We are analyzing https://link.springer.com/article/10.1007/s00249-015-1106-x.

Title:
Measuring kinetic drivers of pneumolysin pore structure | European Biophysics Journal
Description:
Most membrane attack complex-perforin/cholesterol-dependent cytolysin (MACPF/CDC) proteins are thought to form pores in target membranes by assembling into pre-pore oligomers before undergoing a pre-pore to pore transition. Assembly during pore formation is into both full rings of subunits and incomplete rings (arcs). The balance between arcs and full rings is determined by a mechanism dependent on protein concentration in which arc pores arise due to kinetic trapping of the pre-pore forms by the depletion of free protein subunits during oligomerization. Here we describe the use of a kinetic assay to study pore formation in red blood cells by the MACPF/CDC pneumolysin from Streptococcus pneumoniae. We show that cell lysis displays two kinds of dependence on protein concentration. At lower concentrations, it is dependent on the pre-pore to pore transition of arc oligomers, which we show to be a cooperative process. At higher concentrations, it is dependent on the amount of pneumolysin bound to the membrane and reflects the affinity of the protein for its receptor, cholesterol. A lag occurs before cell lysis begins; this is dependent on oligomerization of pneumolysin. Kinetic dissection of cell lysis by pneumolysin demonstrates the capacity of MACPF/CDCs to generate pore-forming oligomeric structures of variable size with, most likely, different functional roles in biology.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

Education
Fitness & Wellness
Science

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 7,643,078 visitors per month in the current month.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

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

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

Not every website is profit-driven; some are created to spread information or serve as an online presence. Websites can be made for many reasons. This could be one of them. Link.springer.com might have a hidden revenue stream, but it's not something we can detect.

Keywords {🔍}

pore, pubmed, article, google, scholar, gilbert, membrane, lysis, cas, rate, formation, cell, pneumolysin, concentration, prepore, lag, protein, pores, fig, proteins, toxin, phase, temperature, form, oligomerization, data, kinetic, macpfcdc, transition, dependence, poreforming, size, subunits, order, length, shown, model, attack, membranes, oligomers, arcs, concentrations, binding, biol, central, tweten, assembly, mechanism, anderluh, leung,

Topics {✒️}

beta-barrel-forming cholesterol-dependent cytolysin c-terminal membrane-binding domain perforin-mediated target-cell death article download pdf multimeric beta-barrel protein small-angle neutron scattering measuring kinetic drivers membrane attack complex/perforin curve-fitting program profit ce5500 double-beam spectrophotometer clostridium perfringens theta-toxin generate ring-shaped structures principal pore-forming subunit protease-nicked theta-toxin fluorescent dye-labeled proteins negative-stain electron microscopy perforin-mediated myocardial damage monomer-monomer interactions drive target antigen-presenting cells pore-forming protein involved macpf/cdc proteins bind protein molecule binds versatile pore-forming toxins lipid “flip-flop” macpf/cdc proteins—agents steady-state kinetic model real-time printer-plotter macpf/cdc pore size cholesterol-dependent cytolysin intermedilysin bacterial cholesterol-dependent cytolysin cytolytic pore-forming protein european economic area pore-forming proteins involves previously published images pre-pore oligomeric state perforin-related protein pleurotolysin pore-forming protein toxin macpf/cdc pore formation michaelis–menten equation study macpf/cdc proteins membrane attack complex protein subunits—monomers bind steady-state kinetics full size image partially toroidal structure purified pore-forming protein constitute pre-pore assemblies c8alpha-macpf reveals mechanism macpf/cdc pore activity ring-shaped pneumolysin oligomers

Questions {❓}

If rate phase A is governed by pre-pore to pore transition, and phase B by binding to the membrane, what governs the dependence of lag on toxin concentration?
If the pre-pore to pore transition governs rate phase A, what governs phase B?

