ArticleThe Journal of biological chemistry1991
A long helix from the central region of smooth muscle caldesmon.
Article in The Journal of biological chemistry, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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
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Who cites it
34 citing papers in PubMed, 76 citations in OpenAlex.
- Smooth muscle contractile cytoskeleton in health and disease.Journal of muscle research and cell motility · 2026Review
- Remarkable Rigidity of the Single α-Helical Domain of Myosin-VI As Revealed by NMR Spectroscopy.Journal of the American Chemical Society · 2019Article
- Article
- Characterization of long and stable de novo single alpha-helix domains provides novel insight into their stability.Scientific reports · 2017Article
- Distribution and evolution of stable single α-helices (SAH domains) in myosin motor proteins.PloS one · 2017Article
- Functional and Structural Characterization of Novel Type of Linker Connecting Capsid and Nucleocapsid Protein Domains in Murine Leukemia Virus.The Journal of biological chemistry · 2016Article
- Local and macroscopic electrostatic interactions in single α-helices.Nature chemical biology · 2015Article
- Intrinsically disordered caldesmon binds calmodulin via the "buttons on a string" mechanism.PeerJ · 2015Article
- Harnessing the unique structural properties of isolated α-helices.The Journal of biological chemistry · 2014Article
- Myosin VI must dimerize and deploy its unusual lever arm in order to perform its cellular roles.Cell reports · 2014Article
- Smooth muscle caldesmon modulates peristalsis in the wild type and non-innervated zebrafish intestine.Neurogastroenterology and motility · 2012Article
- Helicity of short E-R/K peptides.Protein science : a publication of the Protein Society · 2010Article
- Myosin VI: an innovative motor that challenged the swinging lever arm hypothesis.Nature reviews. Molecular cell biology · 2010Review
- Differential effects of caldesmon on the intermediate conformational states of polymerizing actin.The Journal of biological chemistry · 2010Article
- Combining single-molecule optical trapping and small-angle x-ray scattering measurements to compute the persistence length of a protein ER/K alpha-helix.Biophysical journal · 2009Article
- Myosin VI dimerization triggers an unfolding of a three-helix bundle in order to extend its reach.Molecular cell · 2009Article
- Dynamic charge interactions create surprising rigidity in the ER/K alpha-helical protein motif.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Caldesmon and the regulation of cytoskeletal functions.Advances in experimental medicine and biology · 2008Review
- Interactions between the leucine-zipper motif of cGMP-dependent protein kinase and the C-terminal region of the targeting subunit of myosin light chain phosphatase.Journal of molecular biology · 2007Article
- Caldesmon exhibits a clustered distribution along individual chicken gizzard native thin filaments.Journal of muscle research and cell motility · 2001Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The central region of smooth muscle caldesmon is predicted to form alpha-helices on the basis of its primary structure. We have isolated a fragment (CT54) that contains this region. The hydrodynamic properties and the electron microscopic images suggest that CT54 is an elongated (35 nm), monomeric molecule. The circular dichroic spectrum yields an overall alpha-helical content of 55-58%. These results are consistent with the model that the middle portion of CT54 forms a long stretch of single-stranded alpha-helix. Such a structure, if it in fact exists, is thought to be stabilized by numerous salt bridges between charged residues at positions i and i + 4. The structural characteristics of this fragment not only represent an unusual protein configuration but also provide information about the functional role of caldesmon in smooth muscle contraction.
Indexed as
Identifiers
1856225PMC1262681W2110973514What 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.