MARC Record from Library of Congress

LEADER: 03903cam a22004217i 4500
001 2013945304
003 DLC
005 20151024082223.0
008 130716t20132013nyua b 001 0 eng d
010 $a 2013945304
020 $a9781627036368 (alk. paper)
020 $a1627036369 (alk. paper)
020 $z9781627036375 (eBook)
035 $a(OCoLC)ocn847125726
040 $aYDXCP$beng$cYDXCP$erda$dBTCTA$dRML$dIDL$dOCLCO$dCHVBK$dCDX$dOCLCO$dDLC
042 $alccopycat
050 00 $aQP551$b.S615 2013
082 04 $a547.75$223
245 00 $aSirtuins :$bmethods and protocols /$cedited by Matthew D. Hirschey, Institute of Molecular Physiology, Duke University Medical Center, Durham, NC, USA.
264 1 $aNew York :$bHumana Press,$c[2013]
264 4 $c©2013
300 $axi, 314 pages :$billustrations (some color)$c26 cm.
336 $atext$btxt$2rdacontent
337 $aunmediated$bn$2rdamedia
338 $avolume$bnc$2rdacarrier
490 1 $aMethods in Molecular Biology ;$v1077
490 1 $aSpringer Protocols
504 $aIncludes bibliographical references and index.
505 00 $tIntroduction: sirtuins in aging and diseases /$rLeonard Guarente --$tSirtuins in yeast: phenotypes and tools /$rScott Tsuchiyama [and four others] --$tC. elegans sirtuins /$rMohan Viswanathan and Heidi A. Tissenbaum --$tGenetic and biochemical tools for investigating sirtuin function in Drosophila melanogaster /$rJason G. Wood, Rachel Whitaker, and Stephen L. Helfand --$tGenerating mammalian sirtuin tools for protein-interaction analysis /$rKathleen A. Hershberger [and three others] --$tMass spectrometry-based detection of protein acetylation /$rYu Li [and three others] --$tSILAC-based quantification of Sirt1-responsive lysine acetylome /$rYue Chen, Gozde Colak, and Yingming Zhao --$tTargeted quantitation of acetylated lysine peptides by selected reaction monitoring mass spectrometry /$rMatthew J. Rardin, Jason M. Held, and Bradford W. Gibson --$tIdentification of deacetylase substrates with the biotin switch approach /$rJ. Will Thompson, Alex Robeson, and Joshua L. Andersen --$tAssaying chromatin sirtuins /$rLei Zhong [and four others] --$tMeasurement of sirtuin enzyme activity using a substrate-agnostic fluorometric nicotinamide assay /$rBasil P. Hubbard and David A. Sinclair --$tDetecting sirtuin-catalyzed deacylation reactions using 32P-labeled NAD and thin-layer chromatography /$rAnita Zhu, Xiaoyang Su, and Hening Lin --$tChemical acetylation and deacetylation /$rKristofer S. Fritz --$tAccurate measurement of nicotinamide adenine dinucleotide (NAD+) with high-performance liquid chromatography /$rJun Yoshino and Shin-ichiro Imai --$tIn vivo measurement of the acetylation state of sirtuin substrates as a proxy for sirtuin activity /$rJohn Dominy, Pere Puigserver, and Carles Cantó --$tOxygen flux analysis to understand the biological function of sirtuins /$rDongning Wang [and three others] --$tThe emerging links between sirtuins and autophagy /$rIn Hye Lee, Jeanho Yun, and Toren Finkel --$tMethods to study the role of sirtuins in genome stability /$rPaloma Martínez-Redondo and Alejandro Vaquero --$tCircadian measurements of sirtuin biology /$rKathryn Moynihan Ramsey [and five others] --$tUtilizing calorie restriction to evaluate the role of sirtuins in healthspan and lifespan of mice /$rJessica Curtis and Rafael de Cabo.
650 0 $aProteins.
650 2 $aSirtuins.
655 7 $aLaboratory Manuals.$2mesh
700 1 $aHirschey, Matthew D.,$eeditor.
710 2 $aSpringer Science+Business Media,$ecopyright holder.
830 0 $aMethods in molecular biology (Clifton, N.J.) ;$vv. 1077.
830 0 $aSpringer protocols (Series)
856 42 $3Publisher description$uhttp://www.loc.gov/catdir/enhancements/fy1406/2013945304-d.html
856 41 $3Table of contents only$uhttp://www.loc.gov/catdir/enhancements/fy1406/2013945304-t.html