Here's how LINK.SPRINGER.COM makes money* and how much!

*Please read our disclaimer before using our estimates.
Loading...

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
  12. Libraries
  13. CDN Services

We are analyzing https://link.springer.com/chapter/10.1007/s10254-004-0033-5.

Title:
Large clostridial cytotoxins | SpringerLink
Description:
The large clostridial cytotoxins are a family of structurally and functionally related exotoxins from Clostridium difficile (toxins A and B), C. sordellii (lethal and hemorrhagic toxin) and C. novyi (α-toxin). The exotoxins are major pathogenicity factors which...
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Education
  • Science
  • Telecommunications

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? {💸}

The income method remains a mystery to us.

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 could have a money-making trick up its sleeve, but it's undetectable for now.

Keywords {🔍}

google, scholar, cas, pubmed, clostridium, article, difficile, toxin, biol, infect, toxins, cell, aktories, immun, cells, eichelstreiber, microbiol, chem, rho, human, clostridial, hofmann, lamont, sordellii, pothoulakis, proteins, chapter, large, gtpases, clin, cytotoxins, lethal, effects, protein, domain, mol, thelestam, wilkins, gene, med, biochem, binding, sauerborn, selzer, intestinal, cultured, molecular, diarrhea, structure, cytotoxin,

Topics {✒️}

cation-dependent udp-glucose hydrolases actin-specific adp-ribosyltransferase produced c-terminal structure homologous month download article/chapter toxin b-positive strain rho/rho-kinase mediated signaling small gtp-binding proteins il-1beta-dependent pathway activates dual caspase-dependent phorbol ester-stimulated phospholipase binding-active human glycosphingolipid toxin b-positive strains x-ray crystal structure clostridium novyi alpha-toxin toxin a-negative strains low ph-induced formation sequence galα1-3galβ1-4glcnac n-terminal region involved de vries-smits amm increases intestinal permeability actin-specific adp-ribosyltransferase complete receptor-binding domain clostridium novyi α-toxin streptococcal ligand-binding proteins n-terminal catalytic domain high n-terminal homology inhibit small gtpases rho-gtpases functionally inactive actin-adp-ribosylating toxins single-chain protein toxins von eichel-streiber cytotoxin l-encoding gene toxin a-negative ras-related protein ral metal binding sites tight junction permeability large clostridial cytotoxins large clostridial cytotoxins rhizoid tip growth human carbohydrate antigens privacy choices/manage cookies carbohydrate binding region complete binary toxin ph-induced conformational mediates monocytes necrosis chaves-olarte β-galactoside-a-1 sordellii lethal toxin n-terminal region device instant download

Questions {❓}

  • Boquet P, Lemichez E (2003) Bacterial virulence factors targeting Rho GTPases: parasitism or symbiosis?

Schema {🗺️}

ScholarlyArticle:
      headline:Large clostridial cytotoxins
      pageEnd:47
      pageStart:23
      image:https://media.springernature.com/w153/springer-static/cover/book/978-3-540-27115-4.jpg
      genre:
         Biomedical and Life Sciences
         Biomedical and Life Sciences (R0)
      isPartOf:
         name:Reviews of Physiology, Biochemistry and Pharmacology
         isbn:
            978-3-540-27115-4
            978-3-540-23131-8
         type:Book
      publisher:
         name:Springer Berlin Heidelberg
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:I. Just
            affiliation:
                  name:Medizinische Hochschlule Hannover
                  address:
                     name:Institut für Toxikologie, Medizinische Hochschlule Hannover, Hannover, Germany
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
            name:R. Gerhard
            affiliation:
                  name:Medizinische Hochschlule Hannover
                  address:
                     name:Institut für Toxikologie, Medizinische Hochschlule Hannover, Hannover, Germany
                     type:PostalAddress
                  type:Organization
            type:Person
      keywords:Clostridium Difficile, Pseudomembranous Colitis, Lethal Toxin, Clostridium Difficile Toxin, Guanine Nucleotide Dissociation Inhibitor
      description:The large clostridial cytotoxins are a family of structurally and functionally related exotoxins from Clostridium difficile (toxins A and B), C. sordellii (lethal and hemorrhagic toxin) and C. novyi (α-toxin). The exotoxins are major pathogenicity factors which in addition to their in vivo effects are cytotoxic to cultured cell lines causing reorganization of the cytoskeleton accompanied by morphological changes. The exotoxins are single-chain protein toxins, which are constructed of three domains: receptor-binding, translocation and catalytic domain. These domains reflect the self-mediated cell entry via receptor-mediated endocytosis, translocation into the cytoplasm, and execution of their cytotoxic activity by an inherent enzyme activity. Enzymatically, the toxins catalyze the transfer of a glucosyl moiety from UDP-glucose to the intracellular target proteins which are the Rho and Ras GTPases. The covalent attachment of the glucose moiety to a conserved threonine within the effector region of the GTPases renders the Rho-GTPases functionally inactive. Whereas the molecular mode of cytotoxic effects is fully understood, the mechanisms leading to inflammatory processes in the context of disease (e.g., antibiotic-associated pseudomembranous colitis caused by Clostridium difficile) are less clear.
      datePublished:2004
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
      context:https://schema.org
Book:
      name:Reviews of Physiology, Biochemistry and Pharmacology
      isbn:
         978-3-540-27115-4
         978-3-540-23131-8
Organization:
      name:Springer Berlin Heidelberg
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Medizinische Hochschlule Hannover
      address:
         name:Institut für Toxikologie, Medizinische Hochschlule Hannover, Hannover, Germany
         type:PostalAddress
      name:Medizinische Hochschlule Hannover
      address:
         name:Institut für Toxikologie, Medizinische Hochschlule Hannover, Hannover, Germany
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:I. Just
      affiliation:
            name:Medizinische Hochschlule Hannover
            address:
               name:Institut für Toxikologie, Medizinische Hochschlule Hannover, Hannover, Germany
               type:PostalAddress
            type:Organization
      email:[email protected]
      name:R. Gerhard
      affiliation:
            name:Medizinische Hochschlule Hannover
            address:
               name:Institut für Toxikologie, Medizinische Hochschlule Hannover, Hannover, Germany
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Institut für Toxikologie, Medizinische Hochschlule Hannover, Hannover, Germany
      name:Institut für Toxikologie, Medizinische Hochschlule Hannover, Hannover, Germany
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(469)

Analytics and Tracking {📊}

  • Google Tag Manager

Libraries {📚}

  • Clipboard.js

CDN Services {📦}

  • Pbgrd

5.71s.