All Stanford University & Hospital ID holders are now welcome to visit Lane Library! Learn more
Today's Hours: 8:00am - 10:00pm


Filter Applied Clear All

Did You Mean:

Search Results

  • Book
    edited by Paul Chang.
    Vitamin B3 in health and disease : toward the second century of discovery / Myron K. Jacobson and Elaine L. Jacobson -- Monitoring poly(ADP-Ribosyl)ation in response to DNA damage in live cells using fluorescently tagged macrodomains / Rebecca Smith and Gyula Timinszky -- In vitro techniques for ADP-ribosylated substrate identification / Giovanna Grimaldi, Giuliana Catara, Carmen Valente, and Daniela Corda -- Assessment of intracellular auto-modification levels of ARTD10 using mono-ADP-ribose-specific macrodomains 2 and 3 of murine Artd8 / Mareike Bütepage, Sarah Krieg, Laura Eckei, Jinyu Li, Giulia Rossetti, Patricia Verheugd, and Bernhard Lüscher -- Biochemical and biophysical assays of PAR-WWE domain interactions and production of iso-ADPr for PAR-binding analysis / Zhizhi Wang and Wenqing Xu -- Assays for NAD+-dependent reactions and NAD+ metabolites / Michael B. Schultz, Yuancheng Lu, Nady Braidy, and David A. Sinclair -- Generating protein-linked and protein-free mono-, oligo-, and poly(ADP-ribose) in vitro / Ken Y. Lin, Dan Huang, and W. Lee Kraus -- Methods to study TCDD-inducible poly-ADP-ribose polymerase (TIPARP) mono-ADP-ribosyltransferase activity / David Hutin, Giulia Grimaldi, and Jason Matthews -- Dictyostelium as a model to assess site-specific ADP-ribosylation events / Anna-Lena Kolb, Duen-Wei Hsu, Ana B. A. Wallis, Seiji Ura, Alina Rakhimova, Catherine J. Pears, and Nicholas D. Lakin -- Mono-ADP-ribosylation catalyzed by arginine-specific ADP-ribosyltransferases / Linda A. Stevens and Joel Moss -- Monitoring expression and enzyme activity of ecto-ARTCs / Stephan Menzel, Sahil Adriouch, Peter Bannas, Friedrich Haag, and Friedrich Koch-Nolte -- ADP-ribosyl-acceptor hydrolase activities catalyzed by the ARH family of proteins / Masato Mashimo and Joel Moss -- Mono-ADP-ribosylhydrolase assays / Jeannette Abplanalp, Ann-Katrin Hopp, and Michael O. Hottiger -- Hydrolysis of ADP-ribosylation by macrodomains/ Melanija Posavec Marjanovic, Gytis Jankevicius, and Ivan Ahel -- HPLC-based enzyme assays for sirtuins / Jun Young Hong, Xiaoyu Zhang, and Hening Lin -- Small-molecule screening assay for mono-ADP-ribosyltransferases / Teemu Haikarainen, Sudarshan Murthy, Mirko M. Maksimainen, and Lari Lehtiö -- Simple, sensitive, and generalizable plate assay for screening PARP inhibitors / Ilsa T. Kirby, Rory K. Morgan, and Michael S. Cohen -- Nonlocalized searching of HCD data for fast and sensitive identification of ADP-ribosylated peptides / Thomas Colby, Juan José Bonfiglio, and Ivan Matic -- Quantitative determination of MAR hydrolase residue specificity in vitro by tandem mass spectrometry / Robert Lyle McPherson, Shao-En Ong, and Anthony K. L. Leung -- Detection of ADP-ribosylating bacterial toxins / Chen Chen and Joseph T. Barbieri -- Preparation of recombinant alphaviruses for functional studies of ADP-ribosylation / Rachy Abraham, Robert Lyle McPherson, Easwaran Sreekumar, Anthony K. L. Leung, and Diane E. Griffin -- Monitoring the sensitivity of T cell populations towards NAD+ released during cell preparation / Björn Rissiek, Marco Lukowiak, Friedrich Haag, Tim Magnus, and Friedrich Koch-Nolte -- Identifying target RNAs of PARPs / Florian J. Bock and Paul Chang -- ADPr-peptide synthesis / Hans A. V. Kistemaker, Jim Voorneveld, and Dmitri V. Filippov -- Identifying genomic sites of ADP-ribosylation mediated byspecific nuclear PARP enzymes using click-ChIP / Ryan A. Rogge, Bryan A. Gibson, and W. Lee Kraus -- Methods for using a genetically encoded fluorescent biosensor to monitor nuclear NAD+ / Michael S. Cohen, Melissa L. Stewart, Richard H. Goodman, and Xiaolu A. Cambronne.
    Digital Access Springer 2018