scholarly journals High resolution mass spectrometry imaging of plant tissues: towards a plant metabolite atlas

The Analyst ◽  
2015 ◽  
Vol 140 (22) ◽  
pp. 7696-7709 ◽  
Author(s):  
Dhaka Ram Bhandari ◽  
Qing Wang ◽  
Wolfgang Friedt ◽  
Bernhard Spengler ◽  
Sven Gottwald ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Mass Spectrometry Imaging ◽  
High Spatial Resolution ◽  
High Resolution Mass Spectrometry ◽  
Chemical Imaging ◽  
Plant Tissues ◽  
Label Free ◽  
Wide Range ◽  
Plant Metabolite ◽  
Resolution Mass

Label-free chemical imaging of a wide range of metabolites in all major plant organs acquired at high spatial resolution.

Perspective on Advances in Laser-Based High-Resolution Mass Spectrometry Imaging

2019 ◽  
Vol 92 (1) ◽  
pp. 543-553 ◽  
Author(s):  
Tongtong Wang ◽  
Xiaoling Cheng ◽  
Hexin Xu ◽  
Yifan Meng ◽  
Zhibin Yin ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
High Resolution ◽  
Mass Spectrometry Imaging ◽  
High Resolution Mass Spectrometry ◽  
High Resolution Mass ◽  
Resolution Mass

scholarly journals Quantification and Identification of Post-Translational Modifications Using Modern Proteomics

2021 ◽  
pp. 225-235
Author(s):  
Anja Holtz ◽  
Nathan Basisty ◽  
Birgit Schilling
Keyword(s):  
Mass Spectrometry ◽  
High Resolution ◽  
High Throughput ◽  
High Resolution Mass Spectrometry ◽  
Label Free ◽  
Post Translational Modifications ◽  
Data Independent Acquisition ◽  
Lysine Residues ◽  
Detailed Protocol ◽  
Resolution Mass

AbstractPost-translational modifications (PTMs) occur dynamically, allowing cells to quickly respond to changes in the environment. Lysine residues can be targeted by several modifications including acylations (acetylation, succinylation, malonylation, glutarylation, and others), methylation, ubiquitination, and other modifications. One of the most efficient methods for the identification of post-translational modifications is utilizing immunoaffinity enrichment followed by high-resolution mass spectrometry. This workflow can be coupled with comprehensive data-independent acquisition (DIA) mass spectrometry to be a high-throughput, label-free PTM quantification approach. Below we describe a detailed protocol to process tissue by homogenization and proteolytically digest proteins, followed by immunoaffinity enrichment of lysine-acetylated peptides to identify and quantify relative changes of acetylation comparing different conditions.

scholarly journals 6,6′-{[Ethane-1,2-diylbis(azaneylylidene)]bis(methaneylylidene)}bis[2-(hexyloxy)phenolato] Nickel(II)

Molbank ◽  
10.3390/m1174 ◽  
2020 ◽  
Vol 2020 (4) ◽  
pp. M1174
Author(s):  
Daniil A. Lukyanov ◽  
Anna S. Borisova ◽  
Oleg V. Levin
Keyword(s):  
Crystal Structure ◽  
Mass Spectrometry ◽  
Nuclear Magnetic Resonance ◽  
Fourier Transform ◽  
High Resolution Mass Spectrometry ◽  
Nickel Complexes ◽  
Polar Solvents ◽  
13C Nuclear Magnetic Resonance ◽  
Wide Range ◽  
Resolution Mass

Polymeric nickel complexes of salen ligands meet a wide range of applications in catalysis and electrochemistry. Because these polymers usually form very rigid films, the introduction of the conformationally flexible fragments in the corresponding monomers favors the amorphization and, thus, the mass transport. Herein we report a preparation of the hexyloxy-substituted monomeric NiSalen complex by the direct alkylation of the hydroxy-substituted complex. The resulting product was characterized by the 1H and 13C nuclear magnetic resonance (NMR), ESI-high resolution mass spectrometry (ESI-HRMS, and Fourier-transform infrared spectroscopy (FTIR). The crystal structure of the product was examined by an XRD, indicating the formation of the solvate with dichloromethane. The obtained product was found to be highly soluble in non-polar solvents, in contrast to typical NiSalens.

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