We are analyzing https://link.springer.com/protocol/10.1007/978-1-61779-474-2_15.

Title:
Synthesis and Analysis of K11-Linked Ubiquitin Chains | SpringerLink
Description:
Much has been learned about protein ubiquitination by studying the structural, biochemical, and biophysical properties of ubiquitin chains in vitro. However, these analyses were limited to K48-, K63-linked, and linear ubiquitin chains. Only recently, enzymatic and...
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Keywords {🔍}

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Topics {✒️}

month download article/chapter k11-linked ubiquitin chains human anaphase-promoting complex c-terminal diglycine motif ubiquitin family modifiers privacy choices/manage cookies device instant download linear ubiquitin chains unconventional ubiquitin chains building ubiquitin chains editor information editors promote mitotic exit humana press lys63-linked polyubiquitin journal finder publish ubiquitin-chain formation intrinsic k11-specificity european economic area chemical assembly systems remaining chain types track lysine-48 ubiquitination conditions privacy policy e2 enzyme ube2s physiological e2 module accepting optional cookies protocol bremm quantitative proteomics reveals david komander ubiquitin chains main content log online author correspondence check access ethics access journal publish protocol usd 49 social media permissions reprints k63-linked chapter log protein ubiquitination protocol cite privacy policy ubiquitin system unanchored ubiquitin biol chem 283 books a mol cell 33 mol cell 29 optional cookies

Schema {🗺️}

ScholarlyArticle:
      headline:Synthesis and Analysis of K11-Linked Ubiquitin Chains
      pageEnd:228
      pageStart:219
      image:https://media.springernature.com/w153/springer-static/cover/book/978-1-61779-474-2.jpg
      genre:
         Springer Protocols
      isPartOf:
         name:Ubiquitin Family Modifiers and the Proteasome
         isbn:
            978-1-61779-474-2
            978-1-61779-473-5
         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:Anja Bremm
            affiliation:
                  name:MRC Laboratory of Molecular Biology
                  address:
                     name:Protein and Nucleic Acid Chemistry Division, MRC Laboratory of Molecular Biology, Cambridge, UK
                     type:PostalAddress
                  type:Organization
            type:Person
            name:David Komander
            affiliation:
                  name:MRC Laboratory of Molecular Biology
                  address:
                     name:Protein and Nucleic Acid Chemistry Division, MRC Laboratory of Molecular Biology, Cambridge, UK
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      keywords:Ubiquitin, K11 linkage, Atypical ubiquitin chains, UBE2S
      description:Much has been learned about protein ubiquitination by studying the structural, biochemical, and biophysical properties of ubiquitin chains in vitro. However, these analyses were limited to K48-, K63-linked, and linear ubiquitin chains. Only recently, enzymatic and chemical assembly systems for the remaining chain types have been developed. Here, we describe a method to synthesise K11-linked ubiquitin chains in vitro by exploiting the intrinsic K11-specificity of the E2 enzyme UBE2S.
      datePublished:2012
      isAccessibleForFree:
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         cssSelector:.main-content
         type:WebPageElement
      context:https://schema.org
Book:
      name:Ubiquitin Family Modifiers and the Proteasome
      isbn:
         978-1-61779-474-2
         978-1-61779-473-5
Organization:
      name:Humana Press
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:MRC Laboratory of Molecular Biology
      address:
         name:Protein and Nucleic Acid Chemistry Division, MRC Laboratory of Molecular Biology, Cambridge, UK
         type:PostalAddress
      name:MRC Laboratory of Molecular Biology
      address:
         name:Protein and Nucleic Acid Chemistry Division, MRC Laboratory of Molecular Biology, Cambridge, UK
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Anja Bremm
      affiliation:
            name:MRC Laboratory of Molecular Biology
            address:
               name:Protein and Nucleic Acid Chemistry Division, MRC Laboratory of Molecular Biology, Cambridge, UK
               type:PostalAddress
            type:Organization
      name:David Komander
      affiliation:
            name:MRC Laboratory of Molecular Biology
            address:
               name:Protein and Nucleic Acid Chemistry Division, MRC Laboratory of Molecular Biology, Cambridge, UK
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Protein and Nucleic Acid Chemistry Division, MRC Laboratory of Molecular Biology, Cambridge, UK
      name:Protein and Nucleic Acid Chemistry Division, MRC Laboratory of Molecular Biology, Cambridge, UK
WebPageElement:
      isAccessibleForFree:
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