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|a 9781603274753
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|a Lin, Ren-Jang
|e [editor]
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245 |
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|a RNA-Protein Interaction Protocols
|h Elektronische Ressource
|c edited by Ren-Jang Lin
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|a 2nd ed. 2008
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260 |
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|a Totowa, NJ
|b Humana
|c 2008, 2008
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300 |
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|a XVI, 416 p
|b online resource
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|a Quantification of MicroRNAs, Splicing Isoforms, and Homologous mRNAs With the Invader Assay -- Analysis of RNA Structure and RNA-Protein Interactions in Mammalian Cells by Use of Terminal Transferase-Dependent PCR -- Duplex Unwinding and RNP Remodeling With RNA Helicases -- Preparation of Efficient Splicing Extracts From Whole Cells, Nuclei, and Cytoplasmic Fractions -- Designing and Utilization of siRNAs Targeting RNA Binding Proteins -- The use of Saccharomyces cerevisiae proteomic libraries to identify RNA-modifying proteins
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|a Isolation of a Sequence-Specific RNA Binding Protein, Polypyrimidine Tract Binding Protein, Using RNA Affinity Chromatography -- An Affinity Oligonucleotide Displacement Strategy to Purify Ribonucleoprotein Complexes Applied to Human Telomerase -- RNA Affinity Tags for the Rapid Purification and Investigation of RNAs and RNA–Protein Complexes -- Assembly and Glycerol Gradient Isolation of Yeast Spliceosomes Containing Transcribed or Synthetic U6 snRNA -- Purification of Ribonucleoproteins Using Peptide-Elutable Antibodies and Other Affinity Techniques -- CLIP: Crosslinking and ImmunoPrecipitation of In Vivo RNA Targets of RNA-Binding Proteins -- Quantitative Analysis of Protein-RNA Interactions by Gel Mobility Shift -- Monitoring Assembly of Ribonucleoprotein Complexes by Isothermal Titration Calorimetry -- Characterization of RNA—Protein Interactions by Phosphorothioate Footprinting and Its Applications to the Ribosome --
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|a In Vivo Analysis of Ribonucleoprotein Complexes Using Nucleotide Analog Interference Mapping -- T7 RNA Polymerase-Mediated Incorporation of 8-N3AMP Into RNA for Studying Protein-RNA Interactions -- A Simple Crosslinking Method, CLAMP, to Map the Sites of RNA-Contacting Domains Within a Protein -- Proteins Specifically Modified With a Chemical Nuclease as Probes of RNA-Protein Interaction -- RNA-Protein Crosslink Mapping Using TEV Protease -- Structural Analysis of Protein-RNA Interactions With Mass Spectrometry -- Analyzing RNA-Protein Crosslinking Sites in Unlabeled Ribonucleoprotein Complexes by Mass Spectrometry -- In Vitro Selection of Random RNA Fragments to Identify Protein-Binding Sites Within Large RNAs -- Immunoprecipitation Analysis to Study RNA-Protein Interactions in Xenopus Oocytes -- Mapping the Regions of RNase P Catalytic RNA That Are Potentially inClose Contact With Its Protein Cofactor --
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653 |
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|a Cell Biology
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653 |
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|a Medical Genetics
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653 |
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|a Protein Biochemistry
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653 |
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|a Cytology
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653 |
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|a Medical genetics
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653 |
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|a Biochemistry
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653 |
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|a Proteins
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|a eng
|2 ISO 639-2
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989 |
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|b Springer
|a Springer eBooks 2005-
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490 |
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|a Methods in Molecular Biology
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5 |
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|a 10.1007/978-1-60327-475-3
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|u https://doi.org/10.1007/978-1-60327-475-3?nosfx=y
|x Verlag
|3 Volltext
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|a 572
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|a Due to the vital biological importance of RNA and proteins functioning together within a cell, a protocol volume describing experimental procedures to study their interactions should find a home in many laboratories. RNA-Protein Interaction Protocols, Second Edition updates, complements, and expands upon the popular first edition by providing a collection of cutting-edge techniques developed or refined in the past few years along with tried-and-true methods. The expert contributors explore the isolation and characterization of RNA-protein complexes, the analysis and measurement of RNA-protein interaction, and related novel techniques and strategies. Written in the highly successful Methods in Molecular Biology™ series format, the chapters include brief introductions to the material, lists of necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and a Notes section which highlights tips on troubleshooting and avoiding known pitfalls. Comprehensive and up-to-date, RNA-Protein Interaction Protocols, Second Edition is an ideal guide for researchers continuing the study of this all-important biological partnership
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