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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 {πŸ“š}

  • Education
  • Science
  • Health & Fitness

Content Management System {πŸ“}

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Custom-built

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Traffic Estimate {πŸ“ˆ}

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

πŸ™οΈ Massive Traffic: 50M - 100M visitors per month


Based on our best estimate, this website will receive around 76,749,346 visitors per month in the current month.

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How Does Doi.org Make Money? {πŸ’Έ}

We don't see any clear sign of profit-making.

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. Doi.org has a secret sauce for making money, but we can't detect it yet.

Keywords {πŸ”}

pubmed, article, google, scholar, cas, leishmania, protein, central, phosphatase, donovani, hsp, parasite, cell, major, morales, differentiation, biol, mol, stress, access, resistance, clos, molecular, beverley, intracellular, expression, heat, kinase, human, plos, microbiol, parasitol, httpsdoiorgs, content, research, phosphorylation, norrismullins, parasites, drug, role, shock, references, leishmaniasis, serinethreonine, chem, stage, spath, activity, lines, death,

Topics {βœ’οΈ}

loading [mathjax]/jax/output/html-css/config author information authors mitogen-activated protein kinase major pp5 null-mutant stage-specific gene expression pp5 null-mutant parasites article norris-mullins extracellular signal-regulated kinase privacy choices/manage cookies methylene tetrahydrofolate dehydrogenase/cyclohydrolase institutional animal care n-terminal dimerization reaction wild-type catalytic proficiency stress-regulated cochaperone aha1 supplementary figure 2 negative selection principle full article pdf attractive potential target tpr domain-mediated regulation life-cycle differentiation signal leishmania donovani phosphoglycans leishmania donovani isolates leishmania donovani treated heat stress conditions dominant negative mutant natural antimony resistance quantifying leishmania major leishmania phosphatase pp5 pathogenic amastigote stage leishmania donovani interacts regulating parasite stress intracellular protozoan parasites stable mutants intracellular pathogenic amastigote conditions privacy policy human breast cancer central players williams ma experimental paromomycin resistance requena jm stress response article log carboxy-terminal region density gradient centrifugation author correspondence molecular chaperone hsp90 forms protein complex check access instant access important neglected diseases

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
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            Medical Microbiology
            Microbiology
            Immunology
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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.
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          Leishmania
         Stress response
         Phosphatase
         Virulence
         Drug target
         Medical Microbiology
         Microbiology
         Immunology
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