Screen LibraryADP-ribosylation and NAD+ utilizing enzymes : methods and protocols /
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| Group Author: | |
|---|---|
| Published: |
Humana Press,
|
| Publisher Address: | New York, NY : |
| Publication Dates: | [2018] |
| Literature type: | Book |
| Language: | English |
| Series: |
Methods in molecular biology,
1813 Springer protocols |
| Subjects: | |
| Carrier Form: | xiv, 417 pages : illustrations (some color) ; 27 cm. |
| Bibliography: | Includes bibliographical references and index. |
| ISBN: |
9781493985876 1493985876 |
| Index Number: | QP625 |
| CLC: | Q555-33 |
| Call Number: | Q555-33/A241 |
| Contents: |
Vitamin B3 in health and disease : toward the second century of discovery / Monitoring poly(ADP-Ribosyl)ation in response to DNA damage in live cells using fluorescently tagged macrodomains / In vitro techniques for ADP-ribosylated substrate identification / Assessment of intracellular auto-modification levels of ARTD10 using mono-ADP-ribose-specific macrodomains 2 and 3 of murine Artd8 / Biochemical and biophysical assays of PAR-WWE domain interactions and production of iso-ADPr for PAR-binding analysis / Assays for NAD+-dependent reactions and NAD+ metabolites / Generating protein-linked and protein-free mono-, oligo-, and poly(ADP-ribose) in vitro / Methods to study TCDD-inducible poly-ADP-ribose polymerase (TIPARP) mono-ADP-ribosyltransferase activity / Dictyostelium as a model to assess site-specific ADP-ribosylation events / Mono-ADP-ribosylation catalyzed by arginine-specific ADP-ribosyltransferases / Monitoring expression and enzyme activity of ecto-ARTCs / ADP-ribosyl-acceptor hydrolase activities catalyzed by the ARH family of proteins / Mono-ADP-ribosylhydrolase assays / Hydrolysis of ADP-ribosylation by macrodomains/ HPLC-based enzyme assays for sirtuins / Small-molecule screening assay for mono-ADP-ribosyltransferases / Simple, sensitive, and generalizable plate assay for screening PARP inhibitors / Nonlocalized searching of HCD data for fast and sensitive identification of ADP-ribosylated peptides / Quantitative determination of MAR hydrolase residue specificity in vitro by tandem mass spectrometry / Detection of ADP-ribosylating bacterial toxins / Preparation of recombinant alphaviruses for functional studies of ADP-ribosylation / Monitoring the sensitivity of T cell populations towards NAD+ released during cell preparation / Identifying target RNAs of PARPs / ADPr-peptide synthesis / Identifying genomic sites of ADP-ribosylation mediated byspecific nuclear PARP enzymes using click-ChIP / Methods for using a genetically encoded fluorescent biosensor to monitor nuclear NAD+ / |