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  • English  (163)
  • 1
    Online Resource
    Online Resource
    Totowa, NJ : Humana Press
    UID:
    (DE-627)1652146024
    Format: Online-Ressource (XI, 266 p. 54 illus., 18 illus. in color, digital)
    ISBN: 9781627033053
    Series Statement: Methods in Molecular Biology, Methods and Protocols 981
    Content: Validation of Protein Acetylation by Mass Spectrometry -- Application of the CIRAD Mass Spectrometry Approach for Lysine Acetylation Site Discovery -- Application of the MIDAS Approach for Analysis of Lysine Acetylation Sites -- Application of High Content Biology to Yield Quantitative Spatial Proteomic Information on Protein Acetylations -- Towards the N-terminal Acetylome: An N-terminal Acetylated Peptide Enrichment Method Using CNBr-Activated Sepharose Resin -- Identification and Analysis of O-acetylated Sialoglycoproteins -- HPLC-based Quantification of in vitro N-terminal Acetylation -- Separation and Purification of Multiply Acetylated Proteins using Cation-exchange Chromatography -- In-gel N-acetylation for the Quantification of the Degree of Protein in vivo N-terminal Acetylation -- Computational Prediction of Lysine Acetylation Proteome-wide -- Generation and Characterization of Pan-specific Anti-acetyllysine Antibody -- Using Functional Proteome Microarrays to Study Protein Lysine Acetylation -- Quantitation of Nucleosome Acetylation and other Histone Post-Translational Modifications Using Microscale NU-ELISA -- Preparing Semisynthetic and Fully Synthetic Histones H3 and H4 to Modify the Nucleosome Core -- Production of Amino-terminally Acetylated Recombinant Proteins in E. coli -- Identification of Lysine Acetyltransferase Substrates using Bioorthogonal Chemical Proteomics -- Non-radioactive in-vitro Assays for Histone Deacetylases -- The Fluorescence-Based Acetylation Assay Using Thiol-Sensitive Probes -- Analysis of Protein Acetyltransferase Structure-function Relation by Surface-Enhanced Raman Scattering (SERS): A Tool to Screen and Characterize Small Molecule Modulators.
    Content: Thousands of proteins have been identified to be acetylated. Immense research power has been dedicated to experiments to solve the biological implications of each and every protein acetylation. Two particular sites of protein acetylation have been described intensively: the N-terminal methionine residue of a nascent protein and lysine residues within a protein. In Protein Acetylation: Methods and Protocols, expert researchers in the field detail many of the methods which are now commonly used to study protein acetylation. These include methods and techniques for identification of protein acetylation, column- and gel electrophoresis-based approaches, computationally prediction, and the biological response to protein acetylation. Written in the highly successful Methods in Molecular Biology™ series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and key tips on troubleshooting and avoiding known pitfalls. Authoritative and practical, Protein Acetylation: Methods and Protocols seeks to aid scientists in the further study of the technical aspects involved in understanding protein acetylation.
    Additional Edition: 9781627033046
    Additional Edition: Buchausg. u.d.T. 978-1-627-03304-6
    Language: English
    URL: Cover
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  • 2
    Online Resource
    Online Resource
    Totowa, NJ : Humana Press
    UID:
    (DE-604)BV044951274
    Format: 1 Online-Ressource (XI, 266 p. 54 illus., 18 illus. in color)
    ISBN: 9781627033053
    Series Statement: Methods in Molecular Biology, Methods and Protocols 981
    Content: Thousands of proteins have been identified to be acetylated. Immense research power has been dedicated to experiments to solve the biological implications of each and every protein acetylation. Two particular sites of protein acetylation have been described intensively: the N-terminal methionine residue of a nascent protein and lysine residues within a protein. In Protein Acetylation: Methods and Protocols, expert researchers in the field detail many of the methods which are now commonly used to study protein acetylation. These include methods and techniques for identification of protein acetylation, column- and gel electrophoresis-based approaches, computationally prediction,  and the biological response to protein acetylation. Written in the highly successful Methods in Molecular Biology™ series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and key tips on troubleshooting and avoiding known pitfalls.   Authoritative and practical, Protein Acetylation: Methods and Protocols seeks to aid scientists in the further study of the technical aspects involved in understanding protein acetylation
    Additional Edition: Erscheint auch als Druck-Ausgabe ISBN 9781627033046
    Language: English
    URL: Volltext  (URL des Erstveröffentlichers)
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  • 3
    Book
    Book
    New York [u.a.] : Humana Pr.
