FACULTYOPINIONS . COM {}

Analyzed Page
Matching Content Categories
CMS
Monthly Traffic Estimate
How Does Facultyopinions.com Make Money
Keywords
Topics
Schema
Social Networks
External Links
Analytics And Tracking
Hosting Providers

We began analyzing https://archive.connect.h1.co/article/1325996/, but it redirected us to https://archive.connect.h1.co/article/1325996/. The analysis below is for the second page.

Title[redir]:
Cyclophilin D modulates mitochondr ... | Article | H1 Connect
Description:
Blue native gel electrophoresis purification and immunoprecipitation of F(0)F(1)-ATP synthase from bovine heart mitochondria revealed that cyclophilin (CyP

Matching Content Categories {📚}

Science
Education
Health & Fitness

Content Management System {📝}

What CMS is facultyopinions.com built with?

Custom-built

No common CMS systems were detected on Facultyopinions.com, but we identified it was custom coded using Next.js (JavaScript).

Traffic Estimate {📈}

What is the average monthly size of facultyopinions.com audience?

🚗 Small Traffic: 1k - 5k visitors per month

Based on our best estimate, this website will receive around 1,019 visitors per month in the current month.
However, some sources were not loaded, we suggest to reload the page to get complete results.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Facultyopinions.com Make Money? {💸}

We can't figure out the monetization strategy.

Many websites are intended to earn money, but some serve to share ideas or build connections. Websites exist for all kinds of purposes. This might be one of them. Facultyopinions.com has a secret sauce for making money, but we can't detect it yet.

Keywords {🔍}

synthase, mitochondrial, latest, recommendation, atp, protein, finding, chemistry, proteomics, cypd, biocatalysis, subunit, jan, feb, confirmation, faculty, ffatp, complex, dec, regulation, membrane, biology, structure, apr, cyclophilin, interacting, stalk, biological, show, good, activity, csa, interest, role, permeability, transition, mptp, cell, death, processes, proteins, functional, complexes, folding, dynamics, assembly, ffoatp, technical, advance, jul,

Topics {✒️}

mitochondrial f1f0-atp synthase membrane protein biogenesis mitochondrial atp synthase f1fo-atp synthase atp synthase complex fo atp synthase mitochondrial permeability transition mitochondrial hsp70 controls biological chemistry van der laan atp synthase cyclic peptide interacting rigid cap structure normal biological processes subunit faculty opinions +-atpase/synthase mitochondrial atpase latest recommendation h1 company membrane proteins enzymatic activity finding evaluations authors show finding structure doctors search lateral stalk interaction results energy metabolism previous work functional complexes functionally incorporated electron cryomicroscopy rubinstein jl yidc pathway robert fillingame 06 cryo-em baker la peripheral stalk thermus thermophilus lee lk 10 blog faq privacy policy archived cyclophilin displaces cyp complex 2009 dec 04 role finding interacting

Schema {🗺️}

ScholarlyArticle:
      context:https://schema.org
      headline:Cyclophilin D modulates mitochondrial F0F1-ATP synthase by interacting with the lateral stalk of the complex.
      abstract:Blue native gel electrophoresis purification and immunoprecipitation of F(0)F(1)-ATP synthase from bovine heart mitochondria revealed that cyclophilin (CyP) D associates to the complex. Treatment of intact mitochondria with the membrane-permeable bifunctional reagent dimethyl 3,3-dithiobis-propionimidate (DTBP) cross-linked CyPD with the lateral stalk of ATP synthase, whereas no interactions with F(1) sector subunits, the ATP synthase natural inhibitor protein IF1, and the ATP/ADP carrier were observed. The ATP synthase-CyPD interactions have functional consequences on enzyme catalysis and are modulated by phosphate (increased CyPD binding and decreased enzyme activity) and cyclosporin (Cs) A (decreased CyPD binding and increased enzyme activity). Treatment of MgATP submitochondrial particles or intact mitochondria with CsA displaced CyPD from membranes and activated both hydrolysis and synthesis of ATP sustained by the enzyme. No effect of CsA was detected in CyPD-null mitochondria, which displayed a higher specific activity of the ATP synthase than wild-type mitochondria. Modulation by CyPD binding appears to be independent of IF1, whose association to ATP synthase was not affected by CsA treatment. These findings demonstrate that CyPD association to the lateral stalk of ATP synthase modulates the activity of the complex.
      hasPart:
         type:WebPageElement
         isAccessibleForFree:
         cssSelector:.paywalled-content
      isAccessibleForFree:
      mainEntityOfPage:
         type:WebPage
         id:https://connect.h1.co/article/1325996
WebPage:
      id:https://connect.h1.co/article/1325996

Social Networks {👍}(2)

External Links {🔗}(41)

Analytics and Tracking {📊}

Google Analytics
Google Tag Manager

Emails and Hosting {✉️}

Mail Servers:

aspmx.l.google.com
alt1.aspmx.l.google.com
alt2.aspmx.l.google.com
alt3.aspmx.l.google.com
alt4.aspmx.l.google.com

Name Servers:

ns-1466.awsdns-55.org
ns-15.awsdns-01.com
ns-1815.awsdns-34.co.uk
ns-887.awsdns-46.net

6.73s.