.0092183openalex-snapshot
Cysteine Residues Impact the Stability and Micelle Interaction Dynamics of the Human Mitochondrial β-Barrel Anion Channel hVDAC-2
inferred← citeshttps://doi.org/10.16943/ptinsa/2015/v81i2/48099openalex-snapshot
Folding and Stability of Transmembrane b-Barrels of Bacterial and Human Origin: Probing Underlying Similarities and Principal Differences Using In vitro Systems
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