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We are analyzing https://link.springer.com/article/10.1007/bf00260706.

Title:
TheSaccharomyces cerevisiae genes (CMP1 andCMP2) encoding calmodulin-binding proteins homologous to the catalytic subunit of mammalian protein phosphatase 2B | Molecular Genetics and Genomics
Description:
Saccharomyces cerevisiae genomic clones that encode calmodulin-binding proteins were isolated by screening a λgt11 expression library using125I-labeled calmodulin as probe. Among the cloned yeast genes, we found two closely related genes (CMP1 andCMP2) that encode proteins homologous to the catalytic subunit of phosphoprotein phosphatase. The presumed CMP1 protein (62999 Da) and CMP2 protein (68496 Da) contain a 23 amino acid sequence very similar to those identified as calmodulin-binding sites in many calmodulin-regulated proteins. The yeast genes encode proteins especially homologous to the catalytic subunit of mammalian phosphoprotein phosphatase type 213 (calcineurin). The products of theCMP1 andCMP2 genes were identified by immunoblot analysis of cell extracts as proteins of 62000 and 64000 Da, respectively. Gene disruption experiments demonstrated that elimination of either or both of these genes had no effect on cell viability, indicating that these genes are not essential for normal cell growth.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Science
  • Education
  • Telecommunications

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month


Based on our best estimate, this website will receive around 7,626,432 visitors per month in the current month.

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How Does Link.springer.com Make Money? {💸}

We find it hard to spot revenue streams.

Websites don't always need to be profitable; some serve as platforms for education or personal expression. Websites can serve multiple purposes. And this might be one of them. Link.springer.com might be plotting its profit, but the way they're doing it isn't detectable yet.

Keywords {🔍}

google, scholar, article, pubmed, cas, protein, proteins, cerevisiae, phosphatase, calmodulin, genes, yeast, calmodulinbinding, cell, gene, usa, molecular, cmp, catalytic, subunit, tanaka, fukui, saccharomyces, calcineurin, proc, natl, acad, sci, privacy, cookies, content, homologous, tsuchiya, miyakawa, access, cohen, analysis, information, publish, search, andcmp, liu, encode, sequence, calcium, cloning, klee, isolation, biophys, laboratory,

Topics {✒️}

ca2+-dependent/calmodulin-stimu-lated protein phosphatase month download article/chapter brain calmodulin-binding protein calmodulin-dependent protein phosphatase encode calmodulin-binding proteins specific calmodulin-dependent enzymes type-2a protein phosphatase thesaccharomyces cerevisiae genes mating pheromone α-factor saccharomyces cerevisiae calmodulin-regulated proteins encode proteins homologous calmodulin-binding protein closely related genes cold spring harbor full article pdf calmodulin-binding sites ca2+ atpase family privacy choices/manage cookies related subjects yeast secretory pathway cloned yeast genes calmodulin affinity chromatography calmodulin inschizosaccharomyces pombe presumed cmp1 protein thecmp1 andcmp2 genes cmp2 protein phosphatases yeast calmodulin gene article liu normal cell growth protein phosphatase 1 step gene disruption european economic area deduced primary structure cdna clone encoding polyproline structural domain complete primary structure yeast operator overlaps chain-terminating inhibitors conditions privacy policy glucoamylase-producing gene 2b type intron-contained sequence accepting optional cookies rinji akada upstream activation site cyclic amp article molecular main content log phosphoprotein phosphatase