    UID:
    (DE-627)737564725
    Format: XI, 266 S , Ill., graph. Darst
    ISBN: 1627033041 , 9781627033046
    Series Statement: Methods in molecular biology 981
    Content: Thousands of proteins have been identified to be acetylated. Immense research power has been dedicated to experiments to solve the biological implications of each and every protein acetylation. Two particular sites of protein acetylation have been described intensively: the N-terminal methionine residue of a nascent protein and lysine residues within a protein. In Protein Acetylation: Methods and Protocols, expert researchers in the field detail many of the methods which are now commonly used to study protein acetylation. These include methods and techniques for identification of protein acetylation, column- and gel electrophoresis-based approaches, computationally prediction, and the biological response to protein acetylation. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and key tips on troubleshooting and avoiding known pitfalls. Authoritative and practical, Protein Acetylation: Methods and Protocols seeks to aid scientists in the further study of the technical aspects involved in understanding protein acetylation. --
    Note: Includes bibliogaphical references and index , Validation of protein acetylation by mass spectrometry , Validation of protein acetylation by mass spectrometry , Application of the CIRAD mass spectrometry approach for lysine acetylation site discovery , Application of the MIDAS approach for analysis of lysine acetylation sites , Application of high content biology to yield quantitative spatial proteomic information on protein acetylations , Towards the N-Terminal acetylome : an N-Terminal acetylated peptide enrichment method using CNBr-activated sepharose resin , Identification and analysis of o-acetylated sialoglycoproteins , HPLC-based quantification of in vitro N-terminal acetylation , Separation and purification of multiply acetylated proteins using cation-exchange chromatography , In-gel N-acetylation for the quantification of the degree of protein in vivo N-terminal acetylation , Computational prediction of lysine acetylation proteome-wide , Generation and characterization of pan-specific anti-acetyllysine antibody , Using functional proteome microarrays to study protein lysine acetylation , Quantitation of nucleosome acetylation and other histone posttranslational modifications using microscale NU-ELISA , Preparing semisynthetic and fully synthetic histones H3 and H4 to modify the nucleosome core , Production of amino-terminally acetylated recombinant proteins in E. coli , Identification of lysine acetyltransferase substrates using bioorthogonal chemical proteomics , Nonradioactive in vitro assays for histone deacetylases , Fluorescence-based acetylation assay using thiol-sensitive probes , Analysis of protein acetyltransferase structure-function relation by surface-enhanced raman scattering (SERS): a tool to screen and characterize small molecule modulators , Application of the CIRAD mass spectrometry approach for lysine acetylation site discovery , Application of the MIDAS approach for analysis of lysine acetylation sites , Application of high content biology to yield quantitative spatial proteomic information on protein acetylations , Towards the N-Terminal acetylome : an N-Terminal acetylated peptide enrichment method using CNBr-activated sepharose resin , Identification and analysis of o-acetylated sialoglycoproteins , HPLC-based quantification of in vitro N-terminal acetylation , Separation and purification of multiply acetylated proteins using cation-exchange chromatography , In-gel N-acetylation for the quantification of the degree of protein in vivo N-terminal acetylation , Computational prediction of lysine acetylation proteome-wide , Generation and characterization of pan-specific anti-acetyllysine antibody , Using functional proteome microarrays to study protein lysine acetylation , Quantitation of nucleosome acetylation and other histone posttranslational modifications using microscale NU-ELISA , Preparing semisynthetic and fully synthetic histones H3 and H4 to modify the nucleosome core , Production of amino-terminally acetylated recombinant proteins in E. coli , Identification of lysine acetyltransferase substrates using bioorthogonal chemical proteomics , Nonradioactive in vitro assays for histone deacetylases , Fluorescence-based acetylation assay using thiol-sensitive probes , Analysis of protein acetyltransferase structure-function relation by surface-enhanced raman scattering (SERS): a tool to screen and characterize small molecule modulators
