Research Catalog

Poly (ADP-ribose) polymerase : methods and protocols /

Title
Poly (ADP-ribose) polymerase : methods and protocols / edited by Alexei V. Tulin.
Publication
  • New York : Humana Press : Springer, [2017]
  • ©2017

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StatusFormatAccessCall NumberItem Location
TextUse in library QH506 .M45 1984 vol.1608Off-site

Details

Additional Authors
Tulin, Alexei V.,
Description
xv, 528 pages : illustrations (some color); 26 cm.
Series Statement
  • Methods in molecular biology, 1940-6029 ; 1608
  • Springer protocols
Uniform Title
  • Methods in molecular biology (Clifton, N.J.) ; v. 1608.
  • Springer protocols (Series)
Subjects
Bibliography (note)
  • Includes bibliographical references and index.
Additional Formats (note)
  • Also available in an electronic version.
Contents
Quantitation of poly(ADP-ribose) by isotope dilution mass spectrometry / Tabea Zubel, Rita Martello, Alexander Bürkle, and Aswin Mangerich -- Quantification of PARP activity in human tissues : ex vivo assays in blood cells and immunohistochemistry in human biopsies / Eszter M. Horvath, Zsuzsanna K. Zsengellér, and Csaba Szabo -- Detecting and quantifying pADPr in vivo / Yi-Chen Lai, Rajesh K. Aneja, Margaret A. Satchell, and Robert S.B. Clark -- Compartment-specific poly-ADP-ribose formation as a biosensor for subcellular NAD pools / Magali R. VanLinden, Marc Niere, Andrey A. Nikiforov, Mathias Ziegler, and Christian Dölle -- Cell cycle resolved measurements of poly(ADP-ribose) formation and DNA damage signaling by quantitative image-based cytometry / Jone Michelena and Matthias Altmeyer -- Detecting protein ADP-ribosylation using a clickable aminooxy probe / Rory K. Morgan and Michael S. Cohen -- ADP-ribosylated peptide enrichment and site identification : the phosphodiesterase-based method / Casey M. Daniels, Shao-En Ong, and Anthony K.L. Leung -- Using clickable NAD+ analogs to label substrate proteins of PARPs / Lu Zhang and Hening Lin -- Identification of protein substrates of specific PARP enzymes using analog- sensitive PARP mutants and a "Clickable" NAD+ analog / Bryan A. Gibson and W. Lee Kraus -- Identification of ADP-ribose acceptor sites on in vitro modified proteins by liquid chromatography-tandem mass spectrometry / Mario Leutert, Vera Bilan, Peter Gehrig, and Michael O. Hottiger -- Proteome-wide identification of in vivo ADP-ribose acceptor sites by liquid chromatography-tandem mass spectrometry / Sara C. Larsen, Mario Leutert, Vera Bilan, Rita Martello, Stephanie Jungmichel, Clifford Young, Michael O. Hottiger, and Michael L. Nielsen -- Poly(ADP-ribose)-dependent chromatin remodeling in DNA repair / Théo Lebeaupin, Rebecca Smith, Sébastien Huet, and Gyula Timinszky -- Methods to assess the role of poly(ADP-ribose) polymerases in regulating mitochondrial oxidation / Edit Mikó, Tünde Kovács, Tamás Fodor, and Péter Bai -- Approaches for investigating translational regulation controlled by PARP1 : biotin-based UV cross-linking and Luciferase reporter assay / Yingbiao Ji -- Methodology to identify poly-ADP-ribose polymerase 1 (PARP1)-mRNA targets by PAR-CLiP / Manana Mekishvili, Elena Matveeva, and Yvonne Fondufe-Mittendorf -- Biochemical and biophysical methods for analysis of poly(ADP-ribose) polymerase 1 and its interactions with chromatin / Maggie H. Chassé, Uma M. Muthurajan, Nicholas J. Clark, Michael A. Kramer, Srinivas Chakravarthy, Thomas Irving, and Karolin Luger -- PARP-1 interaction with and activation by histones and nucleosomes / Colin Thomas, Elena Kotova, and Alexei V. Tulin -- Strategies employed for the development of PARP inhibitors / Stacie Canan, Karen Maegley, and Nicola J. Curtin -- High-throughput colorimetric assay for identifying PARP-1 inhibitors using a large small-molecule collection / Elena Kotova and Alexei V. Tulin -- Testing PARP inhibitors using a murine xenograft model / Peter Makhov, Sei Naito, and Vladimir M. Kolenko -- In vitro long-term proliferation assays to study antiproliferative effects of PARP inhibitors on cancer cells / Heike Keilhack and Paul Chang -- Use of inosine monophosphate dehydrogenase activity assay to determine the specificity of PARP-1 inhibitors / Sajitha Anthony, Jeffrey R. Peterson, and Yingbiao Ji -- Use of PARP inhibitors in cancer therapy : use as adjuvant with chemotherapy or radiotherapy, use as a single agent in susceptible patients, and techniques used to identify susceptible patients / Sydney Shall, Terry Gaymes, Farzin Farzaneh, Nicola J. Curtin, and Ghulam J. Mufti -- Purification of recombinant human PARP-3 / Jean-Christophe Amé, Barbara Camuzeaux, Françoise Dantzer, and Valérie Schreiber -- Purification of recombinant human PARG and activity assays / Jean-Christophe Amé, Éléa Héberlé, Barbara Camuzeaux, Françoise Dantzer, and Valérie Schreiber -- Studying catabolism of protein ADP-ribosylation / Luca Palazzo, Dominic I. James, Ian D. Waddell, and Ivan Ahel -- Purification of DNA damage-dependent PARPs from E. coli for structural and biochemical analysis / Marie-France Langelier, Jamin D. Steffen, Amanda A. Riccio, Michael McCauley, and John M. Pascal -- Identifying and validating tankyrase binders and substrates : a candidate approach / Katie Pollock, Michael Ranes, Ian Collins, and Sebastian Guettler -- Computational and experimental studies of ADP-ribosylation / Robert G. Hammond, Xuan Tan, Matthew Chan, Anupam Goel, and Margaret A. Johnson.
ISBN
  • 9781493969920
  • 1493969935 (canceled/invalid)
  • 9781493969937 (canceled/invalid)
Owning Institutions
Princeton University Library