Poly (ADP-ribose) polymerase : methods and protocols /
Poly (ADP-ribose) polymerase : methods and protocols /
edited by Alexei V. Tulin.
- Second edition
- 1 online resource (xv, 528 pages) : illustrations (some color)
- Methods in molecular biology, 1608 1940-6029 ; Springer protocols .
- Methods in molecular biology (Clifton, N.J.) ; v. 1608. Springer protocols (Series) .
Includes bibliographical references and index.
Quantitation of poly(ADP-ribose) by isotope dilution mass spectrometry / Quantification of PARP activity in human tissues : ex vivo assays in blood cells and immunohistochemistry in human biopsies / Detecting and quantifying pADPr in vivo / Compartment-specific poly-ADP-ribose formation as a biosensor for subcellular NAD pools / Cell cycle resolved measurements of poly(ADP-ribose) formation and DNA damage signaling by quantitative image-based cytometry / Detecting protein ADP-ribosylation using a clickable aminooxy probe / ADP-ribosylated peptide enrichment and site identification : the phosphodiesterase-based method / Using clickable NAD+ analogs to label substrate proteins of PARPs / Identification of protein substrates of specific PARP enzymes using analog- sensitive PARP mutants and a "Clickable" NAD+ analog / Identification of ADP-ribose acceptor sites on in vitro modified proteins by liquid chromatography-tandem mass spectrometry / Proteome-wide identification of in vivo ADP-ribose acceptor sites by liquid chromatography-tandem mass spectrometry / Poly(ADP-ribose)-dependent chromatin remodeling in DNA repair / Methods to assess the role of poly(ADP-ribose) polymerases in regulating mitochondrial oxidation / Approaches for investigating translational regulation controlled by PARP1 : biotin-based UV cross-linking and Luciferase reporter assay / Methodology to identify poly-ADP-ribose polymerase 1 (PARP1)-mRNA targets by PAR-CLiP / Biochemical and biophysical methods for analysis of poly(ADP-ribose) polymerase 1 and its interactions with chromatin / PARP-1 interaction with and activation by histones and nucleosomes / Strategies employed for the development of PARP inhibitors / High-throughput colorimetric assay for identifying PARP-1 inhibitors using a large small-molecule collection / Testing PARP inhibitors using a murine xenograft model / In vitro long-term proliferation assays to study antiproliferative effects of PARP inhibitors on cancer cells / Use of inosine monophosphate dehydrogenase activity assay to determine the specificity of PARP-1 inhibitors / 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 / Purification of recombinant human PARP-3 / Purification of recombinant human PARG and activity assays / Studying catabolism of protein ADP-ribosylation / Purification of DNA damage-dependent PARPs from E. coli for structural and biochemical analysis / Identifying and validating tankyrase binders and substrates : a candidate approach / Computational and experimental studies of ADP-ribosylation / Tabea Zubel, Rita Martello, Alexander Bürkle, and Aswin Mangerich -- Eszter M. Horvath, Zsuzsanna K. Zsengellér, and Csaba Szabo -- Yi-Chen Lai, Rajesh K. Aneja, Margaret A. Satchell, and Robert S.B. Clark -- Magali R. VanLinden, Marc Niere, Andrey A. Nikiforov, Mathias Ziegler, and Christian Dölle -- Jone Michelena and Matthias Altmeyer -- Rory K. Morgan and Michael S. Cohen -- Casey M. Daniels, Shao-En Ong, and Anthony K.L. Leung -- Lu Zhang and Hening Lin -- Bryan A. Gibson and W. Lee Kraus -- Mario Leutert, Vera Bilan, Peter Gehrig, and Michael O. Hottiger -- Sara C. Larsen, Mario Leutert, Vera Bilan, Rita Martello, Stephanie Jungmichel, Clifford Young, Michael O. Hottiger, and Michael L. Nielsen -- Théo Lebeaupin, Rebecca Smith, Sébastien Huet, and Gyula Timinszky -- Edit Mikó, Tünde Kovács, Tamás Fodor, and Péter Bai -- Yingbiao Ji -- Manana Mekishvili, Elena Matveeva, and Yvonne Fondufe-Mittendorf -- Maggie H. Chassé, Uma M. Muthurajan, Nicholas J. Clark, Michael A. Kramer, Srinivas Chakravarthy, Thomas Irving, and Karolin Luger -- Colin Thomas, Elena Kotova, and Alexei V. Tulin -- Stacie Canan, Karen Maegley, and Nicola J. Curtin -- Elena Kotova and Alexei V. Tulin -- Peter Makhov, Sei Naito, and Vladimir M. Kolenko -- Heike Keilhack and Paul Chang -- Sajitha Anthony, Jeffrey R. Peterson, and Yingbiao Ji -- Sydney Shall, Terry Gaymes, Farzin Farzaneh, Nicola J. Curtin, and Ghulam J. Mufti -- Jean-Christophe Amé, Barbara Camuzeaux, Françoise Dantzer, and Valérie Schreiber -- Jean-Christophe Amé, Éléa Héberlé, Barbara Camuzeaux, Françoise Dantzer, and Valérie Schreiber -- Luca Palazzo, Dominic I. James, Ian D. Waddell, and Ivan Ahel -- Marie-France Langelier, Jamin D. Steffen, Amanda A. Riccio, Michael McCauley, and John M. Pascal -- Katie Pollock, Michael Ranes, Ian Collins, and Sebastian Guettler -- Robert G. Hammond, Xuan Tan, Matthew Chan, Anupam Goel, and Margaret A. Johnson.
