DOI . ORG {}

Analyzed Page
Matching Content Categories
CMS
Monthly Traffic Estimate
How Does Doi.org Make Money
Keywords
Topics
Questions
Schema
Social Networks
External Links
Analytics And Tracking
Libraries
Hosting Providers
CDN Services

We began analyzing https://www.nature.com/articles/nrneph.2017.129, but it redirected us to https://www.nature.com/articles/nrneph.2017.129. The analysis below is for the second page.

Title[redir]:
Endoplasmic reticulum stress, the unfolded protein response and autophagy in kidney diseases | Nature Reviews Nephrology
Description:
Our understanding of endoplasmic reticulum (ER) stress, the unfolded protein response (UPR) and ER stress-induced autophagy in the kidney has increased — using the presence of ER chaperones in the urine as a biomarker of renal ER stress, and using pharmacological agents that improve protein folding or induce the expression of chaperones, may aid in the diagnosis and treatment of kidney disease, respectively. Progress has been made in our understanding of the mechanisms of endoplasmic reticulum (ER) proteostasis, ER stress and the unfolded protein response (UPR), as well as ER stress-induced autophagy, in the kidney. Experimental models have revealed that disruption of the UPR, including a protein that senses misfolded proteins (namely, inositol-requiring enzyme 1α) in mouse podocytes causes podocyte injury and albuminuria as mice age. Protein misfolding and ER stress are evident in various renal diseases, including primary glomerulonephritides, glomerulopathies associated with genetic mutations, diabetic nephropathy, acute kidney injury, chronic kidney disease and renal fibrosis. The induction of ER stress may be cytoprotective, or it may be cytotoxic by activating apoptosis. The UPR may interact in a coordinated manner with autophagy to alleviate protein misfolding and its consequences. Monitoring the excretion of ER chaperones into the urine can potentially serve as a biomarker of renal ER stress. In specific kidney diseases, the treatment of experimental animals with chemical chaperones that improve protein folding or with chaperone inducers has alleviated kidney injury. Given the limited availability of mechanism-based therapies for kidney diseases, normalization of ER stress using pharmacological agents represents a promising therapeutic approach towards preventing or arresting the progression of kidney disease.

Matching Content Categories {📚}

Health & Fitness
Education
Fitness & Wellness

Content Management System {📝}

What CMS is doi.org built with?

Custom-built

No common CMS systems were detected on Doi.org, and no known web development framework was identified.

Traffic Estimate {📈}

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

🏙️ Massive Traffic: 50M - 100M visitors per month

Based on our best estimate, this website will receive around 80,473,390 visitors per month in the current month.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Doi.org Make Money? {💸}

We can't figure out the monetization strategy.

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 revenue plan, but it's either invisible or we haven't found it.

Keywords {🔍}

pubmed, article, google, scholar, cas, stress, endoplasmic, reticulum, kidney, central, autophagy, protein, cell, injury, renal, nephrol, response, disease, nature, biol, physiol, unfolded, nephropathy, diabetic, role, diseases, glomerular, soc, cybulsky, podocytes, acute, nat, podocyte, mice, access, chem, rev, med, apoptosis, mol, plos, ischemic, function, cells, sci, development, proteostasis, fibrosis, therapeutic, stressinduced,

Topics {✒️}

nature portfolio journals permissions reprints nature portfolio privacy policy advertising health research akt/gsk3-beta signaling pathway social media national library research grants hyperglycemia-induced podocyte injury nature+ nature 454 nature 467 nature set7/9-induced histone methylation inositol-requiring enzyme 1α inositol-requiring enzyme-1α dahl salt-sensitive rat complement-mediated glomerular injury n-linked glycosylation sites lead-induced oxidative stress protein-tyrosine phosphatase 1b gov/ct2/show/nct02343094 er stress-induced autophagy albumin overload-induced nephropathy ameliorate protein-folding diseases x-box binding protein-1 personal data ischemia-reperfusion injury author information authors permissions attenuates kidney injury erse-ii element hypoxic conditions stimulate endoplasmic reticulum stress endoplasmic-reticulum stress prevent neurodegeneration nf-κb-mediated inflammation α-actinin-4-mediated fsgs springerlink instant access data protection acute ischemic injury renal tubular injury glomerular basement membrane inhibits cell proliferation acute kidney injury transcription factor xbp-1 impairs cytoskeletal dynamics chop/gadd153 repression

Questions {❓}

Stress in the kidney is the road to pERdition: is endoplasmic reticulum stress a pathogenic mediator of diabetic nephropathy?
Gov/ct2/show/NCT02343094?

