{"product_id":"polyadp-ribose-polymerase-alexei-v-tulin-9781071628904","title":"Poly(adp-Ribose) Polymerase: Methods and Protocols","description":"\u003cp\u003e\u003cb\u003ePart I: Detection and Quantification of pADPr\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e \u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1. Fluorescence-Based Analyses of Poly(ADP-Ribose) Length by Gel Electrophoresis, High Performance Liquid Chromatography, and Capillary Electrophoresis\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Mohsen Badiee, Audrey Boutonnet, Dat Phan, and Anthony K.L. Leung\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e2. Detecting and Quantifying pADPr In Vivo\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Andrew M. Lamade, Yaming Chen, Carla J. Johnson, Hülya Bayır, and Robert S.B. Clark\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e3. Quantitative Analysis of Nuclear Poly(ADP-Ribose) Dynamics in Response to Laser-Induced DNA Damage\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Christopher A. Koczor, Kate M. Saville, Rasha Q. Al-Rahahleh, Joel F. Andrews, Jianfeng Li, and Robert W. Sobol\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e4. Analyzing PARP1 Activity: Small Molecule Reactants and Attached Chains of Poly(ADP-Ribose)\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Johannes Rudolph and Karolin Luger\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e5. Detecting Poly(ADP-Ribose) In Vitro and in Cells Using PAR-Trackers\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Sridevi Challa, Amy L. Whitaker, and W. Lee Kraus\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e6. An Enzyme-Linked Immunosorbent Assay to Quantify Poly(ADP-Ribose) Level In Vivo\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Chieri Ida, Sachiko Yamashita, Takayuki Eguchi, Yasuhito Kuroda, Setsu Nakae, Yoshisuke Nishi, Kazuo Kamemura, Tsuyoshi Shirai, Tamio Mizukami, Masakazu Tanaka, Joel Moss, and Masanao Miwa\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e7. Subcellular Quantitation of ADP-Ribosylation by High Content Microscopy\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Lukas Muskalla, Anka Güldenpfennig, and Michael O. Hottiger\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e8. A Simple Method to Study ADP-Ribosylation Reversal: From Function to Drug Discovery\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Johannes Gregor Matthias Rack and Ivan Ahel\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart II: Identification of Protein Targets\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e \u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9. \u003c\/b\u003e\u003cb\u003eImmunoprecipitation Using Mono-ADP-Ribosylation Specific Antibodies\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Helen Dauben and Ivan Matic\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e10. A Clickable NAD\u003csup\u003e+\u003c\/sup\u003e Analog-Based Assay of Poly(ADP-Ribosyl)ated Proteins\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Dongsheng Yao, Heba Ahmed, and Junqi Song\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e11. Functional Analysis of Histone ADP-Ribosylation In Vitro and in Cells\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Dan Huang, Andrea D. Edwards, Xuan Gong, and W. Lee Kraus\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart III: Functional Analysis\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e \u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12. \u003c\/b\u003e\u003cb\u003eStudying the Immunomodulatory Functions of PARP1 and PARP2 in Mouse Models of Cancer\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Nura Lutfi, Carlos Martínez, and José Yélamos\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e13. Methods for Investigating Transient Receptor Potential Melastatin-2 (TRPM2), a Cation Channel Activated by ADP-Ribose and Involved in Cell Death\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Hannah K. Hall and David W. Koh\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e14. Methods to Assess the Role of PARPs in Regulating Mitochondrial Oxidative Function\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Tünde Kovács, Boglárka Rauch, Edit Mikó, and Péter Bai\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e15. Characterizing ADP-Ribosylation Sites Using Af1521 Enrichment Coupled to ETD-Based Mass Spectrome\u003cbr\u003e\u003cbr\u003e\u003cb\u003eAuthor:\u003c\/b\u003e Alexei V. Tulin\u003cbr\u003e\u003cb\u003eISBN-10:\u003c\/b\u003e 1071628909\u003cbr\u003e\u003cb\u003eISBN-13:\u003c\/b\u003e 9781071628904\u003cbr\u003e\u003cb\u003ePublisher:\u003c\/b\u003e Humana\u003cbr\u003e\u003cb\u003eLanguage:\u003c\/b\u003e English\u003cbr\u003e\u003cb\u003ePublished:\u003c\/b\u003e 12\/15\/2022\u003cbr\u003e\u003cb\u003ePages:\u003c\/b\u003e 446\u003cbr\u003e\u003cb\u003eFormat:\u003c\/b\u003e Hardcover\u003cbr\u003e\u003cb\u003eWeight:\u003c\/b\u003e 2.24lbs\u003cbr\u003e\u003cb\u003eSize:\u003c\/b\u003e 10.00h x 7.00w x 1.00d\u003c\/b\u003e\u003c\/p\u003e","brand":"Alexei V. Tulin","offers":[{"title":"Hardcover","offer_id":48087527260415,"sku":"9781071628904","price":249.99,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0662\/2982\/9887\/files\/img_5ee99d1f-d7bb-4ff9-ba9a-103ef40399c1.jpg?v=1769100558","url":"https:\/\/www.whiterainbookhouse.com\/products\/polyadp-ribose-polymerase-alexei-v-tulin-9781071628904","provider":"WR Book House","version":"1.0","type":"link"}