ReviewBiochemistry2006
An unfolding story of helical transmembrane proteins.
Review in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed.
- Protein-Membrane Interactions Studied by Transmission and Total Internal Reflection FTIR Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Unfolding Individual Domains of BmrA, a Bacterial ABC Transporter Involved in Multidrug Resistance.International journal of molecular sciences · 2023Article
- Free-energy changes of bacteriorhodopsin point mutants measured by single-molecule force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Thermal melt circular dichroism spectroscopic studies for identifying stabilising amphipathic molecules for the voltage-gated sodium channel NavMs.Biopolymers · 2018Article
- Steric trapping reveals a cooperativity network in the intramembrane protease GlpG.Nature chemical biology · 2016Article
- Reversible Unfolding of Rhomboid Intramembrane Proteases.Biophysical journal · 2016Article
- Targeting acidity in diseased tissues: mechanism and applications of the membrane-inserting peptide, pHLIP.Archives of biochemistry and biophysics · 2015Article
- Unfolding study of a trimeric membrane protein AcrB.Protein science : a publication of the Protein Society · 2014Article
- Lipid directed intrinsic membrane protein segregation.Journal of the American Chemical Society · 2013Article
- Thermodynamic stability of bacteriorhodopsin mutants measured relative to the bacterioopsin unfolded state.Biochimica et biophysica acta · 2012Article
- Interaction of a two-transmembrane-helix peptide with lipid bilayers and dodecyl sulfate micelles.Biophysical chemistry · 2011Article
- Stability, denaturation and refolding of Mycobacterium tuberculosis MfpA, a DNA mimicking protein that confers antibiotic resistance.Biophysical chemistry · 2011Article
- Probing membrane protein unfolding with pulse proteolysis.Journal of molecular biology · 2011Review
- Site-directed mutagenesis combined with oxidative methionine labeling for probing structural transitions of a membrane protein by mass spectrometry.Journal of the American Society for Mass Spectrometry · 2010Article
- Protein folding in membranes.Cellular and molecular life sciences : CMLS · 2010Review
- Thermal and chemical unfolding and refolding of a eukaryotic sodium channel.Biochimica et biophysica acta · 2009Article
- Detergent binding explains anomalous SDS-PAGE migration of membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- The transition state for integral membrane protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Buried water molecules in helical transmembrane proteins.Protein science : a publication of the Protein Society · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
Abstract
Reversible unfolding of helical transmembrane proteins could provide valuable information about the free energy of interaction between transmembrane helices. Thermal unfolding experiments suggest that this process for integral membrane proteins is irreversible. Chemical unfolding has been accomplished with organic acids, but the unfolding or refolding pathways involve irreversible steps. Sodium dodecyl sulfate (SDS) has been used as a perturbant to study reversible unfolding and refolding kinetics. However, the interpretation of these experiments is not straightforward. It is shown that the results could be explained by SDS binding without substantial unfolding. Furthermore, the SDS-perturbed state is unlikely to include all of the entropy terms involved in an unfolding process. Alternative directions for future research are suggested: fluorinated alcohols in homogeneous solvent systems, inverse micelles, and fragment association studies.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.