DOI . ORG {}

Analyzed Page
Matching Content Categories
CMS
Monthly Traffic Estimate
How Does Doi.org Make Money
Keywords
Topics
Questions
Schema
External Links
Analytics And Tracking
Libraries
Hosting Providers

We began analyzing https://link.springer.com/article/10.1007/s00436-018-5994-4, but it redirected us to https://link.springer.com/article/10.1007/s00436-018-5994-4. The analysis below is for the second page.

Title[redir]:
Leishmania phosphatase PP5 is a regulator of HSP83 phosphorylation and essential for parasite pathogenicity | Parasitology Research
Description:
Leishmania parasites are responsible for important neglected diseases in humans and animals, ranging from self-healing cutaneous lesions to fatal visceral manifestations. During the infectious cycle, Leishmania differentiates from the extracellular flagellated promastigote to the intracellular pathogenic amastigote. Parasite differentiation is triggered by changes in environmental cues, mainly pH and temperature. In general, extracellular signals are translated into stage-specific gene expression by a cascade of reversible protein phosphorylation regulated by protein kinases and phosphatases. Though protein kinases have been actively studied as potential anti-parasitic drug targets, our understanding of the biology of protein phosphatases in Leishmania is poor. We have previously reported the principal analysis of a novel protein phosphatase 5 (PP5) in Leishmania species. Here, we assessed the role of PP5 in parasite pathogenicity, where we uncovered, using transgenic PP5 over-expressing and PP5 null-mutant parasites, its importance in metacyclogeneisis, maintaining HSP83 phosphorylation homeostasis and virulence. All together, our results indicate the importance of PP5 in regulating parasite stress and adaptation during differentiation, making this protein an attractive potential target for therapeutic intervention.

Matching Content Categories {📚}

Education
Science
Health & Fitness

Content Management System {📝}

What CMS is doi.org built with?

Custom-built

No common CMS systems were detected on Doi.org, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of doi.org audience?

🏙️ Massive Traffic: 50M - 100M visitors per month

Based on our best estimate, this website will receive around 89,058,038 visitors per month in the current month.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Doi.org Make Money? {💸}

We can't see how the site brings in money.

Not all websites focus on profit; some are designed to educate, connect people, or share useful tools. People create websites for numerous reasons. And this could be one such example. Doi.org has a revenue plan, but it's either invisible or we haven't found it.

Keywords {🔍}

pubmed, article, google, scholar, cas, leishmania, protein, central, phosphatase, donovani, parasite, cell, hsp, differentiation, major, morales, biol, mol, access, heat, clos, molecular, beverley, privacy, cookies, content, research, search, phosphorylation, parasites, stress, shock, plos, resistance, microbiol, parasitol, essential, publish, norrismullins, intracellular, expression, kinases, drug, role, kinase, leishmaniasis, human, serinethreonine, chem, stage,

Topics {✒️}

month download article/chapter mitogen-activated protein kinase stage-specific gene expression article norris-mullins extracellular signal-regulated kinase methylene tetrahydrofolate dehydrogenase/cyclohydrolase n-terminal dimerization reaction wild-type catalytic proficiency pp5 null-mutant parasites stress-regulated cochaperone aha1 major pp5 null-mutant negative selection principle full article pdf attractive potential target heat stress conditions intracellular protozoan parasites supplementary figure 2 tpr domain-mediated regulation life-cycle differentiation signal dominant negative mutant related subjects natural antimony resistance privacy choices/manage cookies pathogenic amastigote stage intracellular pathogenic amastigote quantifying leishmania major leishmania phosphatase pp5 leishmania donovani phosphoglycans leishmania donovani isolates leishmania donovani treated regulating parasite stress central players williams ma experimental paromomycin resistance human breast cancer requena jm stress response carboxy-terminal region density gradient centrifugation leishmania donovani interacts forms protein complex molecular chaperone hsp90 intracellular survival institutional animal care article log european economic area important neglected diseases healing cutaneous lesions extracellular flagellated promastigote glucocorticoid receptor heterocomplexes

Questions {❓}

Zangger H, Mottram JC, Fasel N (2002) Cell death in Leishmania induced by stress and differentiation: programmed cell death or necrosis?

