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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. Questions
  9. Schema
  10. External Links
  11. Analytics And Tracking
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We are analyzing https://link.springer.com/article/10.1007/s00424-015-1777-2.

Title:
A Pore Idea: the ion conduction pathway of TMEM16/ANO proteins is composed partly of lipid | Pflügers Archiv - European Journal of Physiology
Description:
Since their first descriptions, ion channels have been conceived as proteinaceous conduits that facilitate the passage of ionic cargo between segregated environments. This concept is reinforced by crystallographic structures of cation channels depicting ion conductance pathways completely lined by protein. Although lipids are sometimes present in fenestrations near the pore or may be involved in channel gating, there is little or no evidence that lipids inhabit the ion conduction pathway. Indeed, the presence of lipid acyl chains in the conductance pathway would curse the design of the channel’s aqueous pore. Here, we make a speculative proposal that anion channels in the TMEM16/ANO superfamily have ion conductance pathways composed partly of lipids. Our reasoning is based on the idea that TMEM16 ion channels evolved from a kind of lipid transporter that scrambles lipids between leaflets of the membrane bilayer and the modeled structural similarity between TMEM16 lipid scramblases and TMEM16 anion channels. This novel view of the TMEM16 pore offers explanation for the biophysical and pharmacological oddness of TMEM16A. We build upon the recent X-ray structure of nhTMEM16 and develop models of both TMEM16 ion channels and lipid scramblases to bolster our proposal. It is our hope that this model of the TMEM16 pore will foster innovative investigation into TMEM16 function.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Education
  • Science
  • TV

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 7,642,828 visitors per month in the current month.

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

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

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. Link.springer.com could be getting rich in stealth mode, or the way it's monetizing isn't detectable.

Keywords {🔍}

pubmed, article, google, scholar, tmema, cas, lipid, channel, channels, tmemf, ion, membrane, central, pore, furrow, tmem, protein, lipids, phospholipid, hydrophilic, currents, head, selectivity, fig, groups, chloride, ions, scrambling, pathway, proteins, cell, function, ionic, structure, nhtmem, scramblases, scramblase, hydrophobic, biol, binding, physiol, conductance, pores, biophys, model, molecular, membranes, cells, shown, single,

Topics {✒️}

uk/memprotmd/beta/protein/pdbid/4wis n-methyl d-glucamine nfa article download pdf calcium-activated chloride conductance ca2+−activated cl-channels inferred calcium-activated chloride conductances calcium-activated chloride channels calcium-activated chloride channel calcium-activated chloride currents cysteine-reactive mts reagents needleman-wunsch alignment algorithm embl-ebi bioinformatics web explaining calcium-dependent gating calcium-dependent phospholipid scrambling ribosome-free membrane microcompartment cell-cell contact areas tmem16a/ano1 chloride channels limb-girdle muscular dystrophy calcium-dependent lipid binding cell-cell junction protein ca2+-activated cl− channels ca2+−activated cl- channels ca2+−activated cl- channel ano5-related muscle diseases ligand-gated ion channels cysteine-substituted tmem16a channels expression-cloning strategy aimed ca2+-dependent phospholipid scrambling european economic area recent x-ray structure de la fuente small pore-forming peptides wild-type tmem16f current large-scale phylogenetic analyses single channel conductance cysteine accessibility mutagenesis tmem16 chloride channels privacy choices/manage cookies manford ag distinct open states human perforin employs clc-0 chloride channel calcium-dependent gating produce multinucleated cells van heerde wl van deenen ll rat sensory neurons small-molecule activators bleeding disorder caused single channel recordings

Questions {❓}

  • A role for lipids in wine tasting?
  • Kunzelmann K, Nilius B, Owsianik G, Schreiber R, Ousingsawat J, Sirianant L, Wanitchakool P, Bevers EM, Heemskerk JW (2014) Molecular functions of anoctamin 6 (TMEM16F): a chloride channel, cation channel, or phospholipid scramblase?
  • Therefore, how does NFA access its binding site from both sides of the membrane and also compete with the permeant ion?