This book presents multiple new and classical methods for studying the vital poly-ADP-ribose (pADPr) pathway. Beginning with techniques for the detection and quantification of the product of poly(ADP-ribose) polymerase (PARP) enzymatic activity and detection of variation in pADPr production during the cell cycle, the volume continues with sections on the identification of pADPr protein acceptors, methods focusing on studying molecular mechanisms of PARP functions in eukaryotic cells, particularly those involved in control of DNA repair and oxidative stress, as well as in expression regulation, approaches to the in vitro reconstitution of PARP-1 interaction with chromatin, the development and testing of small molecule PARP inhibitors, and the functions of understudied members of PARP family. Written for the highly successful Methods in Molecular Biology series, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and practical, Poly(ADP-Ribose) Polymerase: Methods and Protocols, Second Edition serves as an ideal companion to the first edition for scientists whose investigations involve this important pathway. The chapter 'Identifying and Validating Tankyrase Binders and Substrates: A Candidate Approach' is published open access under a CC BY 4.0 license.
9781493969937 1493969935
10.1007/978-1-4939-6993-7 doi
com.springer.onix.9781493969937 Springer Nature
GBB912773 bnb
019183898 Uk
NAD-ADP-ribosyltransferase.
Transferases.
Enzymes.
ADP Ribose Transferases
Poly(ADP-ribose) Polymerases
Poly(ADP-ribose) Polymerase Inhibitors
Transferases
Enzymes
Laboratory Manuals
Poly (ADP-ribose) polymérase.
Transférases.
Enzymes.
enzyme.
Proteins.
Science--Life Sciences--Biochemistry.
Transferases
Enzymes
NAD-ADP-ribosyltransferase
Electronic books.
Laboratory Manual
Laboratory manuals
Laboratory manuals.
Manuels de laboratoire.
QP606.P76
572/.792
W1 / ME9616J v.1608 2017 QU 25
Includes bibliographical references and index.
Quantitation of poly(ADP-ribose) by isotope dilution mass spectrometry / Quantification of PARP activity in human tissues : ex vivo assays in blood cells and immunohistochemistry in human biopsies / Detecting and quantifying pADPr in vivo / Compartment-specific poly-ADP-ribose formation as a biosensor for subcellular NAD pools / Cell cycle resolved measurements of poly(ADP-ribose) formation and DNA damage signaling by quantitative image-based cytometry / Detecting protein ADP-ribosylation using a clickable aminooxy probe / ADP-ribosylated peptide enrichment and site identification : the phosphodiesterase-based method / Using clickable NAD+ analogs to label substrate proteins of PARPs / Identification of protein substrates of specific PARP enzymes using analog- sensitive PARP mutants and a "Clickable" NAD+ analog / Identification of ADP-ribose acceptor sites on in vitro modified proteins by liquid chromatography-tandem mass spectrometry / Proteome-wide identification of in vivo ADP-ribose acceptor sites by liquid chromatography-tandem mass spectrometry / Poly(ADP-ribose)-dependent chromatin remodeling in DNA repair / Methods to assess the role of poly(ADP-ribose) polymerases in regulating mitochondrial oxidation / Approaches for investigating translational regulation controlled by PARP1 : biotin-based UV cross-linking and Luciferase reporter assay / Methodology to identify poly-ADP-ribose polymerase 1 (PARP1)-mRNA targets by PAR-CLiP / Biochemical and biophysical methods for analysis of poly(ADP-ribose) polymerase 1 and its interactions with chromatin / PARP-1 interaction with and activation by histones and nucleosomes / Strategies employed for the development of PARP inhibitors / High-throughput colorimetric assay for identifying PARP-1 inhibitors using a large small-molecule collection / Testing PARP inhibitors using a murine xenograft model / In vitro long-term proliferation assays to study antiproliferative effects of PARP inhibitors on cancer cells / Use of inosine monophosphate dehydrogenase activity assay to determine the specificity of PARP-1 inhibitors / 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 / Purification of recombinant human PARP-3 / Purification