We are analyzing https://link.springer.com/protocol/10.1007/978-1-59745-157-4_4.

Title:
LC3 and Autophagy | SpringerLink
Description:
Microtubule-associated protein 1A/1B-light chain 3 (LC3) is a soluble protein with a molecular mass of ∼17 kDa that is distributed ubiquitously in mammalian tissues and cultured cells. During autophagy, autophagosomes engulf cytoplasmic components,...
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 5,000,019 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 Link.springer.com Make Money? {💸}

We don't see any clear sign of profit-making.

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. Link.springer.com might be plotting its profit, but the way they're doing it isn't detectable yet.

Keywords {🔍}

google, scholar, cas, pubmed, autophagy, article, ueno, tanida, kominami, mammalian, biol, cells, cell, chem, privacy, cookies, content, including, information, publish, protocol, molecular, autophagic, search, autophagosome, lcii, access, gabarap, gate, data, log, journal, research, phagosome, methods, cytosolic, form, autophagosomal, membranes, lysosomal, immunofluorescence, protocols, chapter, deretic, apgp, human, enzyme, press, springer, optional,

Topics {✒️}

leupeptin-administered rat liver springer science+business media human apg3p/aut1p homologue describe basic protocols including cytosolic proteins privacy choices/manage cookies form lc3-phosphatidylethanolamine conjugate intra-autophagosomal components microtubule binding subunit protein-activating enzyme late autophagic vacuoles humana press authentic e2 enzyme autophagosomal membrane depending form-ii formation journal finder publish european economic area nervous system diseases host defence mechanism saccharomyces cerevisiae apg7p endoplasmic reticulum preserved betaine homocysteine methyltransferase limited degradation fragment inhibiting tyrosine hydroxylase endogenous lc3-ii conditions privacy policy phagosome isei tanida mammalian atg8 modifiers mycobacterium tuberculosis inhibition lc3-positive structures autophagy-related processes autophagy generate sites accepting optional cookies juntendo university school main content log lc3 conjugation system light chain 3 multiple substrates autophagosomal membranes autophagic vacuoles check access ethics access journal publish mammalian cells lc3-ii cytosolic form chapter log protocol tanida monitoring autophagy privacy policy

Schema {🗺️}

ScholarlyArticle:
      headline:LC3 and Autophagy
      pageEnd:88
      pageStart:77
      image:https://media.springernature.com/w153/springer-static/cover/book/978-1-59745-157-4.jpg
      genre:
         Springer Protocols
      isPartOf:
         name:Autophagosome and Phagosome
         isbn:
            978-1-59745-157-4
            978-1-58829-853-9
         type:Book
      publisher:
         name:Humana Press
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Isei Tanida
            affiliation:
                  name:Juntendo University School of Medicine
                  address:
                     name:Department of Biochemistry, Juntendo University School of Medicine, Bunkyo-ku, Japan
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Takashi Ueno
            affiliation:
                  name:Juntendo University School of Medicine
                  address:
                     name:Department of Biochemistry, Juntendo University School of Medicine, Bunkyo-ku, Japan
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Eiki Kominami
            affiliation:
                  name:Juntendo University School of Medicine
                  address:
                     name:Department of Biochemistry, Juntendo University School of Medicine, Bunkyo-ku, Japan
                     type:PostalAddress
                  type:Organization
            type:Person
      keywords:LC3, lipidation, ubiquitylation-like reaction, autophagosome, autolysosome, autophagy, ATG conjugation system
      description:Microtubule-associated protein 1A/1B-light chain 3 (LC3) is a soluble protein with a molecular mass of ∼17 kDa that is distributed ubiquitously in mammalian tissues and cultured cells. During autophagy, autophagosomes engulf cytoplasmic components, including cytosolic proteins and organelles. Concomitantly, a cytosolic form of LC3 (LC3-I) is conjugated to phosphatidylethanolamine to form LC3-phosphatidylethanolamine conjugate (LC3-II), which is recruited to autophagosomal membranes. Autophagosomes fuse with lysosomes to form autolysosomes, and intra-autophagosomal components are degraded by lysosomal hydrolases. At the same time, LC3-II in autolysosomal lumen is degraded. Thus, lysosomal turnover of the autophagosomal marker LC3-II reflects starvation-induced autophagic activity, and detecting LC3 by immunoblotting or immunofluorescence has become a reliable method for monitoring autophagy and autophagy-related processes, including autophagic cell death. Here we describe basic protocols to assay for endogenous LC3-II by immunoblotting, immunoprecipitation, and immunofluorescence.
      datePublished:2008
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
      context:https://schema.org
Book:
      name:Autophagosome and Phagosome
      isbn:
         978-1-59745-157-4
         978-1-58829-853-9
Organization:
      name:Humana Press
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Juntendo University School of Medicine
      address:
         name:Department of Biochemistry, Juntendo University School of Medicine, Bunkyo-ku, Japan
         type:PostalAddress
      name:Juntendo University School of Medicine
      address:
         name:Department of Biochemistry, Juntendo University School of Medicine, Bunkyo-ku, Japan
         type:PostalAddress
      name:Juntendo University School of Medicine
      address:
         name:Department of Biochemistry, Juntendo University School of Medicine, Bunkyo-ku, Japan
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Isei Tanida
      affiliation:
            name:Juntendo University School of Medicine
            address:
               name:Department of Biochemistry, Juntendo University School of Medicine, Bunkyo-ku, Japan
               type:PostalAddress
            type:Organization
      name:Takashi Ueno
      affiliation:
            name:Juntendo University School of Medicine
            address:
               name:Department of Biochemistry, Juntendo University School of Medicine, Bunkyo-ku, Japan
               type:PostalAddress
            type:Organization
      name:Eiki Kominami
      affiliation:
            name:Juntendo University School of Medicine
            address:
               name:Department of Biochemistry, Juntendo University School of Medicine, Bunkyo-ku, Japan
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Department of Biochemistry, Juntendo University School of Medicine, Bunkyo-ku, Japan
      name:Department of Biochemistry, Juntendo University School of Medicine, Bunkyo-ku, Japan
      name:Department of Biochemistry, Juntendo University School of Medicine, Bunkyo-ku, Japan
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(84)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js

4.57s.

LINK . SPRINGER . COM {}