DOI . ORG {}

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We began analyzing https://link.springer.com/protocol/10.1007/978-1-4939-6993-7_9, but it redirected us to https://link.springer.com/protocol/10.1007/978-1-4939-6993-7_9. The analysis below is for the second page.

Title[redir]:
Identification of Protein Substrates of Specific PARP Enzymes Using Analog-Sensitive PARP Mutants and a “Clickable” NAD+ Analog | SpringerLink
Description:
The PARP family of ADP-ribosyl transferases contains 17 members in human cells, most of which catalyze the transfer of the ADP-ribose moiety of NAD+ onto their target proteins. This posttranslational modification plays important roles in cellular signaling,...

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Keywords {🔍}

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identifying family-member-specific targets month download article/chapter de murcia jm analog-sensitive parp mutants analog-sensitive parp approach analog-sensitive parp methodology adenosine diphosphate-ribosylated peptides family-wide chemical profiling glu-adp-ribosylated proteome identify site-specific modification �clickable” nad+ analog parp targets reveals parp-specific adp-ribosylation device instant download privacy choices/manage cookies muthurajan um editor information editors unfolded protein responses dna damage response specific amino acids chemical genetics approach adp-ribosylation mediated ida green center family-wide analysis generating protein-linked heterochromatin protein hp1alpha chromatin architectural protein site-specific characterization specific parp enzymes european economic area chemical genetic discovery isolated mammalian nuclei xenopus egg extracts journal finder publish conditions privacy policy accurate transcription initiation reproductive biology sciences core histone tails protein-free mono accepting optional cookies �click chemistry” regulates stress responses substrate specificity author correspondence mono-adp-ribosylase adp-ribosyl transferases rna polymerase ii garcia ba main content log adp-ribose moiety

Schema {🗺️}

ScholarlyArticle:
      headline:Identification of Protein Substrates of Specific PARP Enzymes Using Analog-Sensitive PARP Mutants and a “Clickable” NAD+ Analog
      pageEnd:135
      pageStart:111
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      genre:
         Springer Protocols
      isPartOf:
         name:Poly(ADP-Ribose) Polymerase
         isbn:
            978-1-4939-6993-7
            978-1-4939-6992-0
         type:Book
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         name:Springer New York
         logo:
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      author:
            name:Bryan A. Gibson
            affiliation:
                  name:University of Texas Southwestern Medical Center
                  address:
                     name:Laboratory of Signaling and Gene Regulation, Cecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center, Dallas, USA
                     type:PostalAddress
                  type:Organization
                  name:University of Texas Southwestern Medical Center
                  address:
                     name:Division of Basic Research, Department of Obstetrics and Gynecology, University of Texas Southwestern Medical Center, Dallas, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:W. Lee Kraus
            affiliation:
                  name:University of Texas Southwestern Medical Center
                  address:
                     name:Laboratory of Signaling and Gene Regulation, Cecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center, Dallas, USA
                     type:PostalAddress
                  type:Organization
                  name:University of Texas Southwestern Medical Center
                  address:
                     name:Division of Basic Research, Department of Obstetrics and Gynecology, University of Texas Southwestern Medical Center, Dallas, USA
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      keywords:ADP-ribosylation, Analog-sensitivity, Automodification, Click chemistry, Mono(ADP-ribosyl)ation, Mutation, NAD+ analog, PARP, Poly(ADP-ribose) polymerase, Poly(ADP-ribosyl)ation, Posttranslational modification
      description:The PARP family of ADP-ribosyl transferases contains 17 members in human cells, most of which catalyze the transfer of the ADP-ribose moiety of NAD+ onto their target proteins. This posttranslational modification plays important roles in cellular signaling, especially during cellular stresses, such as heat shock, inflammation, unfolded protein responses, and DNA damage. Knowing the specific proteins that are substrates for individual PARPs, as well as the specific amino acid residues in a given target protein that are ADP-ribosylated, is a key step in understanding the biology of individual PARPs. Recently, we developed a robust NAD+ analog-sensitive approach for PARPs, which allows PARP-specific ADP-ribosylation of substrates that is suitable for subsequent copper-catalyzed azide-alkyne cycloaddition (“click chemistry”) reactions. When coupled with proteomics and mass spectrometry, the analog-sensitive PARP approach can be used to identify the specific amino acids that are ADP-ribosylated by individual PARP proteins. In this chapter, we describe the key facets of the experimental design and application of the analog-sensitive PARP methodology to identify site-specific modification of PARP target proteins.
      datePublished:2017
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      isbn:
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      name:Springer New York
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      name:University of Texas Southwestern Medical Center
      address:
         name:Laboratory of Signaling and Gene Regulation, Cecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center, Dallas, USA
         type:PostalAddress
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      address:
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         type:PostalAddress
      name:University of Texas Southwestern Medical Center
      address:
         name:Laboratory of Signaling and Gene Regulation, Cecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center, Dallas, USA
         type:PostalAddress
      name:University of Texas Southwestern Medical Center
      address:
         name:Division of Basic Research, Department of Obstetrics and Gynecology, University of Texas Southwestern Medical Center, Dallas, USA
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            address:
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               type:PostalAddress
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            address:
               name:Division of Basic Research, Department of Obstetrics and Gynecology, University of Texas Southwestern Medical Center, Dallas, USA
               type:PostalAddress
            type:Organization
      name:W. Lee Kraus
      affiliation:
            name:University of Texas Southwestern Medical Center
            address:
               name:Laboratory of Signaling and Gene Regulation, Cecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center, Dallas, USA
               type:PostalAddress
            type:Organization
            name:University of Texas Southwestern Medical Center
            address:
               name:Division of Basic Research, Department of Obstetrics and Gynecology, University of Texas Southwestern Medical Center, Dallas, USA
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      email:[email protected]
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      name:Laboratory of Signaling and Gene Regulation, Cecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center, Dallas, USA
      name:Division of Basic Research, Department of Obstetrics and Gynecology, University of Texas Southwestern Medical Center, Dallas, USA
      name:Laboratory of Signaling and Gene Regulation, Cecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center, Dallas, USA
      name:Division of Basic Research, Department of Obstetrics and Gynecology, University of Texas Southwestern Medical Center, Dallas, USA
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