    Language: English
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  • 4
    Online Resource
    Online Resource
    Totowa, NJ : Humana Press
    UID:
    (DE-627)737954000
    Format: Online-Ressource (XI, 266 p. 54 illus., 18 illus. in color, digital)
    ISBN: 9781627033053
    Series Statement: Methods in Molecular Biology, Methods and Protocols 981
    Language: English
    Library Location Call Number Volume/Issue/Year Availability
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  • 5
    UID:
    (DE-101)1324924314
    Format: Online-Ressource
    Note: Dissertation Würzburg, Universität Würzburg 2024
    Language: English
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  • 6
    UID:
    (DE-101)1288102348
    Format: Online-Ressource
    Content: To evade the host immune system, several pathogens periodically change their cell-surface epitopes. In the African trypanosomes, antigenic variation is achieved by tightly regulating the expression of a multigene family encoding a large repertoire of variant surface glycoproteins (VSGs). Immune evasion relies on two important features: exposing a single type of VSG at the cell surface and periodically and very rapidly switching the expressed VSG. Transcriptional switching between resident telomeric VSG genes does not involve DNA rearrangements, and regulation is probably epigenetic. The histone methyltransferase DOT1B is a nonessential protein that trimethylates lysine 76 of histone H3 in Trypanosoma brucei. Here we report that transcriptionally silent telomeric VSGs become partially derepressed when DOT1B is deleted, whereas nontelomeric loci are unaffected. DOT1B also is involved in the kinetics of VSG switching: in DeltaDOT1B cells, the transcriptional switch is so slow that cells expressing two VSGs persist for several weeks, indicating that monoallelic transcription is compromised. We conclude that DOT1B is required to maintain strict VSG silencing and to ensure rapid transcriptional VSG switching, demonstrating that epigenetics plays an important role in regulating antigenic variation in T. brucei.
    In: Datenlieferant: Open Access LMU (Ludwig-Maximilians-University Munich)
    Language: English
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  • 7
    UID:
    (DE-603)475487672
    Format: Online-Ressource
    Note: Dissertation Würzburg, Universität Würzburg 2020
    Language: English
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  • 8
    UID:
    (DE-101)1225296048
    Format: Online-Ressource
    Note: Dissertation Würzburg, Universität Würzburg 2020
    Language: English
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  • 9
    UID:
    (DE-627)1747318655
    Format: 1 Online-Ressource
    Note: Dissertation Würzburg, Universität Würzburg 2020
    Language: English
    Keywords: Hochschulschrift ; Dissertation ; Hochschulschrift
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  • 10
    UID:
    (DE-101)1299878989
    Format: Online-Ressource
    ISSN: 1521-3773
    Content: The power of words: According to its generally accepted definition, the process of “design” is the creation of a form that fulfills a given function as well as possible and is also considered aesthetically pleasing. This implies a type of creativity that does not exist in the synthesis of new chemical compounds. This essay discusses the implications of the term “design” in the context of chemistry.
    In: volume:45
    In: number:21
    In: year:2006
    In: pages:3406-3412
    In: extent:7
    In: Angewandte Chemie / International edition, Weinheim : Wiley-VCH, 1962-, 45, Heft 21 (2006), 3406-3412 (gesamt 7), 1521-3773
    Language: English
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