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Leishmania phosphatase PP5 is a regulator of HSP83 phosphorylation and essential for parasite pathogenicity
         description:Leishmania parasites are responsible for important neglected diseases in humans and animals, ranging from self-healing cutaneous lesions to fatal visceral manifestations. During the infectious cycle, Leishmania differentiates from the extracellular flagellated promastigote to the intracellular pathogenic amastigote. Parasite differentiation is triggered by changes in environmental cues, mainly pH and temperature. In general, extracellular signals are translated into stage-specific gene expression by a cascade of reversible protein phosphorylation regulated by protein kinases and phosphatases. Though protein kinases have been actively studied as potential anti-parasitic drug targets, our understanding of the biology of protein phosphatases in Leishmania is poor. We have previously reported the principal analysis of a novel protein phosphatase 5 (PP5) in Leishmania species. Here, we assessed the role of PP5 in parasite pathogenicity, where we uncovered, using transgenic PP5 over-expressing and PP5 null-mutant parasites, its importance in metacyclogeneisis, maintaining HSP83 phosphorylation homeostasis and virulence. All together, our results indicate the importance of PP5 in regulating parasite stress and adaptation during differentiation, making this protein an attractive potential target for therapeutic intervention.
         datePublished:2018-07-08T00:00:00Z
         dateModified:2018-07-08T00:00:00Z
         pageStart:2971
         pageEnd:2985
         sameAs:https://doi.org/10.1007/s00436-018-5994-4
         keywords:
             Leishmania
            Stress response
            Phosphatase
            Virulence
            Drug target
            Medical Microbiology
            Microbiology
            Immunology
         image:
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00436-018-5994-4/MediaObjects/436_2018_5994_Fig1_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00436-018-5994-4/MediaObjects/436_2018_5994_Fig2_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00436-018-5994-4/MediaObjects/436_2018_5994_Fig3_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00436-018-5994-4/MediaObjects/436_2018_5994_Fig4_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00436-018-5994-4/MediaObjects/436_2018_5994_Fig5_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00436-018-5994-4/MediaObjects/436_2018_5994_Fig6_HTML.png
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00436-018-5994-4/MediaObjects/436_2018_5994_Fig7_HTML.png
         isPartOf:
            name:Parasitology Research
            issn:
               1432-1955
               0932-0113
            volumeNumber:117
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Springer Berlin Heidelberg
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Brianna Norris-Mullins
               affiliation:
                     name:University of Notre Dame
                     address:
                        name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Joseph S. Krivda
               affiliation:
                     name:University of Notre Dame
                     address:
                        name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Kathryn L. Smith
               affiliation:
                     name:University of Notre Dame
                     address:
                        name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Micah J. Ferrell
               affiliation:
                     name:University of Notre Dame
                     address:
                        name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Miguel A. Morales
               url:http://orcid.org/0000-0001-7676-2915
               affiliation:
                     name:University of Notre Dame
                     address:
                        name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:Leishmania phosphatase PP5 is a regulator of HSP83 phosphorylation and essential for parasite pathogenicity
      description:Leishmania parasites are responsible for important neglected diseases in humans and animals, ranging from self-healing cutaneous lesions to fatal visceral manifestations. During the infectious cycle, Leishmania differentiates from the extracellular flagellated promastigote to the intracellular pathogenic amastigote. Parasite differentiation is triggered by changes in environmental cues, mainly pH and temperature. In general, extracellular signals are translated into stage-specific gene expression by a cascade of reversible protein phosphorylation regulated by protein kinases and phosphatases. Though protein kinases have been actively studied as potential anti-parasitic drug targets, our understanding of the biology of protein phosphatases in Leishmania is poor. We have previously reported the principal analysis of a novel protein phosphatase 5 (PP5) in Leishmania species. Here, we assessed the role of PP5 in parasite pathogenicity, where we uncovered, using transgenic PP5 over-expressing and PP5 null-mutant parasites, its importance in metacyclogeneisis, maintaining HSP83 phosphorylation homeostasis and virulence. All together, our results indicate the importance of PP5 in regulating parasite stress and adaptation during differentiation, making this protein an attractive potential target for therapeutic intervention.
      datePublished:2018-07-08T00:00:00Z
      dateModified:2018-07-08T00:00:00Z
      pageStart:2971
      pageEnd:2985
      sameAs:https://doi.org/10.1007/s00436-018-5994-4
      keywords:
          Leishmania
         Stress response
         Phosphatase
         Virulence
         Drug target
         Medical Microbiology
         Microbiology
         Immunology
      image:
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00436-018-5994-4/MediaObjects/436_2018_5994_Fig1_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00436-018-5994-4/MediaObjects/436_2018_5994_Fig2_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00436-018-5994-4/MediaObjects/436_2018_5994_Fig3_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00436-018-5994-4/MediaObjects/436_2018_5994_Fig4_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00436-018-5994-4/MediaObjects/436_2018_5994_Fig5_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00436-018-5994-4/MediaObjects/436_2018_5994_Fig6_HTML.png
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00436-018-5994-4/MediaObjects/436_2018_5994_Fig7_HTML.png
      isPartOf:
         name:Parasitology Research
         issn:
            1432-1955
            0932-0113
         volumeNumber:117
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Springer Berlin Heidelberg
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Brianna Norris-Mullins
            affiliation:
                  name:University of Notre Dame
                  address:
                     name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Joseph S. Krivda
            affiliation:
                  name:University of Notre Dame
                  address:
                     name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Kathryn L. Smith
            affiliation:
                  name:University of Notre Dame
                  address:
                     name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Micah J. Ferrell
            affiliation:
                  name:University of Notre Dame
                  address:
                     name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Miguel A. Morales
            url:http://orcid.org/0000-0001-7676-2915
            affiliation:
                  name:University of Notre Dame
                  address:
                     name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Parasitology Research
      issn:
         1432-1955
         0932-0113
      volumeNumber:117
Organization:
      name:Springer Berlin Heidelberg
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:University of Notre Dame
      address:
         name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
         type:PostalAddress
      name:University of Notre Dame
      address:
         name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
         type:PostalAddress
      name:University of Notre Dame
      address:
         name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
         type:PostalAddress
      name:University of Notre Dame
      address:
         name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
         type:PostalAddress
      name:University of Notre Dame
      address:
         name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Brianna Norris-Mullins
      affiliation:
            name:University of Notre Dame
            address:
               name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
               type:PostalAddress
            type:Organization
      name:Joseph S. Krivda
      affiliation:
            name:University of Notre Dame
            address:
               name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
               type:PostalAddress
            type:Organization
      name:Kathryn L. Smith
      affiliation:
            name:University of Notre Dame
            address:
               name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
               type:PostalAddress
            type:Organization
      name:Micah J. Ferrell
      affiliation:
            name:University of Notre Dame
            address:
               name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
               type:PostalAddress
            type:Organization
      name:Miguel A. Morales
      url:http://orcid.org/0000-0001-7676-2915
      affiliation:
            name:University of Notre Dame
            address:
               name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
      name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
      name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
      name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
      name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(279)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js
Prism.js

Emails and Hosting {✉️}

Mail Servers:

mx.zoho.eu
mx2.zoho.eu
mx3.zoho.eu

Name Servers:

josh.ns.cloudflare.com
zita.ns.cloudflare.com

5.31s.