We are analyzing https://link.springer.com/article/10.1007/bf02738118.

Title:
Exonucleases and the incorporation of aranucleotides into DNA | Cell Biochemistry and Biophysics
Description:
The polymerization of nucleotide analogs into DNA is a common strategy used to inhibit DNA synthesis in rapidly dividing tumor cells and viruses. The mammalian DNA polymerases catalyze the insertion of the arabinofuranosyl analogs of dNTPs (aranucleotides) into DNA efficiently, but elongate from the 3′ aranucleotides poorly. Slow elongation provides an opportunity for exonucleases to remove aranucleotides. The exonuclease activity associated with DNA polymerase δ removes araCMP from 3′ termini with the same efficiency that it removes a paired 3′ deoxycytosine suggesting that the proofreading exonucleases associated with DNA polymerases might remove aranucleotides inefficiently. A separate 30 kDa exonuclease has been purified from mammalian cells that removes araCMP from 3′ termini. The activity of this enzyme in the cell could remove aranucleotides from 3′ termini of DNA and decrease the efficacy of the analogs. Inhibition analysis of the purified exonuclease shows that this enzyme is inhibited by thioinosine monophosphate (TIMP) with aK i=17 μM. When high TIMP levels are generated in HL-60 cells, incorporation of araC in DNA is increased about 16-fold relative to total DNA synthesis. This increased araC in DNA is likely a result of exonuclease inhibition in the cell. Thus, exonucleases in cells might play an important role in removing aranucleotides inserted by DNA polymerases.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

Education
Science
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 5,000,019 visitors per month in the current month.
However, some sources were not loaded, we suggest to reload the page to get complete results.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

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

We can't tell how the site generates income.

While profit motivates many websites, others exist to inspire, entertain, or provide valuable resources. Websites have a variety of goals. And this might be one of them. Link.springer.com might have a hidden revenue stream, but it's not something we can detect.

Keywords {🔍}

dna, google, scholar, cas, article, pubmed, incorporation, exonuclease, biol, human, chem, aranucleotides, perrino, cell, synthesis, cells, access, replication, pharmacol, kufe, privacy, cookies, content, exonucleases, mammalian, polymerases, activity, inhibition, monophosphate, arac, egan, publish, search, analogs, remove, polymerase, removes, termini, proofreading, repair, enzymes, usa, effects, res, major, analysis, data, information, log, journal,

Topics {✒️}

anticancer nucleoside arabinosylcytosine month download article/chapter polymerase η–promoted resistance ph-step alkaline elution human dna polymerase-ε anti-neoplastic agent arabinosylcytosine related subjects mismatch repair pre-steady state methods polyacrylamide gel electrophoresis 1-β-d-arabinofuranosyladenosine triphosphate 1-β-d-arabinofuranosycytosine incorporation inhibit dna synthesis total dna synthesis full article pdf distinct enzymes nucleolytic enzymes dna polymerase-β human dna polymerase privacy choices/manage cookies 1-β-d-arabinofuranosylcytosine incorporation nucleotide analogs dna replication fidelity deoxyribonucleic acid synthesis dna polymerases alpha dna polymerase iii specific dna sequences fludarabine-terminated dna article cell biochemistry ε incorporate fialuridine 1-β-d-arabinofuranosylcytosine dna synthesis human myeloblasts correlates human β-polymerases european economic area hydrogen bonding revisited intracellular pharmacodynamic studies excision human neoplastic cells mammalian tumor cells-1 check access instant access conditions privacy policy dna replication van der marel restrained molecular dynamics cytosine arabinoside monophosphate human leukemia cells human leukemic cells accepting optional cookies

