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Titlebook: Analysis of Post-Translational Modifications and Proteolysis in Neuroscience; Jennifer Elizabeth Grant,Hong Li Book 2016 Springer Science+

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發(fā)表于 2025-3-21 18:18:54 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
期刊全稱Analysis of Post-Translational Modifications and Proteolysis in Neuroscience
影響因子2023Jennifer Elizabeth Grant,Hong Li
視頻videohttp://file.papertrans.cn/157/156421/156421.mp4
發(fā)行地址Includes cutting-edge methods and protocols.Provides step-by-step detail essential for reproducible results.Contains key notes and implementation advice from the experts
學(xué)科分類Neuromethods
圖書封面Titlebook: Analysis of Post-Translational Modifications and Proteolysis in Neuroscience;  Jennifer Elizabeth Grant,Hong Li Book 2016 Springer Science+
影響因子.This volume highlights proteomics studies of quantitative PTM changes in both peripheral and central nervous system proteomes utilizing the most recent advances in mass spectrometry. Chapters include practical information pertaining to the fundamentals of sample preparation, liquid chromatography, and tandem mass spectrometry instrumental analysis and will elucidate best practices in the interpretation of data using modern bioinformatics approaches. Written for the popular .Neuromethods.?series, chapters include the kind of detail and key implementation advice that ensures successful results in the laboratory...Authoritative and practical,?.Analysis of Post-Translational Modifications and Proteolysis in Neuroscience .aims.?.to ensure successful results in the further study of this vital field..
Pindex Book 2016
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A Boronic Acid-Based Enrichment for Site-Specific Identification of the N-glycoproteome Using MS-Baides are removed. By virtue of the universal boronic acid-diol recognition, large-scale mapping of N-glycoproteins can be achieved by combining boronic acid-based enrichment, PNGase F treatment in the presence of heavy oxygen (.O) water, and MS analysis. This method can be extensively applied for th
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Phosphoproteomics of Tyrosine Kinases in the Nervous System,growth factor (NGF), after a period of 1–2?min. The identification of the modified residue and its location in the sequence of the peptide can be determined following collision induced dissociation of the precursor peptide in the mass spectrometer and the observation of fragment ions that frame the
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Identification of Protease Substrates in Complex Proteomes by iTRAQ-TAILS on a Thermo Q Exactive Ininates the need for laborious follow-up experiments like Edman sequencing. iTRAQ-TAILS acquires this rich information by exploiting the power of latest generation mass spectrometers as the Thermo Q Exactive instrument. Through quantitative assessment of protein N-termini in protease-exposed and cont
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Identification and Characterization of Protein Posttranslational Modifications by Differential Fluotwo goals in mind, first to share with other scientists some of our experiences in this field, and second to invite those interested in the subject to bring their own contributions to an area that should be further explored and enhanced in order to create a large tool kit for PTM analysis. Although
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