ArticleCroatica chemica acta. Arhiv za kemiju2008
Single Molecule Probing of Exocytotic Protein Interactions Using Force Spectroscopy.
Article in Croatica chemica acta. Arhiv za kemiju, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The trial behind it
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Probing single molecule mechanical interactions of syntaxin 1A with native synaptobrevin 2 residing on a secretory vesicle.Cell calcium · 2022Article
- Binding kinetics of liposome conjugated E-selectin and P-selectin glycoprotein ligand-1 measured with atomic force microscopy.Colloids and surfaces. B, Biointerfaces · 2021Article
- Anisotropy in mechanical unfolding of protein upon partner-assisted pulling and handle-assisted pulling.Communications biology · 2021Article
- SNARE-mediated membrane fusion trajectories derived from force-clamp experiments.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- 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
- 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
- Single molecule probing of SNARE proteins by atomic force microscopy.Annals of the New York Academy of Sciences · 2009Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Relatively recently, the Atomic Force Microscope (AFM) emerged as a powerful tool for single molecule nanomechanical investigations. Parameters that can be measured by force spectroscopy using AFM, such as the force and total mechanical extension required to break bonds between various proteins can yield valuable insights into the nature of the bond (zippering vs. highly localized binding site), the sequence of its interactions and the energy landscape along the length of the interaction. In this review we discuss the use of AFM in force spectroscopy mode to study intermolecular interactions between the exocytotic proteins of the core SNARE complex. Information gathered by force spectroscopy of protein-protein interactions of this complex supplement previous results acquired with other techniques, and allows a deeper understanding of SNARE protein interactions and their role in exocytosis.
Identifiers
20151046PMC2819743W2096066850What 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.