ArticleThe Biochemical journal1986
67 kDa calcimedin, a new Ca2+-binding protein.
Article in The Biochemical journal, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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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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
7 citing papers in PubMed, 41 citations in OpenAlex.
- Evaluation of the annexins as potential mediators of membrane fusion in exocytosis.Journal of bioenergetics and biomembranes · 1990Review
- An immunological and biochemical comparison of 67 kDa calcimedin and 67 kDa calelectrin.The Biochemical journal · 1989Article
- Purification and spectral studies on the Ca2+-binding properties of 67 kDa calcimedin.The Biochemical journal · 1989Article
- Expression of 67,000 MW calcimedin and its binding protein in resident and thioglycolate-elicited macrophages.Immunology · 1988Article
- 67 k calcimedin (67 kDa) is distinct from p67 calelectrin and lymphocyte 68 kDa Ca2+-binding protein.The Biochemical journal · 1988Article
- Human 67-kDa calelectrin contains a duplication of four repeats found in 35-kDa lipocortins.Proceedings of the National Academy of Sciences of the United States of America · 1988Article
- The synaptic vesicle and the cytoskeleton.The Biochemical journal · 1987Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
A set of four proteins, termed calcimedins, are isolatable from smooth, cardiac and skeletal muscle by using a fluphenazine-Sepharose affinity column. The calcimedins show apparent Mr values of 67,000, 35,000, 33,000 and 30,000 by SDS/polyacrylamide-gel electrophoresis. The 67,000-Mr calcimedin (67 kDa calcimedin) has now been purified to homogeneity by using DEAE-cellulose chromatography followed by Ca2+-dependent binding to phenyl-Sepharose. The amino acid analysis of the 67 kDa calcimedin shows this protein does not contain trimethyl-lysine but does contain 2 mol of tryptophan/mol of protein. The 67 kDa calcimedin shows positive ellipticity in the near-u.v. range with c.d. Ca2+-binding studies indicate one high-affinity Ca2+-binding site with Kd 0.4 microM. The data show that the 67 kDa calcimedin is distinct from other Ca2+-binding proteins described to date.
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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.