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Endoplasmic reticulum stress, the unfolded protein response and autophagy in kidney diseases
         description: Our understanding of endoplasmic reticulum (ER) stress, the unfolded protein response (UPR) and ER stress-induced autophagy in the kidney has increased â using the presence of ER chaperones in the urine as a biomarker of renal ER stress, and using pharmacological agents that improve protein folding or induce the expression of chaperones, may aid in the diagnosis and treatment of kidney disease, respectively. Progress has been made in our understanding of the mechanisms of endoplasmic reticulum (ER) proteostasis, ER stress and the unfolded protein response (UPR), as well as ER stress-induced autophagy, in the kidney. Experimental models have revealed that disruption of the UPR, including a protein that senses misfolded proteins (namely, inositol-requiring enzyme 1Î±) in mouse podocytes causes podocyte injury and albuminuria as mice age. Protein misfolding and ER stress are evident in various renal diseases, including primary glomerulonephritides, glomerulopathies associated with genetic mutations, diabetic nephropathy, acute kidney injury, chronic kidney disease and renal fibrosis. The induction of ER stress may be cytoprotective, or it may be cytotoxic by activating apoptosis. The UPR may interact in a coordinated manner with autophagy to alleviate protein misfolding and its consequences. Monitoring the excretion of ER chaperones into the urine can potentially serve as a biomarker of renal ER stress. In specific kidney diseases, the treatment of experimental animals with chemical chaperones that improve protein folding or with chaperone inducers has alleviated kidney injury. Given the limited availability of mechanism-based therapies for kidney diseases, normalization of ER stress using pharmacological agents represents a promising therapeutic approach towards preventing or arresting the progression of kidney disease.
         datePublished:2017-10-03T00:00:00Z
         dateModified:2017-10-03T00:00:00Z
         pageStart:681
         pageEnd:696
         sameAs:https://doi.org/10.1038/nrneph.2017.129
         keywords:
            Diagnostic markers
            Endoplasmic reticulum
            Kidney diseases
            Macroautophagy
            Medicine/Public Health
            general
            Nephrology
         image:
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrneph.2017.129/MediaObjects/41581_2017_Article_BFnrneph2017129_Fig1_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrneph.2017.129/MediaObjects/41581_2017_Article_BFnrneph2017129_Fig2_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrneph.2017.129/MediaObjects/41581_2017_Article_BFnrneph2017129_Fig3_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrneph.2017.129/MediaObjects/41581_2017_Article_BFnrneph2017129_Fig4_HTML.jpg
         isPartOf:
            name:Nature Reviews Nephrology
            issn:
               1759-507X
               1759-5061
            volumeNumber:13
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Nature Publishing Group UK
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Andrey V. Cybulsky
               affiliation:
                     name:McGill University Health Centre Research Institute EM13238
                     address:
                        name:Division of Nephrology, Department of Medicine, McGill University Health Centre Research Institute EM13238, Montreal, Canada
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:Endoplasmic reticulum stress, the unfolded protein response and autophagy in kidney diseases
      description: Our understanding of endoplasmic reticulum (ER) stress, the unfolded protein response (UPR) and ER stress-induced autophagy in the kidney has increased â using the presence of ER chaperones in the urine as a biomarker of renal ER stress, and using pharmacological agents that improve protein folding or induce the expression of chaperones, may aid in the diagnosis and treatment of kidney disease, respectively. Progress has been made in our understanding of the mechanisms of endoplasmic reticulum (ER) proteostasis, ER stress and the unfolded protein response (UPR), as well as ER stress-induced autophagy, in the kidney. Experimental models have revealed that disruption of the UPR, including a protein that senses misfolded proteins (namely, inositol-requiring enzyme 1Î±) in mouse podocytes causes podocyte injury and albuminuria as mice age. Protein misfolding and ER stress are evident in various renal diseases, including primary glomerulonephritides, glomerulopathies associated with genetic mutations, diabetic nephropathy, acute kidney injury, chronic kidney disease and renal fibrosis. The induction of ER stress may be cytoprotective, or it may be cytotoxic by activating apoptosis. The UPR may interact in a coordinated manner with autophagy to alleviate protein misfolding and its consequences. Monitoring the excretion of ER chaperones into the urine can potentially serve as a biomarker of renal ER stress. In specific kidney diseases, the treatment of experimental animals with chemical chaperones that improve protein folding or with chaperone inducers has alleviated kidney injury. Given the limited availability of mechanism-based therapies for kidney diseases, normalization of ER stress using pharmacological agents represents a promising therapeutic approach towards preventing or arresting the progression of kidney disease.
      datePublished:2017-10-03T00:00:00Z
      dateModified:2017-10-03T00:00:00Z
      pageStart:681
      pageEnd:696
      sameAs:https://doi.org/10.1038/nrneph.2017.129
      keywords:
         Diagnostic markers
         Endoplasmic reticulum
         Kidney diseases
         Macroautophagy
         Medicine/Public Health
         general
         Nephrology
      image:
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrneph.2017.129/MediaObjects/41581_2017_Article_BFnrneph2017129_Fig1_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrneph.2017.129/MediaObjects/41581_2017_Article_BFnrneph2017129_Fig2_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrneph.2017.129/MediaObjects/41581_2017_Article_BFnrneph2017129_Fig3_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrneph.2017.129/MediaObjects/41581_2017_Article_BFnrneph2017129_Fig4_HTML.jpg
      isPartOf:
         name:Nature Reviews Nephrology
         issn:
            1759-507X
            1759-5061
         volumeNumber:13
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Nature Publishing Group UK
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Andrey V. Cybulsky
            affiliation:
                  name:McGill University Health Centre Research Institute EM13238
                  address:
                     name:Division of Nephrology, Department of Medicine, McGill University Health Centre Research Institute EM13238, Montreal, Canada
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Nature Reviews Nephrology
      issn:
         1759-507X
         1759-5061
      volumeNumber:13
Organization:
      name:Nature Publishing Group UK
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:McGill University Health Centre Research Institute EM13238
      address:
         name:Division of Nephrology, Department of Medicine, McGill University Health Centre Research Institute EM13238, Montreal, Canada
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Andrey V. Cybulsky
      affiliation:
            name:McGill University Health Centre Research Institute EM13238
            address:
               name:Division of Nephrology, Department of Medicine, McGill University Health Centre Research Institute EM13238, Montreal, Canada
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Division of Nephrology, Department of Medicine, McGill University Health Centre Research Institute EM13238, Montreal, Canada
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

Social Networks {👍}(2)

External Links {🔗}(653)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Prism.js
Zoom.js

Emails and Hosting {✉️}

Mail Servers:

mx.zoho.eu
mx2.zoho.eu
mx3.zoho.eu

Name Servers:

josh.ns.cloudflare.com
zita.ns.cloudflare.com

CDN Services {📦}

Crossref

6.5s.