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Measuring kinetic drivers of pneumolysin pore structure
         description:Most membrane attack complex-perforin/cholesterol-dependent cytolysin (MACPF/CDC) proteins are thought to form pores in target membranes by assembling into pre-pore oligomers before undergoing a pre-pore to pore transition. Assembly during pore formation is into both full rings of subunits and incomplete rings (arcs). The balance between arcs and full rings is determined by a mechanism dependent on protein concentration in which arc pores arise due to kinetic trapping of the pre-pore forms by the depletion of free protein subunits during oligomerization. Here we describe the use of a kinetic assay to study pore formation in red blood cells by the MACPF/CDC pneumolysin from Streptococcus pneumoniae. We show that cell lysis displays two kinds of dependence on protein concentration. At lower concentrations, it is dependent on the pre-pore to pore transition of arc oligomers, which we show to be a cooperative process. At higher concentrations, it is dependent on the amount of pneumolysin bound to the membrane and reflects the affinity of the protein for its receptor, cholesterol. A lag occurs before cell lysis begins; this is dependent on oligomerization of pneumolysin. Kinetic dissection of cell lysis by pneumolysin demonstrates the capacity of MACPF/CDCs to generate pore-forming oligomeric structures of variable size with, most likely, different functional roles in biology.
         datePublished:2016-02-23T00:00:00Z
         dateModified:2016-02-23T00:00:00Z
         pageStart:365
         pageEnd:376
         license:http://creativecommons.org/licenses/by/4.0/
         sameAs:https://doi.org/10.1007/s00249-015-1106-x
         keywords:
            Pore formation
            Kinetics
            MACPF/CDC
            Toroidal pore
            Oligomerization
            Membrane structure
            Biochemistry
            general
            Biological and Medical Physics
            Biophysics
            Cell Biology
            Neurobiology
            Membrane Biology
            Nanotechnology
         image:
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00249-015-1106-x/MediaObjects/249_2015_1106_Fig1_HTML.gif
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00249-015-1106-x/MediaObjects/249_2015_1106_Fig2_HTML.gif
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00249-015-1106-x/MediaObjects/249_2015_1106_Fig3_HTML.gif
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00249-015-1106-x/MediaObjects/249_2015_1106_Fig4_HTML.gif
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00249-015-1106-x/MediaObjects/249_2015_1106_Fig5_HTML.gif
         isPartOf:
            name:European Biophysics Journal
            issn:
               1432-1017
               0175-7571
            volumeNumber:45
            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:Robert J. C. Gilbert
               affiliation:
                     name:University of Oxford
                     address:
                        name:Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
               name:Andreas F.-P. Sonnen
               affiliation:
                     name:Structural and Computational Biology Unit
                     address:
                        name:European Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany
                        type:PostalAddress
                     type:Organization
               type:Person
         isAccessibleForFree:1
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:Measuring kinetic drivers of pneumolysin pore structure
      description:Most membrane attack complex-perforin/cholesterol-dependent cytolysin (MACPF/CDC) proteins are thought to form pores in target membranes by assembling into pre-pore oligomers before undergoing a pre-pore to pore transition. Assembly during pore formation is into both full rings of subunits and incomplete rings (arcs). The balance between arcs and full rings is determined by a mechanism dependent on protein concentration in which arc pores arise due to kinetic trapping of the pre-pore forms by the depletion of free protein subunits during oligomerization. Here we describe the use of a kinetic assay to study pore formation in red blood cells by the MACPF/CDC pneumolysin from Streptococcus pneumoniae. We show that cell lysis displays two kinds of dependence on protein concentration. At lower concentrations, it is dependent on the pre-pore to pore transition of arc oligomers, which we show to be a cooperative process. At higher concentrations, it is dependent on the amount of pneumolysin bound to the membrane and reflects the affinity of the protein for its receptor, cholesterol. A lag occurs before cell lysis begins; this is dependent on oligomerization of pneumolysin. Kinetic dissection of cell lysis by pneumolysin demonstrates the capacity of MACPF/CDCs to generate pore-forming oligomeric structures of variable size with, most likely, different functional roles in biology.
      datePublished:2016-02-23T00:00:00Z
      dateModified:2016-02-23T00:00:00Z
      pageStart:365
      pageEnd:376
      license:http://creativecommons.org/licenses/by/4.0/
      sameAs:https://doi.org/10.1007/s00249-015-1106-x
      keywords:
         Pore formation
         Kinetics
         MACPF/CDC
         Toroidal pore
         Oligomerization
         Membrane structure
         Biochemistry
         general
         Biological and Medical Physics
         Biophysics
         Cell Biology
         Neurobiology
         Membrane Biology
         Nanotechnology
      image:
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00249-015-1106-x/MediaObjects/249_2015_1106_Fig1_HTML.gif
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00249-015-1106-x/MediaObjects/249_2015_1106_Fig2_HTML.gif
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00249-015-1106-x/MediaObjects/249_2015_1106_Fig3_HTML.gif
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00249-015-1106-x/MediaObjects/249_2015_1106_Fig4_HTML.gif
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00249-015-1106-x/MediaObjects/249_2015_1106_Fig5_HTML.gif
      isPartOf:
         name:European Biophysics Journal
         issn:
            1432-1017
            0175-7571
         volumeNumber:45
         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:Robert J. C. Gilbert
            affiliation:
                  name:University of Oxford
                  address:
                     name:Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
            name:Andreas F.-P. Sonnen
            affiliation:
                  name:Structural and Computational Biology Unit
                  address:
                     name:European Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany
                     type:PostalAddress
                  type:Organization
            type:Person
      isAccessibleForFree:1
["Periodical","PublicationVolume"]:
      name:European Biophysics Journal
      issn:
         1432-1017
         0175-7571
      volumeNumber:45
Organization:
      name:Springer Berlin Heidelberg
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:University of Oxford
      address:
         name:Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK
         type:PostalAddress
      name:Structural and Computational Biology Unit
      address:
         name:European Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Robert J. C. Gilbert
      affiliation:
            name:University of Oxford
            address:
               name:Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK
               type:PostalAddress
            type:Organization
      email:[email protected]
      name:Andreas F.-P. Sonnen
      affiliation:
            name:Structural and Computational Biology Unit
            address:
               name:European Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK
      name:European Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany

External Links {🔗}(232)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js
Prism.js

CDN Services {📦}

Crossref

5.23s.

LINK . SPRINGER . COM {}