2023
DOI: 10.1016/j.cclet.2022.07.059
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Probing region-resolved heterogeneity of phosphoproteome in human lens by hybrid metal organic frameworks

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Cited by 17 publications
(11 citation statements)
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“…The mixture was treated at 100 °C for 10 min and then cooled to room temperature and treated with trypsin (1:40, w/w) at 37 °C for 16 h. All trypsin digests obtained were stored at −20 °C for later use. 34 30 μL of skim milk or human saliva was dissolved in 1 mL of NH 4 HCO 3 buffer (50 mM, pH = 8.3). The mixture was treated at 100 °C for 10 min and cooled to room temperature and then treated with trypsin (1:40, w/w) at 37 °C for 16 h. The obtained trypsin digest was stored at −20 °C for later use.…”
Section: ■ Experimental Sectionmentioning
confidence: 99%
See 1 more Smart Citation
“…The mixture was treated at 100 °C for 10 min and then cooled to room temperature and treated with trypsin (1:40, w/w) at 37 °C for 16 h. All trypsin digests obtained were stored at −20 °C for later use. 34 30 μL of skim milk or human saliva was dissolved in 1 mL of NH 4 HCO 3 buffer (50 mM, pH = 8.3). The mixture was treated at 100 °C for 10 min and cooled to room temperature and then treated with trypsin (1:40, w/w) at 37 °C for 16 h. The obtained trypsin digest was stored at −20 °C for later use.…”
Section: ■ Experimental Sectionmentioning
confidence: 99%
“…1 mg of β-casein and 5 mg of bovine serum albumin (BSA) were dissolved in 1 mL of NH 4 HCO 3 buffer (50 mM, pH = 8.3). The mixture was treated at 100 °C for 10 min and then cooled to room temperature and treated with trypsin (1:40, w/w) at 37 °C for 16 h. All trypsin digests obtained were stored at −20 °C for later use 34. 30 μL of skim milk or human saliva was dissolved in 1 mL of NH 4 HCO 3 buffer (50 mM, pH = 8.3).…”
mentioning
confidence: 99%
“…2 Abnormal glycosylation and phosphorylation are popularly applied in clinical proteomics studies and biomarker discovery related to diseases. [3][4][5] It has been discovered that several human diseases, such as cancers and neurodegenerative diseases, are intimately related to abnormal glycosylation and phosphorylation. [6][7][8] Until now, research work has concentrated on the individual functions of glycosylation or phosphorylation in cellular activity.…”
Section: Introductionmentioning
confidence: 99%
“…Protein phosphorylation, as an important mechanism, is known for regulating various cellular functions as well as some diseases like Alzheimer’s disease and cancer. Identifying and comprehensively mapping phosphorylation by mass spectrometry (MS) techniques are crucial for understanding the etiology and pathogenesis of these diseases. , However, the variability and complexity of phosphoproteins have presented many difficulties for direct MS analysis. , The enrichment strategy has become one of the bottlenecks in proteomics research.…”
Section: Introductionmentioning
confidence: 99%
“…4,5 However, the variability and complexity of phosphoproteins have presented many difficulties for direct MS analysis. 6,7 The enrichment strategy has become one of the bottlenecks in proteomics research.…”
Section: Introductionmentioning
confidence: 99%