of recombinant human PARG and activity assays / Studying catabolism of protein ADP-ribosylation / Purification of DNA damage-dependent PARPs from E. coli for structural and biochemical analysis / Identifying and validating tankyrase binders and substrates : a candidate approach / Computational and experimental studies of ADP-ribosylation / Tabea Zubel, Rita Martello, Alexander Bürkle, and Aswin Mangerich -- Eszter M. Horvath, Zsuzsanna K. Zsengellér, and Csaba Szabo -- Yi-Chen Lai, Rajesh K. Aneja, Margaret A. Satchell, and Robert S.B. Clark -- Magali R. VanLinden, Marc Niere, Andrey A. Nikiforov, Mathias Ziegler, and Christian Dölle -- Jone Michelena and Matthias Altmeyer -- Rory K. Morgan and Michael S. Cohen -- Casey M. Daniels, Shao-En Ong, and Anthony K.L. Leung -- Lu Zhang and Hening Lin -- Bryan A. Gibson and W. Lee Kraus -- Mario Leutert, Vera Bilan, Peter Gehrig, and Michael O. Hottiger -- Sara C. Larsen, Mario Leutert, Vera Bilan, Rita Martello, Stephanie Jungmichel, Clifford Young, Michael O. Hottiger, and Michael L. Nielsen -- Théo Lebeaupin, Rebecca Smith, Sébastien Huet, and Gyula Timinszky -- Edit Mikó, Tünde Kovács, Tamás Fodor, and Péter Bai -- Yingbiao Ji -- Manana Mekishvili, Elena Matveeva, and Yvonne Fondufe-Mittendorf -- Maggie H. Chassé, Uma M. Muthurajan, Nicholas J. Clark, Michael A. Kramer, Srinivas Chakravarthy, Thomas Irving, and Karolin Luger -- Colin Thomas, Elena Kotova, and Alexei V. Tulin -- Stacie Canan, Karen Maegley, and Nicola J. Curtin -- Elena Kotova and Alexei V. Tulin -- Peter Makhov, Sei Naito, and Vladimir M. Kolenko -- Heike Keilhack and Paul Chang -- Sajitha Anthony, Jeffrey R. Peterson, and Yingbiao Ji -- Sydney Shall, Terry Gaymes, Farzin Farzaneh, Nicola J. Curtin, and Ghulam J. Mufti -- Jean-Christophe Amé, Barbara Camuzeaux, Françoise Dantzer, and Valérie Schreiber -- Jean-Christophe Amé, Éléa Héberlé, Barbara Camuzeaux, Françoise Dantzer, and Valérie Schreiber -- Luca Palazzo, Dominic I. James, Ian D. Waddell, and Ivan Ahel -- Marie-France Langelier, Jamin D. Steffen, Amanda A. Riccio, Michael McCauley, and John M. Pascal -- Katie Pollock, Michael Ranes, Ian Collins, and Sebastian Guettler -- Robert G. Hammond, Xuan Tan, Matthew Chan, Anupam Goel, and Margaret A. Johnson.
This book presents multiple new and classical methods for studying the vital poly-ADP-ribose (pADPr) pathway. Beginning with techniques for the detection and quantification of the product of poly(ADP-ribose) polymerase (PARP) enzymatic activity and detection of variation in pADPr production during the cell cycle, the volume continues with sections on the identification of pADPr protein acceptors, methods focusing on studying molecular mechanisms of PARP functions in eukaryotic cells, particularly those involved in control of DNA repair and oxidative stress, as well as in expression regulation, approaches to the in vitro reconstitution of PARP-1 interaction with chromatin, the development and testing of small molecule PARP inhibitors, and the functions of understudied members of PARP family. Written for the highly successful Methods in Molecular Biology series, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and practical, Poly(ADP-Ribose) Polymerase: Methods and Protocols, Second Edition serves as an ideal companion to the first edition for scientists whose investigations involve this important pathway. The chapter 'Identifying and Validating Tankyrase Binders and Substrates: A Candidate Approach' is published open access under a CC BY 4.0 license.
9781493969937 1493969935
10.1007/978-1-4939-6993-7 doi
com.springer.onix.9781493969937 Springer Nature
GBB912773 bnb
019183898 Uk
NAD-ADP-ribosyltransferase.
Transferases.
Enzymes.
ADP Ribose Transferases
Poly(ADP-ribose) Polymerases
Poly(ADP-ribose) Polymerase Inhibitors
Transferases
Enzymes
Laboratory Manuals
Poly (ADP-ribose) polymérase.
Transférases.
Enzymes.
enzyme.
Proteins.
Science--Life Sciences--Biochemistry.
Transferases
Enzymes
NAD-ADP-ribosyltransferase
Electronic books.
Laboratory Manual
Laboratory manuals
Laboratory manuals.
Manuels de laboratoire.
QP606.P76
572/.792
W1 / ME9616J v.1608 2017 QU 25