Single stage repair of a giant inguinoscrotal hernia by a combined laparotomy and inguinal approach

Chen, Kerry L; Ong, Ferdinand; Phan‐Thien, Kim‐Chi

doi:10.1111/ans.17189

Cited by 3 publications

(2 citation statements)

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“…This migration pattern in CE is expected since the addition of a phosphate group to a peptide adds a negative charge to the peptide and acetylation at the N-terminus removes a positive charge, either of which leads to a decrease in the overall net charge of the peptide and consequently the effective mobility of the peptide in CE, a phenomenon that has been described in previous studies. 9,34 In data-dependent MS acquisition, this shift in modified peptide migration times helps increase the identification rate by separating phosphopeptides and Nterminal acetylated peptides from the bulk of other peptides. Both phosphorylated and acetylated peptides are known to show lower ionization efficiency than unmodified peptides (Figure S6).…”

Section: ■ Results and Discussionmentioning

confidence: 99%

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Capillary Electrophoresis Coupled to Electrospray Ionization Tandem Mass Spectrometry for Ultra-Sensitive Proteomic Analysis of Limited Samples

et al. 2022

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In this work, we developed an ultra-sensitive CE-MS/ MS method for bottom-up proteomics analysis of limited samples, down to sub-nanogram levels of total protein. Analysis of 880 and 88 pg of the HeLa protein digest standard by CE-MS/MS yielded ∼1100 ± 46 and ∼160 ± 59 proteins, respectively, demonstrating higher protein and peptide identifications than the current state-ofthe-art CE-MS/MS-based proteomic analyses with similar amounts of sample. To demonstrate potential applications of our ultrasensitive CE-MS/MS method for the analysis of limited biological samples, we digested 500 and 1000 HeLa cells using a miniaturized in-solution digestion workflow. From 1-, 5-, and 10-cell equivalents injected from the resulted digests, we identified 744 ± 127, 1139 ± 24, and 1271 ± 6 proteins and 3353 ± 719, 5709 ± 513, and 8527 ± 114 peptide groups, respectively. Furthermore, we performed a comparative assessment of CE-MS/MS and two reversed-phased nano-liquid chromatography (RP-nLC-MS/MS) methods (monolithic and packed columns) for the analysis of a ∼10 ng HeLa protein digest standard. Our results demonstrate complementarity in the protein-and especially peptide-level identifications of the evaluated CE-MS-and RP-nLC-MS-based methods. The techniques were further assessed to detect post-translational modifications and highlight the strengths of the CE-MS/ MS approach in identifying potentially important and biologically relevant modified peptides. With a migration window of ∼60 min, CE-MS/MS identified ∼2000 ± 53 proteins on average from a single injection of ∼8.8 ng of the HeLa protein digest standard. Additionally, an average of 232 ± 10 phosphopeptides and 377 ± 14 N-terminal acetylated peptides were identified in CE-MS/MS analyses at this sample amount, corresponding to 2-and 1.5-fold more identifications for each respective modification found by nLC-MS/MS methods.

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Section: ■ Results and Discussionmentioning

confidence: 99%

“…post-translational modifications (PTMs) that affect the charge of a peptide, such as phosphorylation, may cause a dramatic shift in electrophoretic mobility. 9,11 This shift can separate lowabundance, modified peptides from the bulk of the eluting peptides.…”

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confidence: 99%