Here's how LINK.SPRINGER.COM makes money* and how much!

*Please read our disclaimer before using our estimates.
Loading...

LINK . SPRINGER . COM {}

  1. Analyzed Page
  2. Matching Content Categories
  3. CMS
  4. Monthly Traffic Estimate
  5. How Does Link.springer.com Make Money
  6. Keywords
  7. Topics
  8. Schema
  9. External Links
  10. Analytics And Tracking
  11. Libraries
  12. CDN Services

We are analyzing https://link.springer.com/article/10.1007/bf00039030.

Title:
Cloning and characterization of a cDNA encoding a mRNA rapidly-induced by ABA in barley aleurone layers | Plant Molecular Biology
Description:
Abscisic acid (ABA) inhibits the gibberellic acid induced synthesis of α-amylase in barley aleurone layers, yet ABA itself induces more than a dozen polypeptides (Lin & Ho, Plant Physiol 82: 289–297, 1986). As part of our effort to elucidate the molecular action of ABA in barley aleurone layers, we have isolated and characterized an ABA-induced cDNA clone, pHV A1. This cDNA clone hybridizes to an RNA species of approximately 1.1 kb from ABA-treated barley aleurone layers. The level of this mRNA is tripled within 40 minutes after ABA treatment, reaches a peak at 8–12 h, and is present up to 48 h. The induction of this mRNA responds to concentrations of ABA as low as 10-9 M, but higher ABA concentrations induce higher expression of this mRNA. The products of hybrid-select translation and in vitro transcription/translation with pHV A1 comigrate on SDS gel as a 27 kDa polypeptide. However, the sequence of pHV A1 indicates that it has an open reading frame encoding a 22 kDa protein. This size discrepancy is probably due to the high content of the basic amino acid, lysine. This notion has been confirmed by two-dimensional gel electrophoresis showing that this polypeptide is one of the most basic proteins in ABA-treated barley aleurone layers. The deduced amino acid sequence of pHV A1 contains nine imperfect repeats 11 amino acids long which share homology with cotton Lea 7 protein (Baker, Steele & Dure, Plant Mol Biol, in press). The identity and function of the encoded product of pHV A1 is under investigation.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Science
  • Education
  • Environment

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 5,000,016 visitors per month in the current month.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

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

The income method remains a mystery to us.

Earning money isn't the goal of every website; some are designed to offer support or promote social causes. People have different reasons for creating websites. This might be one such reason. Link.springer.com might be cashing in, but we can't detect the method they're using.

Keywords {🔍}

google, scholar, plant, barley, acid, aleurone, abscisic, layers, article, biol, molecular, aba, physiol, mrna, protein, biology, cloning, synthesis, mol, thd, content, cdna, expression, access, usa, dna, privacy, cookies, phv, sequence, press, gene, cells, publish, search, characterization, uknes, gibberellic, αamylase, action, open, high, amino, proteins, acids, embryos, proc, natl, acad, sci,

Topics {✒️}

month download article/chapter endogenous α-amylase inhibitor probable amylase/protease inhibitor barley amylase/subtilisin inhibitor aba-regulated gene expression aba-induced cdna clone cotton late embryogenesis-abundant barley aleurone layers rapid gene regulation cold spring harbor privacy choices/manage cookies cdna clone hybridizes full article pdf dna cloning techniques β-conglycinin expression barley aleurone cells double-stranded cdna plant mol biol storage-protein synthesis related subjects mature aleurone morphology basic amino acid recombinant dna molecules molecular biology heat-shock response molecular cloning dna fragments separated abscisic acid induction european economic area mrna rapidly-induced van vloten-doting zein cdnas obtained encephalomyocarditis virus-infected chain-terminating inhibitors developing wheat embryos conditions privacy policy july 1988 volume 11 hybrid-select translation messenger rna levels abscisic acid induces α-amylase wheat-germ agglutinin check access instant access accepting optional cookies article hong plant cells vitro transcription/translation nucleotide sequence analysis plant physiol 82

