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  1. Analyzed Page
  2. Matching Content Categories
  3. CMS
  4. Monthly Traffic Estimate
  5. How Does Doi.org Make Money
  6. Keywords
  7. Topics
  8. Questions
  9. Social Networks
  10. External Links
  11. Analytics And Tracking
  12. Libraries
  13. Hosting Providers
  14. CDN Services

We began analyzing https://www.molbiolcell.org/doi/10.1091/mbc.e02-05-0311, but it redirected us to https://www.molbiolcell.org/doi/10.1091/mbc.e02-05-0311. The analysis below is for the second page.

Title[redir]:
A Subset of Chaperones and Folding Enzymes Form Multiprotein Complexes in Endoplasmic Reticulum to Bind Nascent Proteins | Molecular Biology of the Cell
Description:
We demonstrate the existence of a large endoplasmic reticulum (ER)-localized multiprotein complex that is comprised of the molecular chaperones BiP; GRP94; CaBP1; protein disulfide isomerase (PDI); ERdj3, a recently identified ER Hsp40 cochaperone; cyclophilin B; ERp72; GRP170; UDP-glucosyltransferase; and SDF2-L1. This complex is associated with unassembled, incompletely folded immunoglobulin heavy chains. Except for ERdj3, and to a lesser extent PDI, this complex also forms in the absence of nascent protein synthesis and is found in a variety of cell types. Cross-linking studies reveal that the majority of these chaperones are included in the complex. Our data suggest that this subset of ER chaperones forms an ER network that can bind to unfolded protein substrates instead of existing as free pools that assembled onto substrate proteins. It is noticeable that most of the components of the calnexin/calreticulin system, which include some of the most abundant chaperones inside the ER, are either not detected in this complex or only very poorly represented. This study demonstrates an organization of ER chaperones and folding enzymes that has not been previously appreciated and suggests a spatial separation of the two chaperone systems that may account for the temporal interactions observed in other studies.

Matching Content Categories {📚}

  • Science
  • Health & Fitness
  • Education

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 93,436,998 visitors per month in the current month.

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How Does Doi.org Make Money? {💸}

We can't figure out the monetization strategy.

Not all websites are made for profit; some exist to inform or educate users. Or any other reason why people make websites. And this might be the case. Doi.org could be getting rich in stealth mode, or the way it's monetizing isn't detectable.

Keywords {🔍}

vol, protein, cell, proteins, endoplasmic, reticulum, heavy, journal, cells, complex, molecular, biology, chaperones, bip, chains, folding, chaperone, google, scholar, grp, medline, control, stress, complexes, hsp, unfolded, crossref, disulfide, chain, biological, isomerase, jan, quality, erp, binding, analysis, research, chemistry, response, human, crosslinking, biol, present, treated, figure, dsp, kda, immunoglobulin, asepharose, erdj,

Topics {✒️}

special issue protein disulphide-isomerase-deficient microsomes ascb privacy policy thiol-cleavable cross-linker dithiobis adp-ribose-binding macro domains ascb contact sars-cov-2 rbd mutations small thiol-reactive cross-linker mboc info glycoprotein glucosyltransferase-glucosidase ii er peptidyl-prolyl-isomerase high-molecular-weight complexes exist gpi-attachment signals affect thiol–disulfide exchange reactions disulfide-bonded protein products protein-disulfide isomerase facilitates pmt/rt protein family er stress-inducible protein endoplasmic reticulum stress-response lhs1/grp170 chaperones facilitate high-molecular-weight markers hedj/erdj3 cysteine-rich domain bip–grp94-based chaperone system twisting inter-domain motions authors subscription rates quantitative lc‐ms/ms mboc 10 er-stress-induced secretion b-cell antigen receptors goat anti-rabbit ig escherichia coli dnaj thiol-cleavable cross-linker individual folding resources protein a-sepharose beads pattern-recognition receptor efr unusual redox-inactive member collagen post-translational modification goat anti-mouse ig erecta-family receptor kinases n-glycan-dependent determination protein covered udp-glucosyltransferase monoglucosylated n-linked glycans nucleotide exchange factor boca/mesd maturation factors high-molecular-weight complexes hetero-oligomeric ig proteins high-molecular-weight complex er resident j-proteins chaperone/folding catalyst complexes peptidyl-prolyl isomerases

Questions {❓}

  • Can't sign in?
  • Engineering mammalian cell factories for improved recombinant monoclonal antibody production: lessons from nature?
  • Roles of Heat Shock Protein gp96 in the ER Quality Control: Redundant or Unique Function?
  • The endoplasmic reticulum protein folding factory and its chaperones: new targets for drug discovery?
  • Three branches to rule them all?
  • What is a co-chaperone?

Social Networks {👍}(2)

External Links {🔗}(418)

Analytics and Tracking {📊}

  • Google Analytics
  • Google Analytics 4
  • Google Tag Manager
  • Google Universal Analytics

Libraries {📚}

  • AOS
  • Dropzone.js
  • Video.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 {📦}

  • Pbgrd

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