ArticleJournal of nanoneuroscience2009
Single Molecule Measurements of Interaction Free Energies Between the Proteins Within Binary and Ternary SNARE Complexes.
Article in Journal of nanoneuroscience, 2009. 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.
- Probing single molecule mechanical interactions of syntaxin 1A with native synaptobrevin 2 residing on a secretory vesicle.Cell calcium · 2022Article
- v-SNARE function in chromaffin cells.Pflugers Archiv : European journal of physiology · 2018Review
- Energetics, kinetics, and pathway of SNARE folding and assembly revealed by optical tweezers.Protein science : a publication of the Protein Society · 2017Review
- Different infectivity of HIV-1 strains is linked to number of envelope trimers required for entry.PLoS pathogens · 2015Article
- Common intermediates and kinetics, but different energetics, in the assembly of SNARE proteins.eLife · 2014Article
- Temperature dependence of vesicular dynamics at excitatory synapses of rat hippocampus.Cognitive neurodynamics · 2014Article
- Mechanical unzipping and rezipping of a single SNARE complex reveals hysteresis as a force-generating mechanism.Nature communications · 2013Article
- SNARE requirements en route to exocytosis: from many to few.Journal of molecular neuroscience : MN · 2012Review
- Single reconstituted neuronal SNARE complexes zipper in three distinct stages.Science (New York, N.Y.) · 2012Article
- Single-molecule measurements of dissociation rates and energy landscapes of binary trans snare complexes in parallel versus antiparallel orientation.Biophysical journal · 2011Article
- Munc18-1 tuning of vesicle merger and fusion pore properties.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Docking and fast fusion of synaptobrevin vesicles depends on the lipid compositions of the vesicle and the acceptor SNARE complex-containing target membrane.Biophysical journal · 2010Article
- SNAREs: could they be the answer to an energy landscape riddle in exocytosis?TheScientificWorldJournal · 2010Review
- Single molecule measurements of mechanical interactions within ternary SNARE complexes and dynamics of their disassembly: SNAP25 vs. SNAP23.The Journal of physiology · 2009Article
- Energetics of (Dis)Assembly of the Ternary SNARE Complex.Frontiers in neuroenergetics · 2009Article
- Single molecule probing of SNARE proteins by atomic force microscopy.Annals of the New York Academy of Sciences · 2009Article
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.
Funding
Abstract
We use an Atomic Force Microscope based single molecule measurements to evaluate the activation free energy in the interaction of SNARE proteins syntaxin 1A, SNAP25B and synaptobrevin 2 which regulate intracellular fusion of vesicles with target membranes. The dissociation rate of the binary syntaxin-synaptobrevin and the ternary syntaxin-SNAP25B-synaptobrevin complex was measured from the rupture force distribution as a function of the rate of applied force. The temperature dependence of the spontaneous dissociation rate was used to obtain the activation energy to the transition state of 19.8 +/- 3.5 kcal/mol = 33 +/- 6 k(B)T and 25.7 +/- 3.0 kcal/mol = 43 +/- 5 k(B)T for the binary and ternary complex, respectively. They are consistent with those measured previously for the ternary complex in lipid membranes and are of order expected for bilayer fusion and pore formation. The DeltaG was 12.4-16.6 kcal/mol = 21-28 k(B)T and 13.8-18.0 kcal/mol = 23-30 k(B)T for the binary and ternary complex, respectively. The ternary complex was more stable by 1.4 kcal/mol = 2.3 k(B)T, consistent with the spontaneous dissociation rates. The higher adhesion energies and smaller molecular extensions measured with SNAP25B point to its possible unique and important physiological role in tethering/docking the vesicle in closer proximity to the plasma membrane and increasing the probability for fusion completion.
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.