We are analyzing https://link.springer.com/article/10.1007/s00018-008-8072-8.

Title:
UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97 | Cellular and Molecular Life Sciences
Description:
The highly conserved AAA ATPase Cdc48/p97 acts on ubiquitylated substrate proteins in cellular processes as diverse as the fusion of homotypic membranes and the degradation of misfolded proteins. The ‘Ubiquitin regulatory X’ (UBX) domain-containing proteins constitute the so far largest family of Cdc48/p97 cofactors. UBX proteins are involved in substrate recruitment to Cdc48/p97 and in the temporal and spatial regulation of its activity. In combination with UBX-like proteins and other cofactors, they can assemble into a large variety of Cdc48/p97-cofactor complexes possessing distinct cellular functions. This review gives an overview of the different subfamilies of UBX proteins and their functions, and discusses general principles of Cdc48/p97 regulation by these cofactors.
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Keywords {🔍}

article, proteins, access, ubx, cdcp, open, privacy, cookies, atpase, content, information, publish, search, cellular, domain, aaa, schuberth, buchberger, protein, data, journal, research, molecular, life, regulators, download, ubiquitin, cofactors, discover, authors, cell, optional, personal, parties, policy, find, track, sciences, major, review, published, april, cite, pdf, full, manuscript, explore, ubiquitylated, substrate, degradation,

Topics {✒️}

aaa atpase cdc48/p97 ubiquitylated substrate proteins aaa atpase valosin molecular cell biology ubx domain proteins cdc48/p97 regulation related subjects article download pdf cdc48/p97 cofactors protein complexes authors correspondence privacy choices/manage cookies cdc48 atpase cdc48/p97 �ubiquitin regulatory original author ubx proteins major regulators full access european economic area discusses general principles max planck institute misfolded proteins proteins constitute conditions privacy policy accepting optional cookies scope submit manuscript journal finder publish protein 1007/s00018-008-8072-8 keywords proteins ubx domain cellular processes article cite article schuberth search search life sci cell information vcp privacy policy personal data books a optional cookies manage preferences data protection essential cookies cookies skip degradation substrate recruitment

Schema {🗺️}

WebPage:
      mainEntity:
         headline:UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97
         description:The highly conserved AAA ATPase Cdc48/p97 acts on ubiquitylated substrate proteins in cellular processes as diverse as the fusion of homotypic membranes and the degradation of misfolded proteins. The ‘Ubiquitin regulatory X’ (UBX) domain-containing proteins constitute the so far largest family of Cdc48/p97 cofactors. UBX proteins are involved in substrate recruitment to Cdc48/p97 and in the temporal and spatial regulation of its activity. In combination with UBX-like proteins and other cofactors, they can assemble into a large variety of Cdc48/p97-cofactor complexes possessing distinct cellular functions. This review gives an overview of the different subfamilies of UBX proteins and their functions, and discusses general principles of Cdc48/p97 regulation by these cofactors.
         datePublished:2008-04-26T00:00:00Z
         dateModified:2008-04-26T00:00:00Z
         pageStart:2360
         pageEnd:2371
         license:https://creativecommons.org/licenses/by-nc/2.0
         sameAs:https://doi.org/10.1007/s00018-008-8072-8
         keywords:
            AAA ATPase
            valosin-containing protein (VCP)
            ubiquitin/proteasome system
            protein degradation
            UBA domain
            ubiquitin-like fold
            Cell Biology
            Biomedicine
            general
            Life Sciences
            Biochemistry
         image:
         isPartOf:
            name:Cellular and Molecular Life Sciences
            issn:
               1420-9071
               1420-682X
            volumeNumber:65
            type:
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         publisher:
            name:SP Birkhäuser Verlag Basel
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:C. Schuberth
               affiliation:
                     name:EMBL Heidelberg
                     address:
                        name:Cell Biology and Biophysics Unit, EMBL Heidelberg, Heidelberg, Germany
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
               name:A. Buchberger
               affiliation:
                     name:Max Planck Institute of Biochemistry
                     address:
                        name:Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Martinsried, Germany
                        type:PostalAddress
                     type:Organization
               email:[email protected]
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ScholarlyArticle:
      headline:UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97
      description:The highly conserved AAA ATPase Cdc48/p97 acts on ubiquitylated substrate proteins in cellular processes as diverse as the fusion of homotypic membranes and the degradation of misfolded proteins. The ‘Ubiquitin regulatory X’ (UBX) domain-containing proteins constitute the so far largest family of Cdc48/p97 cofactors. UBX proteins are involved in substrate recruitment to Cdc48/p97 and in the temporal and spatial regulation of its activity. In combination with UBX-like proteins and other cofactors, they can assemble into a large variety of Cdc48/p97-cofactor complexes possessing distinct cellular functions. This review gives an overview of the different subfamilies of UBX proteins and their functions, and discusses general principles of Cdc48/p97 regulation by these cofactors.
      datePublished:2008-04-26T00:00:00Z
      dateModified:2008-04-26T00:00:00Z
      pageStart:2360
      pageEnd:2371
      license:https://creativecommons.org/licenses/by-nc/2.0
      sameAs:https://doi.org/10.1007/s00018-008-8072-8
      keywords:
         AAA ATPase
         valosin-containing protein (VCP)
         ubiquitin/proteasome system
         protein degradation
         UBA domain
         ubiquitin-like fold
         Cell Biology
         Biomedicine
         general
         Life Sciences
         Biochemistry
      image:
      isPartOf:
         name:Cellular and Molecular Life Sciences
         issn:
            1420-9071
            1420-682X
         volumeNumber:65
         type:
            Periodical
            PublicationVolume
      publisher:
         name:SP Birkhäuser Verlag Basel
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:C. Schuberth
            affiliation:
                  name:EMBL Heidelberg
                  address:
                     name:Cell Biology and Biophysics Unit, EMBL Heidelberg, Heidelberg, Germany
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
            name:A. Buchberger
            affiliation:
                  name:Max Planck Institute of Biochemistry
                  address:
                     name:Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Martinsried, Germany
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      isAccessibleForFree:1
["Periodical","PublicationVolume"]:
      name:Cellular and Molecular Life Sciences
      issn:
         1420-9071
         1420-682X
      volumeNumber:65
Organization:
      name:SP Birkhäuser Verlag Basel
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:EMBL Heidelberg
      address:
         name:Cell Biology and Biophysics Unit, EMBL Heidelberg, Heidelberg, Germany
         type:PostalAddress
      name:Max Planck Institute of Biochemistry
      address:
         name:Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Martinsried, Germany
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:C. Schuberth
      affiliation:
            name:EMBL Heidelberg
            address:
               name:Cell Biology and Biophysics Unit, EMBL Heidelberg, Heidelberg, Germany
               type:PostalAddress
            type:Organization
      email:[email protected]
      name:A. Buchberger
      affiliation:
            name:Max Planck Institute of Biochemistry
            address:
               name:Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Martinsried, Germany
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Cell Biology and Biophysics Unit, EMBL Heidelberg, Heidelberg, Germany
      name:Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Martinsried, Germany

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