000 06211nam a22005775i 4500
001 978-1-0716-2942-0
003 DE-He213
005 20260610083640.0
007 cr nn 008mamaa
008 230403s2023 xxu| s |||| 0|eng d
020 _a9781071629420
_9978-1-0716-2942-0
024 7 _a10.1007/978-1-0716-2942-0
_2doi
050 4 _aQD431-431.7
072 7 _aPSBC
_2bicssc
072 7 _aSCI013040
_2bisacsh
072 7 _aPSB
_2thema
082 0 4 _a572.6
_223
245 1 0 _aProtein Arginylation
_h[electronic resource] :
_bMethods and Protocols /
_cedited by Anna S. Kashina.
250 _a2nd ed. 2023.
264 1 _aNew York, NY :
_bSpringer US :
_bImprint: Humana,
_c2023.
300 _aX, 297 p. 56 illus., 35 illus. in color.
_bonline resource.
336 _atext
_btxt
_2rdacontent
337 _acomputer
_bc
_2rdamedia
338 _aonline resource
_bcr
_2rdacarrier
341 0 _bTable of contents navigation
_2onix
341 0 _bSingle logical reading order
_2onix
341 0 _bShort alternative textual descriptions
_2onix
341 0 _bUse of color is not sole means of conveying information
_2onix
341 0 _bUse of high contrast between text and background color
_2onix
341 0 _bNext / Previous structural navigation
_2onix
341 0 _bAll non-decorative content supports reading without sight
_2onix
347 _atext file
_bPDF
_2rda
490 1 _aMethods in Molecular Biology,
_x1940-6029 ;
_v2620
505 0 _aProtein arginylation: milestones of discovery -- Recollection of how we came across the protein modification with amino acids by aminoacyl tRNA-protein transferase -- Arginyltransferase: a personal and historical perspective -- Arginylation in a Partially Purified Fraction of 150,000xg Supernatants of Axoplasm and Injured Vertebrate Nerves -- Preparation of ATE1 enzyme from native mammalian tissues -- Correlated measurement of endogenous ATE1 activity on native acceptor proteins in tissues and cultured cells to detect cellular aging -- Assaying the Post-translational Arginylation of Proteins in Cultured Cells -- Assaying ATE1 activity in yeast by β-gal degradation -- Assaying arginylation activity in cell lysates using a fluorescent reporter -- Assaying intracellular arginylation activity using a fluorescent reporter -- Bacterial expression and purification of recombinant arginyltransferase (ATE1) and Arg-tRNA synthetase (RRS) for arginylation assays -- Preparation of tRNAArg for arginylation assay by in vitro transcription -- Preparation of an enriched tRNAArg fraction for arginylation by expression in E. coli -- Enzymatic aminoacylation of tRNAArg using recombinant Arg-tRNA synthetase -- Assaying ATE1 activity in vitro -- High throughput arginylation assay in microplate format -- Assaying for arginyltransferase activity and specificity by peptide arrays -- Assay of arginyltransferase activity by a fluorescent HPLC method -- Identification of arginylated proteins by mass spectrometry -- Analysis of arginylated peptides by subtractive Edman degradation -- Transferase-Mediated Labeling of Protein N-Termini with Click Chemistry Handles -- Synthesis of peptides and proteins with site-specific glutamate arginylation -- Reconstitution of the arginyltransferase (ATE1) iron-sulfur cluster -- N-terminal arginylation pulldown analysis using the R-catcher tool -- Identification of protein arginylation by encapsulated N-terminal peptide enrichmentmethod -- Monitoring the Activation of Selective Autophagy via N-terminal Arginylation -- Analyzing the Interaction of Arginylated Proteins and Nt-Arg-Mimicking Chemical Compounds to N-Recognins -- Synthesis of Stably Charged Arg-tRNAArg for Structural Analysis -- A High-Throughput Colorimetric Microplate Assay for Determination of Plasma Arginase Activity -- Development of new tools for the studies of protein arginylation.
520 _aThis second edition provides updated and new chapters that detail comprehensive overview of all the existing methods on analyzing protein arginylation. Chapters guide readers through the early methods utilizing crude protein preparations and whole-cell assays to the latest advanced methods involving recombinant protein techniques, antibodies, high precision mass spectrometry, and chemical probes. Written in the format of the highly successful Methods in Molecular Biology series, each chapter includes an introduction to the topic, lists necessary materials and methods, includes tips on troubleshooting and known pitfalls, and step-by-step, readily reproducible protocols. Cutting-edge and thorough, Protein Arginylation: Methods and Protocols, Second Edition aims to be of interest to novice researchers involved in posttranslational arginylation research and researchers working on a broad range of posttranslational modifications.
532 8 _aAccessibility summary: This PDF does not fully comply with PDF/UA standards, but does feature limited screen reader support, described non-text content (images, graphs), bookmarks for easy navigation and searchable, selectable text. Users of assistive technologies may experience difficulty navigating or interpreting content in this document. We recognize the importance of accessibility, and we welcome queries about accessibility for any of our products. If you have a question or an access need, please get in touch with us at accessibilitysupport@springernature.com.
532 8 _aNo reading system accessibility options actively disabled
532 8 _aPublisher contact for further accessibility information: accessibilitysupport@springernature.com
650 0 _aProteins.
650 1 4 _aProteins.
700 1 _aKashina, Anna S.
_eeditor.
_0(orcid)0000-0002-0243-6866
_1https://orcid.org/0000-0002-0243-6866
_4edt
_4http://id.loc.gov/vocabulary/relators/edt
710 2 _aSpringerLink (Online service)
773 0 _tSpringer Nature eBook
776 0 8 _iPrinted edition:
_z9781071629413
776 0 8 _iPrinted edition:
_z9781071629437
776 0 8 _iPrinted edition:
_z9781071629444
830 0 _aMethods in Molecular Biology,
_x1940-6029 ;
_v2620
856 4 0 _uhttps://doi.org/10.1007/978-1-0716-2942-0
912 _aZDB-2-PRO
999 _c6067
_d6067