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We are analyzing https://link.springer.com/article/10.1007/s00436-018-5994-4.

Title:
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.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {πŸ“š}

  • Education
  • Science
  • Health & Fitness

Content Management System {πŸ“}

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 {πŸ“ˆ}

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.
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How Does Link.springer.com Make Money? {πŸ’Έ}

We're unsure how the site profits.

Many websites are intended to earn money, but some serve to share ideas or build connections. Websites exist for all kinds of purposes. This might be one of them. Link.springer.com could have a money-making trick up its sleeve, but it's undetectable for now.

Keywords {πŸ”}

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 {βœ’οΈ}

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 {πŸ—ΊοΈ}

WebPage:
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         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
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                        name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
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      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
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               type:PostalAddress
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            address:
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               type:PostalAddress
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      name:Eck Institute for Global Health, Department of Biological Sciences, 278 Galvin Life Science, University of Notre Dame, Notre Dame, USA
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