Mesoporous metal oxide nanoparticles for selective enrichment of phosphopeptides from complex sample matrices

Han, Meng; Li, Zhen

doi:10.1039/c6ay02069k

Cited by 8 publications

(3 citation statements)

References 28 publications

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“…The bound proteins were then eluted using TBS with 200 μL of FLAG peptide (300 ng/mL, Sigma, USA) and incubated for 1 h. The eluted protein was detected by anti-Flag antibody (Li et al 2011), and was used for MS analysis and RNA/DNA binding assay. MS analysis was performed as described (Han and Li 2016). The eluant was analyzed by liquid chromatography tandem mass spectrometry (LC-MS/MS) after digestion with trypsin .…”

Section: Affinity Protein Purification and Ms Analysismentioning

confidence: 99%

A glycine-rich protein MoGrp1 functions as a novel splicing factor to regulate fungal virulence and growth in Magnaporthe oryzae

et al. 2019

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Glycine-rich proteins (GRPs) have diverse amino acid sequences and are involved in a variety of biological processes. The role of GRPs in plant pathogenic fungi has not been reported. In this study, we identified and functionally characterized a novel gene named MoGRP1 in Magnaporthe oryzae, which encodes a protein that has an N-terminal RNA recognition motif (RRM) and a C-terminal glycine-rich domain with four Arg-Gly-Gly (RGG) repeats. Deletion of MoGRP1 resulted in dramatic reductions in fungal virulence, mycelial growth, and conidiation. The ΔMogrp1 mutants were also defective in cell wall integrity and in their responses to different stresses. MoGrp1 was localized to the nucleus and was co-immunoprecipitated with several components of the spliceosome, including subunits of the U1 snRNP and U2 snRNP complexes. Moreover, MoGrp1 exhibited binding affinity for poly(U). Importantly, MoGrp1 was responsible for the normal splicing of genes involved in infection-related morphogenesis. Domain deletion assays showed that both the RRM domain and its two adjacent RGG repeats were essential to the full function of MoGrp1. Notably, the nine amino acids between the first and the second RGG repeats were indispensable for nuclear localization and for the biological functions of MoGrp1. Taken together, our data suggest that MoGrp1 functions as a novel splicing factor with poly(U) binding activity to regulate fungal virulence, development, and stress responses in the rice blast fungus.

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Section: Affinity Protein Purification and Ms Analysismentioning

confidence: 99%

A glycine-rich protein MoGrp1 functions as a novel splicing factor to regulate fungal virulence and growth in Magnaporthe oryzae

et al. 2019

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“…Mesoporous nanomaterials, with tridimensional structures, high surface areas and numerous nanoscale pore channels, are widely utilized in phosphopeptides enrichment [31]. For instance, to enrich phosphopeptides from Hela cell extracts, hollow magnetic macro/mesoporous TiO 2 nanoparticles with large pore volume (0.52 cm 3 g −1 ) were synthesized, showing better selectivity and sensitivity for phosphopeptide when compared with hollow magnetic mesoporous TiO 2 with small pore volume (0.37 cm 3 g −1 ) and solid magnetic macro/mesoporous TiO 2 [32].…”

Section: Phosphoprotein/phosphopeptide Enrichment or Phosphate Recmentioning

confidence: 99%

Recent Advances in Protein Kinase Activity Analysis Based on Nanomaterials

Deng

Liu

2019

IJMS

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Protein phosphorylation regulated by protein kinases, as well as their dephosphorylation, is one of the most common post-translational modifications, and plays important roles in physiological activities, such as intracellular signal communications, gene transcription, cell proliferation and apoptosis. Over-expression of protein kinases is closely associated with various diseases. Consequently, accurate detection of protein kinases activities and their relevant inhibitors screening is critically important, not only to the biochemical research, but also to the clinical diagnosis and therapy. Nanomaterials, taking advantage of large surface areas, as well as excellent electrical, catalytic, magnetic and optical properties, have been utilized as target concentrators, recognition components, signal transducer or amplification elements in protein kinase related assays. This review summarizes the recent representative works to highlight the applications of nanomaterials in different biosensor technologies for protein kinases activities detection and their inhibitors screening. First, different nanomaterials developed for phosphoprotein/phosphopeptide enrichment and phosphate recognition are introduced. Next, representative works are selected that mainly focus on the utilization of nanomaterials as signal transducer or amplification elements in various protein kinases sensing platforms, such as electrochemical, colorimetric, fluorescent, and mass spectroscopy-based approaches. Finally, the major challenges and perspectives of nanomaterials being applied in protein kinases related assays are discussed.

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“…Surfaces of the materials such as titanium dioxide (TiO 2 ) and zirconium dioxide (ZrO 2 ) become positively charged at low pH, making them suitable for binding of phosphopeptides. TiO 2 is the most commonly used metal oxide in the phosphopeptide enrichment methods [20,35]. Oxides of various metals other than titanium are also used in the phosphopeptide enrichment studies [31,[36][37][38][39][40][41].…”

Section: Enrichment Of Phosphopeptides From the Mixture Of β-Casein/bsa Digestsmentioning

confidence: 99%

Sol‐Gel Materials Used in Phosphoproteomics and Glycoproteomics Applications

Kayili¹,

Atakay²,

Salih³

2017

Recent Applications in Sol-Gel Synthesis

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Glycosylation and phosphorylation are two of the most commonly seen and important post-translational modifications (PTMs) of proteins. Both play key role in many vital biological processes. Mass spectrometry is the most favored technique used for monitoring the dynamics of PTMs. Mass spectrometric analysis of phosphopeptide and glycopeptide is a crucial step in phosphoproteomics and glycoproteomics to understand the role of these modifications in the cellular pathways. Enrichment and purification of (phosphoand glyco-) peptides and glycans are recommended prior to mass spectrometric analysis because of the lower amount of modified peptides in a peptide mixture. Herein, we present titanium/silica and zirconium/silica sol-gel materials for the enrichment of (phospho-and glyco-) peptides and glycans to enhance MALDI-MS analysis performance. Enrichment of (phospho-and glyco-) peptides was successfully applied using standard proteins including β-casein, fetuin, and IgG as well as some complex medium. The solgel materials were compared with commercial metal oxides regarding their modified peptide enrichment performances.

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Mesoporous metal oxide nanoparticles for selective enrichment of phosphopeptides from complex sample matrices

Abstract: Selective enrichment of phosphopeptides using mesoporous metal oxide nanoparticles.

Cited by 8 publications

References 28 publications

A glycine-rich protein MoGrp1 functions as a novel splicing factor to regulate fungal virulence and growth in Magnaporthe oryzae

A glycine-rich protein MoGrp1 functions as a novel splicing factor to regulate fungal virulence and growth in Magnaporthe oryzae

Recent Advances in Protein Kinase Activity Analysis Based on Nanomaterials

Sol‐Gel Materials Used in Phosphoproteomics and Glycoproteomics Applications

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