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Protein post-translational modifications : methods and protocols / edited by Xu Zhang, Rui Chen, Jianjun Li
- Format:
- Book
- Series:
- Methods in molecular biology (Clifton, N.J.) ; v. 3018.
- Springer protocols (Series)
- Methods in molecular biology, 1940-6029 ; 3018
- Springer protocols
- Language:
- English
- Subjects (All):
- Post-translational modification--Laboratory manuals.
- Post-translational modification.
- Proteins--Analysis--Laboratory manuals.
- Proteins.
- Proteins--Analysis.
- Physical Description:
- 1 online resource : illustrations
- illustration
- Place of Publication:
- New York, NY : Humana Press, [2026]
- Summary:
- "This detailed volume explores robust analytical workflows for post-translational modification (PTM) analysis in both basic and translational contexts. After brief foundational reviews of the field, the book delves into detailed experimental and computational protocols for traditional bottom-up strategies and top-down proteoform analysis, as well as PTM analysis of biotherapeutic proteins, reflecting the growing emphasis on PTMs as critical quality attributes in biologic drug development and regulation. Written for the highly successful Methods in Molecular Biology series, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step and readily reproducible laboratory protocols, and tips for troubleshooting and avoiding known pitfalls.Authoritative and practical, Protein Post-Translational Modifications: Methods and Protocols serves as a foundational and forward-looking resource to support and inspire continued exploration in this rapidly evolving field"-- Springer Nature Link
- Contents:
- An overview of mass spectrometry-based methods to analyze post-translational modifications / Rui Chen, Xu Zhang and Jianjun Li
- Post-translational modifications in protein therapeutics : Importance and analytical tools / Emily E. F. Fekete, Huixin Lu and Xu Zhang
- Decoding the SUMO proteome : A mass spectrometry workflow for site-specific identification / Chongyang Li and Pierre Thibault
- Computational pipelines for protein ubiquitylation analysis and prediction / Anastasiya Potapenko, Lyndal Henden, Ghasem Azemi, Antonio Di Ieva, Angela S. Laird, Roger Chung, Albert Lee and Jennilee M. Davidson
- Extensive characterization of N-glycosylation from major histocompatibility complex with hydrophilic interaction chromatography and mass spectrometry / Rui Chen
- Endogenous phosphopeptidomics analysis by using mesoporous IMAC materials / Ci Wu, Bing Liu and Junfeng Ma
- O- and N-phosphoproteomic analysis using online alkaline-pH reversed-phase nanoelectrospray-tandem mass spectrometry / Yuqui Wang, Minchu Tang and Wenfan Xie
- Phosphoproteomics protocol for the identification of novel biomarkers from extracellular vesicles of cancerous cells / Zoran Minic, Suttinee Poolsup, Yingxi Li, Rochelle D’Mello and Maxim V. Berezovski
- Mapping cellular protein lysine methylation using targeted-mass spectrometry / Anand Chopra, Matthew Hoekstra, William G. Willmore and Kyle K. Biggar
- Enrichment and metaproteomic analysis of lysine acetylation in fecal microbiome samples / Xu Zhang, Zhibin Ning and Daniel Figeys
- Generation of high-quality succinyl spectral libraries for improved proteome-wide succinylome analysis using data-independent acquisition / Alice Zhang, Birgit Schilling and Joanna Bons
- Combining SDS-PAGE with capillary zone electrophoresis-tandem mass spectrometry for top-down proteomics analysis of intact histone proteoforms / Fei Fang and Liangliang Sun
- PEPPI-SP3 : A gel-based high-resolution sample preparation workflow for in-depth top-down analysis of intact proteoforms by mass spectrometry / Ayako Takemori, Jake T. Kline, Luca Fornelli and Nobuaki Takemori
- Profiling O-acetylation in sialoglycans using MALDI-TOF and LC-MS/MS with methylamidation and permethylation derivatization / Zhaoguan Wu and Isabelle Sirois
- Purification of protein-free and protein-linked poly(ADP-ribose) from biochemical reactions and from human cells / Marie-France Langelier, Manja Mirhasan and John M. Pascal
- An NMR-based approach for global arginine methylation analysis / Tobias Huberts, Hansjörg Habisch and Tobias Madl
- Nanopore-based detection of protein posttranslational modifications / Meng-Yin Li, Yan Gao, Jie Jiang and Yi-Tao Long
- Mass spectrometry analysis of biotherapeutic monoclonal antibody glycosylation / Min Fang, Timothy R. Rudd and Gail C. Whiting
- Glycoengineering of monoclonal antibodies with homogeneous glycan isomers with asymmetric antennae / Roger Y. Tam, Grayson Hatfield and Lioudmila Tepliakova
- Deamidation analysis of biotherapeutic proteins by capillary electrophoresis-mass spectrometry / Yun Wang and Huixin Lu
- Notes:
- Includes bibliographical references and index
- Online resource; title from PDF title page (SpringerLink, viewed August 10, 2026).
- Other Format:
- Print version: Protein post-translational modifications
- ISBN:
- 9781071651667
- 1071651668
- OCLC:
- 1610821144
- Publisher Number:
- CIPO000366802
- Access Restriction:
- Restricted for use by site license
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