By Stefanie Mädler, Elisabetta Boeri Erba (auth.), Zongwei Cai, Shuying Liu (eds.)
MALDI-ToF Mass Spectrometry for learning Noncovalent Complexes of Biomolecules, via Stefanie Mädler, Elisabetta Boeri Erba, Renato Zenobi software of MALDI-TOF-Mass Spectrometry to Proteome research utilizing Stain-Free Gel Electrophoresis, by means of Iuliana Susnea, Bogdan Bernevic, Michael Wicke, Li Ma, Shuying Liu, Karl Schellander, Michael Przybylski MALDI Mass Spectrometry for Nucleic Acid research, via Xiang Gao, Boon-Huan Tan, Richard J. Sugrue, Kai Tang selection of Peptide and Protein Disulfide Linkages via MALDI Mass Spectrometry, by means of Hongmei Yang, Ning Liu, Shuying Liu MALDI In-Source Decay, from Sequencing to Imaging, via Delphine Debois, Nicolas Smargiasso, Kevin Demeure, Daiki Asakawa, Tyler A. Zimmerman, Loïc Quinton, Edwin De Pauw Advances of MALDI-TOF MS within the research of conventional chinese language medicinal drugs, by means of Minghua Lu, Zongwei Cai Chemical and Biochemical functions of MALDI TOF-MS in response to studying the Small natural Compounds, through Haoyang Wang, Zhixiong Zhao, Yinlong Guo Bioinformatic research of knowledge Generated from MALDI Mass Spectrometry for Biomarker Discovery, by means of Zengyou He, Robert Z. Qi, Weichuan Yu
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Additional resources for Applications of MALDI-TOF Spectroscopy
38 41 41 41 42 43 43 43 43 48 48 52 53 Abbreviations 1D 2D MALDI-TOF MS PMF SDS-PAGE One-dimensional gel electrophoresis Two-dimensional gel electrophoresis Matrix assisted laser desorption/ionization–time-of-flight Mass spectrometry Peptide mass fingerprinting Sodium dodecyl sulfate polyacrylamide gel electrophoresis 1 Introduction Matrix assisted laser desorption/ionization–mass spectrometry (MALDI-MS), introduced by Karas and Hillenkamp in 1988 [1, 2], is now widely used in proteomics studies.
Nat Protocol 2:119–130 34 S. M€adler et al. 166. Yanes O, Villanueva J, Querol E et al (2005) Functional screening of serine protease inhibitors in the medical leech Hirudo medicinalis monitored by intensity fading MALDITOF MS. Mol Cell Proteomics 4:1602–1613 167. Yanes O, Aviles FX, Roepstorff P et al (2007) Exploring the "intensity fading" phenomenon in the study of noncovalent interactions by MALDI-TOF mass spectrometry. J Am Soc Mass Spectrom 18:359–367 168. Shabab M, Kulkarni MJ, Khan MI (2008) Study of papain-cystatin interaction by intensity fading MALDI-TOF-MS.
Bich C, Scott M, Panagiotidis A et al (2008) Characterization of antibody-antigen interactions: comparison between surface plasmon resonance measurements and highmass matrix-assisted laser desorption/ionization mass spectrometry. Anal Biochem 375:35–45 106. Bovet C, Ruff M, Eiler S et al (2008) Monitoring ligand modulation of protein-protein interactions by mass spectrometry: estrogen receptor a-SRC1. Anal Chem 80:7833–7839 107. Yanes O, Nazabal A, Wenzel R et al (2006) Detection of noncovalent complexes in biological samples by intensity fading and high-mass detection MALDI-TOF mass spectrometry.
Applications of MALDI-TOF Spectroscopy by Stefanie Mädler, Elisabetta Boeri Erba (auth.), Zongwei Cai, Shuying Liu (eds.)