| 000 | 03715nam a22003615i 4500 | ||
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| 005 | 20221220020646.0 | ||
| 007 | cr nn 008mamaa | ||
| 008 | 150430s2015 xxu| s |||| 0|eng d | ||
| 020 | _a9781493926480 | ||
| 024 | 7 |
_a10.1007/978-1-4939-2648-0 _2doi |
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| 040 |
_aES-MaUEC _bspa _cES-MaUEC |
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| 245 | 1 | 0 |
_aPlant Phosphoproteomics _bMethods and Protocols _cedited by Waltraud X. Schulze. |
| 250 | _a1st edition 2015 | ||
| 264 | 1 |
_aNew York, NY _bSpringer International Publishing _c2015 |
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| 300 |
_a1 recurso en línea (X, 231 páginas) _b24 ilustraciones, 16 ilustraciones a color |
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| 336 |
_atexto _btxt _2rdacontent |
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| 337 |
_aelectrónico _bc _2rdamedia |
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| 338 |
_arecurso electrónico _bcr _2rdacarrier |
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| 347 |
_aarchivo de texto _bPDF |
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| 490 | 0 |
_aMethods in Molecular Biology _x1940-6029 _v1306 |
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| 505 | 0 | _aThe Plant Kinome -- Phosphatases in Plants -- Phosphoproteomics in Cereals -- Screening of Kinase Substrates Using Kinase-Knockout Mutants -- Phosphopeptide Profiling of Receptor Kinase Mutants -- Combining Metabolic 15N Labelling with Improved TandemMOAC for Enhanced Probing of the Phosphoproteome -- Kinase Activity and Specificity Assay Using Synthetic Peptides -- Absolute Quantitation of Protein Post-Translational Modification Isoform -- Phosphorylation Stoichiometry Determination in Plant Photosynthetic Membranes -- Phosphopeptide Immuno-Affinity Enrichment to Enhance Detection of Tyrosine Phosphorylation in Plants -- The Peptide Microarray ChloroPhos1.0: A Screening Tool for the Identification of Arabidopsis thaliana Chloroplast Protein Kinase Substrates -- Plant Protein Kinase Substrates Identification Using Protein Microarrays -- Targeted Analysis of Protein Phosphorylation by 2D Electrophoresis -- Computational Phosphorylation Network Reconstruction: Methods and Resources -- Computational Identification of Protein Kinases and Kinase-Specific Substrates in Plants -- Databases for Plant Phosphoproteomics -- Phosphorylation Site Prediction in Plants. | |
| 520 | _aThis detailed volume addresses recent developments in phosphoproteomic techniques with a particular focus on the plant system. Over the recent decades, proteomic methods were refined to study the significance and dynamics of protein phosphorylation in various biological contexts. However, working with plant tissue imposes particular challenges to the biologist which are attributed to the rigid cell wall making protein extraction more difficult, the skewed protein abundance with Rubisco as a highly abundant protein, and a large central vacuole leading to low protein yield and increased degradative enzyme activity. The methodologies in this book seek to move beyond these issues. Written for the Methods in Molecular Biology series, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Practical and authoritative, Plant Phosphoproteomics: Methods and Protocols serves as an ideal reference for researchers investigating this vital area of plant science. | ||
| 700 | 1 |
_aSchulze, Waltraud X _eeditor literario _4edt _4http://id.loc.gov/vocabulary/relators/edt |
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| 776 | 0 | 8 |
_iPrinted edition: _z9781493926473 |
| 776 | 0 | 8 |
_iPrinted edition: _z9781493926497 |
| 776 | 0 | 8 |
_iPrinted edition: _z9781493949373 |
| 856 | 4 | 0 |
_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1007/978-1-4939-2648-0 _z(usuarios Universidad Europea de Valencia) |
| 942 |
_2lcc _cLE |
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| 988 | _aSpringer_Protocols_2015 | ||
| 999 |
_c235135 _d235135 |
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