ArticleLangmuir : the ACS journal of surfaces and colloids2011
Long-term storage of surface-adsorbed protein machines.
Article in Langmuir : the ACS journal of surfaces and colloids, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
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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.
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Who cites it
6 citing papers in PubMed, 18 citations in OpenAlex.
- Improved longevity of actomyosin in vitro motility assays for sustainable lab-on-a-chip applications.Scientific reports · 2024Article
- An automated in vitro motility assay for high-throughput studies of molecular motors.Lab on a chip · 2018Article
- Magnetic capture from blood rescues molecular motor function in diagnostic nanodevices.Journal of nanobiotechnology · 2013Article
- Article
- Translational actomyosin research: fundamental insights and applications hand in hand.Journal of muscle research and cell motility · 2012Review
- Antibodies covalently immobilized on actin filaments for fast myosin driven analyte transport.PloS one · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The effective and simple long-term storage of complex functional proteins is critical in achieving commercially viable biosensors. This issue is particularly challenging in recently proposed types of nanobiosensors, where molecular-motor-driven transportation substitutes microfluidics and forms the basis for novel detection schemes. Importantly, therefore, we here describe that delicate heavy meromyosin (HMM)-based nanodevices (HMM motor fragments adsorbed to silanized surfaces and actin bound to HMM) fully maintain their function when stored at -20 °C for more than a month. The mechanisms for the excellent preservation of acto-HMM motor function upon repeated freeze-thaw cycles are discussed. The results are important to the future commercial implementation of motor-based nanodevices and are of more general value to the long-term storage of any protein-based bionanodevice.
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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.