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Cloning and characterization of a cDNA encoding a mRNA rapidly-induced by ABA in barley aleurone layers
         description:Abscisic acid (ABA) inhibits the gibberellic acid induced synthesis of α-amylase in barley aleurone layers, yet ABA itself induces more than a dozen polypeptides (Lin & Ho, Plant Physiol 82: 289–297, 1986). As part of our effort to elucidate the molecular action of ABA in barley aleurone layers, we have isolated and characterized an ABA-induced cDNA clone, pHV A1. This cDNA clone hybridizes to an RNA species of approximately 1.1 kb from ABA-treated barley aleurone layers. The level of this mRNA is tripled within 40 minutes after ABA treatment, reaches a peak at 8–12 h, and is present up to 48 h. The induction of this mRNA responds to concentrations of ABA as low as 10-9 M, but higher ABA concentrations induce higher expression of this mRNA. The products of hybrid-select translation and in vitro transcription/translation with pHV A1 comigrate on SDS gel as a 27 kDa polypeptide. However, the sequence of pHV A1 indicates that it has an open reading frame encoding a 22 kDa protein. This size discrepancy is probably due to the high content of the basic amino acid, lysine. This notion has been confirmed by two-dimensional gel electrophoresis showing that this polypeptide is one of the most basic proteins in ABA-treated barley aleurone layers. The deduced amino acid sequence of pHV A1 contains nine imperfect repeats 11 amino acids long which share homology with cotton Lea 7 protein (Baker, Steele & Dure, Plant Mol Biol, in press). The identity and function of the encoded product of pHV A1 is under investigation.
         datePublished:
         dateModified:
         pageStart:495
         pageEnd:506
         sameAs:https://doi.org/10.1007/BF00039030
         keywords:
            abscisic acid
            barley aleurone layers
            cDNA cloning
            gene expression
            Plant Sciences
            Biochemistry
            general
            Plant Pathology
         image:
         isPartOf:
            name:Plant Molecular Biology
            issn:
               1573-5028
               0167-4412
            volumeNumber:11
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Kluwer Academic Publishers
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Bimei Hong
               affiliation:
                     name:Washington University
                     address:
                        name:Plant Biology Program, Department of Biology, Division of Biology and Biomedical Sciences, Washington University, St. Louis, USA
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Scott J. Uknes
               affiliation:
                     name:Washington University
                     address:
                        name:Plant Biology Program, Department of Biology, Division of Biology and Biomedical Sciences, Washington University, St. Louis, USA
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Tuan-hua David Ho
               affiliation:
                     name:Washington University
                     address:
                        name:Plant Biology Program, Department of Biology, Division of Biology and Biomedical Sciences, Washington University, St. Louis, USA
                        type:PostalAddress
                     type:Organization
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:Cloning and characterization of a cDNA encoding a mRNA rapidly-induced by ABA in barley aleurone layers
      description:Abscisic acid (ABA) inhibits the gibberellic acid induced synthesis of α-amylase in barley aleurone layers, yet ABA itself induces more than a dozen polypeptides (Lin & Ho, Plant Physiol 82: 289–297, 1986). As part of our effort to elucidate the molecular action of ABA in barley aleurone layers, we have isolated and characterized an ABA-induced cDNA clone, pHV A1. This cDNA clone hybridizes to an RNA species of approximately 1.1 kb from ABA-treated barley aleurone layers. The level of this mRNA is tripled within 40 minutes after ABA treatment, reaches a peak at 8–12 h, and is present up to 48 h. The induction of this mRNA responds to concentrations of ABA as low as 10-9 M, but higher ABA concentrations induce higher expression of this mRNA. The products of hybrid-select translation and in vitro transcription/translation with pHV A1 comigrate on SDS gel as a 27 kDa polypeptide. However, the sequence of pHV A1 indicates that it has an open reading frame encoding a 22 kDa protein. This size discrepancy is probably due to the high content of the basic amino acid, lysine. This notion has been confirmed by two-dimensional gel electrophoresis showing that this polypeptide is one of the most basic proteins in ABA-treated barley aleurone layers. The deduced amino acid sequence of pHV A1 contains nine imperfect repeats 11 amino acids long which share homology with cotton Lea 7 protein (Baker, Steele & Dure, Plant Mol Biol, in press). The identity and function of the encoded product of pHV A1 is under investigation.
      datePublished:
      dateModified:
      pageStart:495
      pageEnd:506
      sameAs:https://doi.org/10.1007/BF00039030
      keywords:
         abscisic acid
         barley aleurone layers
         cDNA cloning
         gene expression
         Plant Sciences
         Biochemistry
         general
         Plant Pathology
      image:
      isPartOf:
         name:Plant Molecular Biology
         issn:
            1573-5028
            0167-4412
         volumeNumber:11
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Kluwer Academic Publishers
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Bimei Hong
            affiliation:
                  name:Washington University
                  address:
                     name:Plant Biology Program, Department of Biology, Division of Biology and Biomedical Sciences, Washington University, St. Louis, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Scott J. Uknes
            affiliation:
                  name:Washington University
                  address:
                     name:Plant Biology Program, Department of Biology, Division of Biology and Biomedical Sciences, Washington University, St. Louis, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Tuan-hua David Ho
            affiliation:
                  name:Washington University
                  address:
                     name:Plant Biology Program, Department of Biology, Division of Biology and Biomedical Sciences, Washington University, St. Louis, USA
                     type:PostalAddress
                  type:Organization
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Plant Molecular Biology
      issn:
         1573-5028
         0167-4412
      volumeNumber:11
Organization:
      name:Kluwer Academic Publishers
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Washington University
      address:
         name:Plant Biology Program, Department of Biology, Division of Biology and Biomedical Sciences, Washington University, St. Louis, USA
         type:PostalAddress
      name:Washington University
      address:
         name:Plant Biology Program, Department of Biology, Division of Biology and Biomedical Sciences, Washington University, St. Louis, USA
         type:PostalAddress
      name:Washington University
      address:
         name:Plant Biology Program, Department of Biology, Division of Biology and Biomedical Sciences, Washington University, St. Louis, USA
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Bimei Hong
      affiliation:
            name:Washington University
            address:
               name:Plant Biology Program, Department of Biology, Division of Biology and Biomedical Sciences, Washington University, St. Louis, USA
               type:PostalAddress
            type:Organization
      name:Scott J. Uknes
      affiliation:
            name:Washington University
            address:
               name:Plant Biology Program, Department of Biology, Division of Biology and Biomedical Sciences, Washington University, St. Louis, USA
               type:PostalAddress
            type:Organization
      name:Tuan-hua David Ho
      affiliation:
            name:Washington University
            address:
               name:Plant Biology Program, Department of Biology, Division of Biology and Biomedical Sciences, Washington University, St. Louis, USA
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Plant Biology Program, Department of Biology, Division of Biology and Biomedical Sciences, Washington University, St. Louis, USA
      name:Plant Biology Program, Department of Biology, Division of Biology and Biomedical Sciences, Washington University, St. Louis, USA
      name:Plant Biology Program, Department of Biology, Division of Biology and Biomedical Sciences, Washington University, St. Louis, USA
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(67)

Analytics and Tracking {📊}

  • Google Tag Manager

Libraries {📚}

  • Clipboard.js
  • Prism.js

CDN Services {📦}

  • Crossref

4.47s.