Schema {🗺️}

WebPage:
      mainEntity:
         headline:A Pore Idea: the ion conduction pathway of TMEM16/ANO proteins is composed partly of lipid
         description:Since their first descriptions, ion channels have been conceived as proteinaceous conduits that facilitate the passage of ionic cargo between segregated environments. This concept is reinforced by crystallographic structures of cation channels depicting ion conductance pathways completely lined by protein. Although lipids are sometimes present in fenestrations near the pore or may be involved in channel gating, there is little or no evidence that lipids inhabit the ion conduction pathway. Indeed, the presence of lipid acyl chains in the conductance pathway would curse the design of the channel’s aqueous pore. Here, we make a speculative proposal that anion channels in the TMEM16/ANO superfamily have ion conductance pathways composed partly of lipids. Our reasoning is based on the idea that TMEM16 ion channels evolved from a kind of lipid transporter that scrambles lipids between leaflets of the membrane bilayer and the modeled structural similarity between TMEM16 lipid scramblases and TMEM16 anion channels. This novel view of the TMEM16 pore offers explanation for the biophysical and pharmacological oddness of TMEM16A. We build upon the recent X-ray structure of nhTMEM16 and develop models of both TMEM16 ion channels and lipid scramblases to bolster our proposal. It is our hope that this model of the TMEM16 pore will foster innovative investigation into TMEM16 function.
         datePublished:2016-01-06T00:00:00Z
         dateModified:2016-01-06T00:00:00Z
         pageStart:455
         pageEnd:473
         sameAs:https://doi.org/10.1007/s00424-015-1777-2
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            TMEM16
            Chloride channel
            Phospholipid scrambling
            Protein-lipid interactions
            Calcium
            Human Physiology
            Molecular Medicine
            Neurosciences
            Cell Biology
            Receptors
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      headline:A Pore Idea: the ion conduction pathway of TMEM16/ANO proteins is composed partly of lipid
      description:Since their first descriptions, ion channels have been conceived as proteinaceous conduits that facilitate the passage of ionic cargo between segregated environments. This concept is reinforced by crystallographic structures of cation channels depicting ion conductance pathways completely lined by protein. Although lipids are sometimes present in fenestrations near the pore or may be involved in channel gating, there is little or no evidence that lipids inhabit the ion conduction pathway. Indeed, the presence of lipid acyl chains in the conductance pathway would curse the design of the channel’s aqueous pore. Here, we make a speculative proposal that anion channels in the TMEM16/ANO superfamily have ion conductance pathways composed partly of lipids. Our reasoning is based on the idea that TMEM16 ion channels evolved from a kind of lipid transporter that scrambles lipids between leaflets of the membrane bilayer and the modeled structural similarity between TMEM16 lipid scramblases and TMEM16 anion channels. This novel view of the TMEM16 pore offers explanation for the biophysical and pharmacological oddness of TMEM16A. We build upon the recent X-ray structure of nhTMEM16 and develop models of both TMEM16 ion channels and lipid scramblases to bolster our proposal. It is our hope that this model of the TMEM16 pore will foster innovative investigation into TMEM16 function.
      datePublished:2016-01-06T00:00:00Z
      dateModified:2016-01-06T00:00:00Z
      pageStart:455
      pageEnd:473
      sameAs:https://doi.org/10.1007/s00424-015-1777-2
      keywords:
         Anoctamin
         TMEM16
         Chloride channel
         Phospholipid scrambling
         Protein-lipid interactions
         Calcium
         Human Physiology
         Molecular Medicine
         Neurosciences
         Cell Biology
         Receptors
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                  address:
                     name:Department of Cell Biology, Emory University School of Medicine, Atlanta, USA
                     type:PostalAddress
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            type:Person
            name:H. Criss Hartzell
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                  name:Emory University School of Medicine
                  address:
                     name:Department of Cell Biology, Emory University School of Medicine, Atlanta, USA
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            name:Emory University School of Medicine
            address:
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               type:PostalAddress
            type:Organization
      name:H. Criss Hartzell
      url:http://orcid.org/0000-0002-3393-1528
      affiliation:
            name:Emory University School of Medicine
            address:
               name:Department of Cell Biology, Emory University School of Medicine, Atlanta, USA
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Department of Cell Biology, Emory University School of Medicine, Atlanta, USA
      name:Department of Cell Biology, Emory University School of Medicine, Atlanta, USA

External Links {🔗}(552)

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