ArticleProceedings of the National Academy of Sciences of the United States of America1997
Kinetic characterization of brush border myosin-I ATPase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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.
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.
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Who cites it
27 citing papers in PubMed, 67 citations in OpenAlex.
- Pathophysiology of human hearing loss associated with variants in myosins.Frontiers in physiology · 2024Review
- The dynamics of actin protrusions can be controlled by tip-localized myosin motors.The Journal of biological chemistry · 2024Article
- High-resolution cryo-EM structures of actin-bound myosin states reveal the mechanism of myosin force sensing.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Shaping the intestinal brush border.The Journal of cell biology · 2014Review
- Molecular characterization and subcellular localization of Arabidopsis class VIII myosin, ATM1.The Journal of biological chemistry · 2014Article
- Motor and tail homology 1 (Th1) domains antagonistically control myosin-1 dynamics.Biophysical journal · 2014Article
- Regulation and control of myosin-I by the motor and light chain-binding domains.Trends in cell biology · 2013Review
- Myosin IC generates power over a range of loads via a new tension-sensing mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Myosin Ia is required for CFTR brush border membrane trafficking and ion transport in the mouse small intestine.Traffic (Copenhagen, Denmark) · 2012Article
- Shaking the myosin family tree: biochemical kinetics defines four types of myosin motor.Seminars in cell & developmental biology · 2011Review
- Loop 1 dynamics in smooth muscle myosin: isoform specific differences modulate ADP release.Journal of muscle research and cell motility · 2011Article
- A hearing loss-associated myo1c mutation (R156W) decreases the myosin duty ratio and force sensitivity.Biochemistry · 2011Article
- Leveraging the membrane - cytoskeleton interface with myosin-1.Trends in cell biology · 2010Review
- Myosin-1a: A motor for microvillar membrane movement and mechanics.Communicative & integrative biology · 2010Article
- Myosin-1a powers the sliding of apical membrane along microvillar actin bundles.The Journal of cell biology · 2007Article
- Temperature dependence of nucleotide association and kinetic characterization of myo1b.Biochemistry · 2006Article
- Dimerized Drosophila myosin VIIa: a processive motor.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Myosin-1a is critical for normal brush border structure and composition.Molecular biology of the cell · 2005Article
- A role for myosin-1A in the localization of a brush border disaccharidase.The Journal of cell biology · 2004Article
- MYO1A (brush border myosin I) dynamics in the brush border of LLC-PK1-CL4 cells.Biophysical journal · 2002Article
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 3 institutions in 1 country.
Funding
Abstract
Brush border myosin-I (BBM-I) is a single-headed unconventional myosin found in the microvilli of intestinal epithelial cells. We used stopped-flow kinetic analysis to measure the rate and equilibrium constants for several steps in the BBM-I ATPase cycle. We determined the rates for ATP binding to BBM-I and brush border actomyosin-I (actoBBM-I), the rate of actoBBM-I dissociation by ATP, and the rates for the steps in ADP dissociation from actoBBM-I. The rate and equilibrium constants for several of the steps in the actoBBM-I ATPase are significantly different from those of other members of the myosin superfamily. Most notably, dissociation of the actoBBM-I complex by ATP and release of ADP from actoBBM-I are both very slow. The slow rates of these steps may play a role in lengthening the time spent in force-generating states and in limiting the maximal rate of BBM-I motility. In addition, release of ADP from the actoBBM-I complex occurs in at least two steps. This study provides evidence for a member of the myosin superfamily with markedly divergent kinetic behavior.
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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.