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Exonucleases and the incorporation of aranucleotides into DNA
         description:The polymerization of nucleotide analogs into DNA is a common strategy used to inhibit DNA synthesis in rapidly dividing tumor cells and viruses. The mammalian DNA polymerases catalyze the insertion of the arabinofuranosyl analogs of dNTPs (aranucleotides) into DNA efficiently, but elongate from the 3′ aranucleotides poorly. Slow elongation provides an opportunity for exonucleases to remove aranucleotides. The exonuclease activity associated with DNA polymerase δ removes araCMP from 3′ termini with the same efficiency that it removes a paired 3′ deoxycytosine suggesting that the proofreading exonucleases associated with DNA polymerases might remove aranucleotides inefficiently. A separate 30 kDa exonuclease has been purified from mammalian cells that removes araCMP from 3′ termini. The activity of this enzyme in the cell could remove aranucleotides from 3′ termini of DNA and decrease the efficacy of the analogs. Inhibition analysis of the purified exonuclease shows that this enzyme is inhibited by thioinosine monophosphate (TIMP) with aK i=17 μM. When high TIMP levels are generated in HL-60 cells, incorporation of araC in DNA is increased about 16-fold relative to total DNA synthesis. This increased araC in DNA is likely a result of exonuclease inhibition in the cell. Thus, exonucleases in cells might play an important role in removing aranucleotides inserted by DNA polymerases.
         datePublished:
         dateModified:
         pageStart:331
         pageEnd:352
         sameAs:https://doi.org/10.1007/BF02738118
         keywords:
            DNA replication
            DNA repair
            chemosensitivity
            anticancer therapy
            Biochemistry
            general
            Pharmacology/Toxicology
            Biotechnology
            Cell Biology
            Biological and Medical Physics
            Biophysics
         image:
         isPartOf:
            name:Cell Biochemistry and Biophysics
            issn:
               1559-0283
               1085-9195
            volumeNumber:30
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Humana Press
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Fred W. Perrino
               affiliation:
                     name:Wake Forest University School of Medicine
                     address:
                        name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Dan J. Mazur
               affiliation:
                     name:Wake Forest University School of Medicine
                     address:
                        name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Heather Ward
               affiliation:
                     name:Wake Forest University School of Medicine
                     address:
                        name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Scott Harvey
               affiliation:
                     name:Wake Forest University School of Medicine
                     address:
                        name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
                        type:PostalAddress
                     type:Organization
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:Exonucleases and the incorporation of aranucleotides into DNA
      description:The polymerization of nucleotide analogs into DNA is a common strategy used to inhibit DNA synthesis in rapidly dividing tumor cells and viruses. The mammalian DNA polymerases catalyze the insertion of the arabinofuranosyl analogs of dNTPs (aranucleotides) into DNA efficiently, but elongate from the 3′ aranucleotides poorly. Slow elongation provides an opportunity for exonucleases to remove aranucleotides. The exonuclease activity associated with DNA polymerase δ removes araCMP from 3′ termini with the same efficiency that it removes a paired 3′ deoxycytosine suggesting that the proofreading exonucleases associated with DNA polymerases might remove aranucleotides inefficiently. A separate 30 kDa exonuclease has been purified from mammalian cells that removes araCMP from 3′ termini. The activity of this enzyme in the cell could remove aranucleotides from 3′ termini of DNA and decrease the efficacy of the analogs. Inhibition analysis of the purified exonuclease shows that this enzyme is inhibited by thioinosine monophosphate (TIMP) with aK i=17 μM. When high TIMP levels are generated in HL-60 cells, incorporation of araC in DNA is increased about 16-fold relative to total DNA synthesis. This increased araC in DNA is likely a result of exonuclease inhibition in the cell. Thus, exonucleases in cells might play an important role in removing aranucleotides inserted by DNA polymerases.
      datePublished:
      dateModified:
      pageStart:331
      pageEnd:352
      sameAs:https://doi.org/10.1007/BF02738118
      keywords:
         DNA replication
         DNA repair
         chemosensitivity
         anticancer therapy
         Biochemistry
         general
         Pharmacology/Toxicology
         Biotechnology
         Cell Biology
         Biological and Medical Physics
         Biophysics
      image:
      isPartOf:
         name:Cell Biochemistry and Biophysics
         issn:
            1559-0283
            1085-9195
         volumeNumber:30
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Humana Press
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Fred W. Perrino
            affiliation:
                  name:Wake Forest University School of Medicine
                  address:
                     name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Dan J. Mazur
            affiliation:
                  name:Wake Forest University School of Medicine
                  address:
                     name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Heather Ward
            affiliation:
                  name:Wake Forest University School of Medicine
                  address:
                     name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Scott Harvey
            affiliation:
                  name:Wake Forest University School of Medicine
                  address:
                     name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
                     type:PostalAddress
                  type:Organization
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Cell Biochemistry and Biophysics
      issn:
         1559-0283
         1085-9195
      volumeNumber:30
Organization:
      name:Humana Press
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Wake Forest University School of Medicine
      address:
         name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
         type:PostalAddress
      name:Wake Forest University School of Medicine
      address:
         name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
         type:PostalAddress
      name:Wake Forest University School of Medicine
      address:
         name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
         type:PostalAddress
      name:Wake Forest University School of Medicine
      address:
         name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Fred W. Perrino
      affiliation:
            name:Wake Forest University School of Medicine
            address:
               name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
               type:PostalAddress
            type:Organization
      name:Dan J. Mazur
      affiliation:
            name:Wake Forest University School of Medicine
            address:
               name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
               type:PostalAddress
            type:Organization
      name:Heather Ward
      affiliation:
            name:Wake Forest University School of Medicine
            address:
               name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
               type:PostalAddress
            type:Organization
      name:Scott Harvey
      affiliation:
            name:Wake Forest University School of Medicine
            address:
               name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
      name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
      name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
      name:Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(109)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js
Prism.js

CDN Services {📦}

Crossref

3.96s.

LINK . SPRINGER . COM {}