ArticleJournal of muscle research and cell motility1998
Amino-acid sequence of squid myosin heavy chain.
Article in Journal of muscle research and cell motility, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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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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Who cites it
9 citing papers in PubMed, 24 citations in OpenAlex.
- Tuning of shortening speed in coleoid cephalopod muscle: no evidence for tissue-specific muscle myosin heavy chain isoforms.Invertebrate biology : a quarterly journal of the American Microscopical Society and the Division of Invertebrate Zoology/ASZ · 2016Article
- The Musculature of Coleoid Cephalopod Arms and Tentacles.Frontiers in cell and developmental biology · 2016Review
- The making of an octopus arm.EvoDevo · 2015Article
- Purification, crystallization and preliminary X-ray crystallographic analysis of squid heavy meromyosin.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Muscular tissues of the squid Doryteuthis pealeii express identical myosin heavy chain isoforms: an alternative mechanism for tuning contractile speed.The Journal of experimental biology · 2012Article
- Association of a nonmuscle myosin II with axoplasmic organelles.Molecular biology of the cell · 2002Article
- Microsequencing of myosins for PCR primer design.Methods in molecular biology (Clifton, N.J.) · 2001Review
- Primary structure of myosin from the striated adductor muscle of the Atlantic scallop, Pecten maximus, and expression of the regulatory domain.Journal of muscle research and cell motility · 2000Article
- Primary peptide sequences from squid muscle and optic lobe myosin IIs: a strategy to identify an organelle myosin.Cell biology international · 1998Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
This work describes the determination of the cDNA sequence encoding the myosin heavy chain (MHC) of the squid, Loligo pealei. To date, the amino-acid sequence of the MHC of calcium-regulated myosins is known only for two closely related species of scallops. We have determined the sequence of the entire coding region of the muscle MHC of squid, a cephalopod, and compared it with the MHC of scallops, which are pelecypods, and to other regulated and non-regulated myosins. Residues present in the MHC of only regulated myosins have been identified. The 6504 base pair (bp) sequence contains an open reading frame of 5805 nucleotides, which encodes 1935 amino acids. The sequence includes 697 bps of 3' untranslated sequence and 2 bps of 5' untranslated sequence. The deduced amino-acid sequence shows the squid MHC to be 72-73% identical and 86-87% similar to the calcium-regulated scallop MHCs cloned previously. In contrast, the squid MHC sequence is only 54-55% identical and 74% similar to skeletal MHCs of non-regulated myosins such as human fast skeletal embryonic and human perinatal skeletal muscle, and 39-40% identical and 60-62% similar to smooth muscle MHC of rabbit uterus muscle and chicken gizzard muscle, respectively. We have also detected two isoforms of the MHC in squid that appear to be spliced variants of a single myosin gene. These isoforms differ in the sequence encoding the surface loop at the nucleotide binding site. Taken together, our data may help to identify more precisely the residues that are crucial in regulated myosins.
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