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03106nam a22002895i 4500 |
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000276788 |
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20200921135604.0 |
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cr nn 008mamaa |
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180810s2018 xxu| s |||| 0|eng d |
| 020 |
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|a 9781493985883
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| 024 |
7 |
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|a 10.1007/978-1-4939-8588-3
|2 doi
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| 040 |
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|a Sistema de Bibliotecas del Tecnológico de Costa Rica
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| 245 |
1 |
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|a ADP-ribosylation and NAD+ Utilizing Enzymes :
|b Methods and Protocols /
|c edited by Paul Chang.
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| 250 |
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|a 1st ed. 2018.
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| 260 |
# |
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|a New York, NY :
|b Springer New York :
|b Imprint: Humana,
|c 2018.
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| 300 |
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|a XIV, 417 p. 95 illus., 51 illus. in color. :
|b online resource.
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| 336 |
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|a text
|b txt
|2 rdacontent
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| 337 |
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|a computer
|b c
|2 rdamedia
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| 338 |
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|a online resource
|b cr
|2 rdacarrier
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| 490 |
1 |
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|a Methods in Molecular Biology,
|v 1813
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| 505 |
0 |
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|a 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 -- A Simple, Sensitive, and Generalizable Plate Assay for Screening PARP Inhibitors -- Non-Localized 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 by Specific Nuclear PARP Enzymes Using Click-ChIP -- Methods for Using a Genetically-Encoded Fluorescent Biosensor to Monitor Nuclear NAD+.
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| 650 |
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0 |
|a Biochemistry.
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| 650 |
1 |
4 |
|a Biochemistry, general.
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| 700 |
1 |
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|a Chang, Paul.
|e editor.
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| 710 |
2 |
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|a SpringerLink (Online service)
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| 773 |
0 |
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|t Springer eBooks
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| 900 |
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|a Libro descargado a ALEPH en bloque (proveniente de proveedor)
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