DOI . ORG {}

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We began analyzing https://link.springer.com/protocol/10.1007/978-1-59745-157-4_4, but it redirected us to https://link.springer.com/protocol/10.1007/978-1-59745-157-4_4. The analysis below is for the second page.

Title[redir]:
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,...

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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:
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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
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      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:
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