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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. Schema
  9. External Links
  10. Analytics And Tracking
  11. Libraries
  12. CDN Services

We are analyzing https://link.springer.com/chapter/10.1007/978-3-030-84965-8_10.

Title:
Redox Proteostasis in Subcellular Aging | SpringerLink
Description:
Aging is a process which leads to gradual redox status deterioration at the subcellular level. Proteostasis is a dynamic event that regulates protein’s redox status within the aging process to maintain redox stability of proteome. Proteostasis also includes the...
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Education
  • Health & Fitness
  • 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 5,000,019 visitors per month in the current month.
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How Does Link.springer.com Make Money? {💸}

We find it hard to spot revenue streams.

Websites don't always need to be profitable; some serve as platforms for education or personal expression. Websites can serve multiple purposes. And this might be one of them. Link.springer.com might have a hidden revenue stream, but it's not something we can detect.

Keywords {🔍}

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Topics {✒️}

nonenzymatic post-translational modifications month download article/chapter proteasome-autophagy systems possess streptozotocin-induced sporadic alzheimer endoplasmic reticulum-mitochondrial axis degenerated mitochondria-er contacts produce reactive oxygen species mitochondria-endoplasmic reticulum contacts aging-related impaired redoxtasis protein redox-regulation mechanisms aging-induced proteinopathies de paz ja privacy choices/manage cookies jean beltran pm device instant download membrane contact sites post-mitotic tissues chapter redox signaling misfolded protein aggregates reactive oxygen species central implication impaired cellular redoxtasis ubiquitin–proteasome system heath s-hd aged mouse livers aged mouse liver editor information editors decreased enzyme activities oxidative protein damage endoplasmic reticulum stress misfolded protein accumulation declined antioxidant status mitochondrial permeability transition european economic area establish promising therapies virus-host interface silva-palacios boylston wh 3rd commercially insured population mild cognitive impairment ca2+ cross-talk protein-folding diseases mitochondria-er contact aging-related factors protein misfolding endoplasmic reticulum membranes age-related disorders age-related diseases maintain redox stability conditions privacy policy

Schema {🗺️}

ScholarlyArticle:
      headline:Redox Proteostasis in Subcellular Aging
      pageEnd:228
      pageStart:209
      image:https://media.springernature.com/w153/springer-static/cover/book/978-3-030-84965-8.jpg
      genre:
         Biomedical and Life Sciences
         Biomedical and Life Sciences (R0)
      isPartOf:
         name:Redox Signaling and Biomarkers in Ageing
         isbn:
            978-3-030-84965-8
            978-3-030-84964-1
         type:Book
      publisher:
         name:Springer International Publishing
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Mehmet Can Atayik
            affiliation:
                  name:Istanbul University-Cerrahpasa
                  address:
                     name:Medical Program, Cerrahpasa Faculty of Medicine, Istanbul University-Cerrahpasa, Istanbul, Turkey
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Karolin Yanar
            affiliation:
                  name:Istanbul University-Cerrahpasa
                  address:
                     name:Department of Medical Biochemistry, Cerrahpasa Faculty of Medicine, Istanbul University-Cerrahpasa, Istanbul, Turkey
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Ufuk Çakatay
            affiliation:
                  name:Istanbul University-Cerrahpasa
                  address:
                     name:Department of Medical Biochemistry, Cerrahpasa Faculty of Medicine, Istanbul University-Cerrahpasa, Istanbul, Turkey
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      keywords:Aging, Redoxtasis, Proteostasis, Protein misfolding, Proteasome autophagy, Ubiquitin–proteasome system
      description:Aging is a process which leads to gradual redox status deterioration at the subcellular level. Proteostasis is a dynamic event that regulates protein’s redox status within the aging process to maintain redox stability of proteome. Proteostasis also includes the highly complex redox regulatory signaling pathways that affect various functions in the aging cell. At the subcellular level, other cellular organelles besides mitochondria, such as lysosomes, peroxisomes, and endoplasmic reticulum (ER), also produce reactive oxygen species (ROS) that contribute to proteomic aging. The optimum stability and function of proteome may be deteriorated by many aging-related factors such as impaired cellular redoxtasis, nonenzymatic post-translational modifications, and ER stress. Misfolded protein accumulation in the ER lumen interferes signal transduction-related events. Proteasome-autophagy systems possess the removal activity for oxidatively modified proteins and aging organelles. The ubiquitin–proteasome system is major intracellular protein degradation system that controls the garbage recycle process in the aging proteome. Aging-related impaired redoxtasis may cause nonenzymatic post-translational modification- related proteinopathies. The gradual accumulation of oxidatively modified and misfolded protein aggregates is the main characteristics of proteinopathies. Aging-induced interorganellar redox imbalance, impaired oxidative garbage removal, and deposition of modified proteins like amyloid β, tau proteins, α-synuclein, and amyloid polypeptides are all related to age-related protein misfolding diseases. Thus, in the long term, novel antiaging and senolytic strategies to restore proteostasis in aging proteome may provide an effective way to establish promising therapies for Alzheimer’s disease and other aging-induced protein misfolding diseases.
      datePublished:2022
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         type:WebPageElement
      context:https://schema.org
Book:
      name:Redox Signaling and Biomarkers in Ageing
      isbn:
         978-3-030-84965-8
         978-3-030-84964-1
Organization:
      name:Springer International Publishing
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Istanbul University-Cerrahpasa
      address:
         name:Medical Program, Cerrahpasa Faculty of Medicine, Istanbul University-Cerrahpasa, Istanbul, Turkey
         type:PostalAddress
      name:Istanbul University-Cerrahpasa
      address:
         name:Department of Medical Biochemistry, Cerrahpasa Faculty of Medicine, Istanbul University-Cerrahpasa, Istanbul, Turkey
         type:PostalAddress
      name:Istanbul University-Cerrahpasa
      address:
         name:Department of Medical Biochemistry, Cerrahpasa Faculty of Medicine, Istanbul University-Cerrahpasa, Istanbul, Turkey
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Mehmet Can Atayik
      affiliation:
            name:Istanbul University-Cerrahpasa
            address:
               name:Medical Program, Cerrahpasa Faculty of Medicine, Istanbul University-Cerrahpasa, Istanbul, Turkey
               type:PostalAddress
            type:Organization
      name:Karolin Yanar
      affiliation:
            name:Istanbul University-Cerrahpasa
            address:
               name:Department of Medical Biochemistry, Cerrahpasa Faculty of Medicine, Istanbul University-Cerrahpasa, Istanbul, Turkey
               type:PostalAddress
            type:Organization
      name:Ufuk Çakatay
      affiliation:
            name:Istanbul University-Cerrahpasa
            address:
               name:Department of Medical Biochemistry, Cerrahpasa Faculty of Medicine, Istanbul University-Cerrahpasa, Istanbul, Turkey
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Medical Program, Cerrahpasa Faculty of Medicine, Istanbul University-Cerrahpasa, Istanbul, Turkey
      name:Department of Medical Biochemistry, Cerrahpasa Faculty of Medicine, Istanbul University-Cerrahpasa, Istanbul, Turkey
      name:Department of Medical Biochemistry, Cerrahpasa Faculty of Medicine, Istanbul University-Cerrahpasa, Istanbul, Turkey
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(216)

Analytics and Tracking {📊}

  • Google Tag Manager

Libraries {📚}

  • Clipboard.js

CDN Services {📦}

  • Pbgrd

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