ArticleBiophysical journal1999
Localization and environment of tryptophans in soluble and membrane-bound states of a pore-forming toxin from Staphylococcus aureus.
Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 65 citations in OpenAlex.
- The Study of Cell-Penetrating Peptides to Deliver dsRNA and siRNA by Feeding in the Desert Locust,Insects · 2023Article
- Estimation of a stronger heparin binding locus in fibronectin domain IIIRSC advances · 2020Article
- GFP fluorescence: A few lesser-known nuggets that make it work.Journal of biosciences · 2018Article
- Organization and dynamics of tryptophan residues in brain spectrin: novel insight into conformational flexibility.Journal of fluorescence · 2015Article
- A C-terminal membrane anchor affects the interactions of prion proteins with lipid membranes.The Journal of biological chemistry · 2014Article
- Nanosecond Dynamics of InfluenzaA/M2TM and an Amantadine Resistant Mutant Probed by Time-Dependent Red Shifts of a Native Tryptophan.Chemical physics · 2013Article
- Hydramacin-1 in action: scrutinizing the barnacle model.Antimicrobial agents and chemotherapy · 2013Article
- Exploring tryptophan dynamics in acid-induced molten globule state of bovine alpha-lactalbumin: a wavelength-selective fluorescence approach.European biophysics journal : EBJ · 2010Article
- Fluorescence quenching as a tool to investigate quinolone antibiotic interactions with bacterial protein OmpF.The Journal of membrane biology · 2009Article
- Positioning of proteins in membranes: a computational approach.Protein science : a publication of the Protein Society · 2006Article
- Role of tryptophan residues in toxicity of Cry1Ab toxin from Bacillus thuringiensis.Applied and environmental microbiology · 2006Article
- A two-dimensional infrared study of localization, structure, and dynamics of a dipeptide in membrane environment.Biophysical journal · 2004Article
- Monitoring gramicidin conformations in membranes: a fluorescence approach.Biophysical journal · 2004Article
- Chemical and photochemical modification of colicin E1 and gramicidin A in bilayer lipid membranes.The Journal of membrane biology · 2004Article
- Organization and dynamics of tryptophan residues in erythroid spectrin: novel structural features of denatured spectrin revealed by the wavelength-selective fluorescence approach.Protein science : a publication of the Protein Society · 2003Article
- Differential interaction of equinatoxin II with model membranes in response to lipid composition.Biophysical journal · 2001Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The location and environment of tryptophans in the soluble and membrane-bound forms of Staphylococcus aureus alpha-toxin were monitored using intrinsic tryptophan fluorescence. Fluorescence quenching of the toxin monomer in solution indicated varying degrees of tryptophan burial within the protein interior. N-Bromosuccinimide readily abolished 80% of the fluorescence in solution. The residual fluorescence of the modified toxin showed a blue-shifted emission maximum, a longer fluorescence lifetime as compared to the unmodified and membrane-bound alpha-toxin, and a 5- to 6-nm red edge excitation shift, all indicating a restricted tryptophan environment and deeply buried tryptophans. In the membrane-bound form, the fluorescence of alpha-toxin was quenched by iodide, indicating a conformational change leading to exposure of some tryptophans. A shorter average lifetime of tryptophans in the membrane-bound alpha-toxin as compared to the native toxin supported the conclusions based on iodide quenching of the membrane-bound toxin. Fluorescence quenching of membrane-bound alpha-toxin using brominated and spin-labeled fatty acids showed no quenching of fluorescence using brominated lipids. However, significant quenching was observed using 5- and 12-doxyl stearic acids. An average depth calculation using the parallax method indicated that the doxyl-quenchable tryptophans are located at an average depth of 10 A from the center of the bilayer close to the membrane interface. This was found to be in striking agreement with the recently described structure of the membrane-bound form of alpha-toxin.
Indexed as
Identifiers
What OpenQuestion holds
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.