ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2004
Molecular engineering of myosin.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed, 18 citations in OpenAlex.
- Converter domain mutations in myosin alter structural kinetics and motor function.The Journal of biological chemistry · 2019Article
- Controllable molecular motors engineered from myosin and RNA.Nature nanotechnology · 2018Article
- Detailed tuning of structure and intramolecular communication are dispensable for processive motion of myosin VI.Biophysical journal · 2011Article
- Myosin VI: an innovative motor that challenged the swinging lever arm hypothesis.Nature reviews. Molecular cell biology · 2010Review
- The power stroke of myosin VI and the basis of reverse directionality.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Fifty years on: where have we reached?Journal of muscle research and cell motility · 2006Article
- Introduction.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004Article
- The motor mechanism of myosin V: insights for muscle contraction.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004Review
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 at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein engineering and design provide excellent tools to investigate the principles by which particular structural features relate to the mechanisms that underlie the biological function of a protein. In addition to studies aimed at dissecting the communication pathways within enzymes, recent advances in protein engineering approaches make it possible to generate enzymes with increased catalytic efficiency and specifically altered or newly introduced functions. Here, two approaches using state-of-the-art protein design and engineering are described in detail to demonstrate how key features of the myosin motor can be changed in a specific and predictable manner. First, it is shown how replacement of an actin-binding surface loop with synthetic sequences, whose flexibility and charge density is varied, can be employed to manipulate the actin affinity, the catalytic activity and the efficiency of coupling between actin- and nucleotide-binding sites of myosin motor constructs. Then the use of pre-existing molecular building blocks, which are derived from unrelated proteins, is described for manipulating the velocity and even the direction of movement of recombinant myosins.
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.