Schema {🗺️}

WebPage:
      mainEntity:
         headline:TheSaccharomyces cerevisiae genes (CMP1 andCMP2) encoding calmodulin-binding proteins homologous to the catalytic subunit of mammalian protein phosphatase 2B
         description: Saccharomyces cerevisiae genomic clones that encode calmodulin-binding proteins were isolated by screening a λgt11 expression library using125I-labeled calmodulin as probe. Among the cloned yeast genes, we found two closely related genes (CMP1 andCMP2) that encode proteins homologous to the catalytic subunit of phosphoprotein phosphatase. The presumed CMP1 protein (62999 Da) and CMP2 protein (68496 Da) contain a 23 amino acid sequence very similar to those identified as calmodulin-binding sites in many calmodulin-regulated proteins. The yeast genes encode proteins especially homologous to the catalytic subunit of mammalian phosphoprotein phosphatase type 213 (calcineurin). The products of theCMP1 andCMP2 genes were identified by immunoblot analysis of cell extracts as proteins of 62000 and 64000 Da, respectively. Gene disruption experiments demonstrated that elimination of either or both of these genes had no effect on cell viability, indicating that these genes are not essential for normal cell growth.
         datePublished:
         dateModified:
         pageStart:52
         pageEnd:59
         sameAs:https://doi.org/10.1007/BF00260706
         keywords:
             Saccharomyces cerevisiae
            Calmodulin-binding protein
            Protein phosphatase (2B type)
            Calcineurin A
            Plant Genetics and Genomics
            Human Genetics
            Microbial Genetics and Genomics
            Animal Genetics and Genomics
            Biochemistry
            general
         image:
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               0026-8925
            volumeNumber:227
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               Periodical
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      headline:TheSaccharomyces cerevisiae genes (CMP1 andCMP2) encoding calmodulin-binding proteins homologous to the catalytic subunit of mammalian protein phosphatase 2B
      description: Saccharomyces cerevisiae genomic clones that encode calmodulin-binding proteins were isolated by screening a λgt11 expression library using125I-labeled calmodulin as probe. Among the cloned yeast genes, we found two closely related genes (CMP1 andCMP2) that encode proteins homologous to the catalytic subunit of phosphoprotein phosphatase. The presumed CMP1 protein (62999 Da) and CMP2 protein (68496 Da) contain a 23 amino acid sequence very similar to those identified as calmodulin-binding sites in many calmodulin-regulated proteins. The yeast genes encode proteins especially homologous to the catalytic subunit of mammalian phosphoprotein phosphatase type 213 (calcineurin). The products of theCMP1 andCMP2 genes were identified by immunoblot analysis of cell extracts as proteins of 62000 and 64000 Da, respectively. Gene disruption experiments demonstrated that elimination of either or both of these genes had no effect on cell viability, indicating that these genes are not essential for normal cell growth.
      datePublished:
      dateModified:
      pageStart:52
      pageEnd:59
      sameAs:https://doi.org/10.1007/BF00260706
      keywords:
          Saccharomyces cerevisiae
         Calmodulin-binding protein
         Protein phosphatase (2B type)
         Calcineurin A
         Plant Genetics and Genomics
         Human Genetics
         Microbial Genetics and Genomics
         Animal Genetics and Genomics
         Biochemistry
         general
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            name:Yusen Liu
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                     type:PostalAddress
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            name:Satoru Ishii
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                  name:Faculty of Engineering
                  address:
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               type:PostalAddress
            type:Organization
      name:Kazuma Tanaka
      affiliation:
            name:Faculty of Engineering
            address:
               name:Department of Fermentation Technology, Faculty of Engineering, Higashi-Hiroshima, Japan
               type:PostalAddress
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      name:Eiko Tsuchiya
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            address:
               name:Department of Fermentation Technology, Faculty of Engineering, Higashi-Hiroshima, Japan
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            address:
               name:Department of Fermentation Technology, Faculty of Engineering, Higashi-Hiroshima, Japan
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               name:Department of Fermentation Technology, Faculty of Engineering, Higashi-Hiroshima, Japan
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      name:Department of Fermentation Technology, Faculty of Engineering, Higashi-Hiroshima, Japan
      name:Department of Fermentation Technology, Faculty of Engineering, Higashi-Hiroshima, Japan
      name:Center for Gene Science, Hiroshima University, Higashi-Hiroshima, Japan
      name:Department of Fermentation Technology, Faculty of Engineering, Higashi-Hiroshima, Japan
      name:Department of Fermentation Technology, Faculty of Engineering, Higashi-Hiroshima, Japan
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      name:Department of Fermentation Technology, Faculty of Engineering, Higashi-Hiroshima, Japan
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External Links {🔗}(119)

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