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N-terminome Method Development

ABSTRACT: Developed a method to enrich N-terminome. Several parameters were change to optimization

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell, Cell Culture

SUBMITTER: Shinyeong Ju

LAB HEAD: Cheolju Lee

PROVIDER: PXD011117 | Pride | 2020-05-25

REPOSITORIES: Pride

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			Action	DRS
	161109_iNrich_161108_E01.msf	Msf
	161109_iNrich_161108_E01.msfView	Msf
	161109_iNrich_161108_E01.pdResult	Other
	161109_iNrich_161108_E01.pdResultView	Other
	161109_iNrich_161108_E01.raw	Raw

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Publications

iNrich, Rapid and Robust Method to Enrich N-Terminal Proteome in a Highly Multiplexed Platform.

Ju Shinyeong S Kwon Yumi Y Kim Jeong-Mok JM Park Daechan D Lee Seonjeong S Lee Jin-Won JW Hwang Cheol-Sang CS Lee Cheolju C

Analytical chemistry 20200421 9

The field of terminal proteomics is limited in that it is optimized for large-scale analysis via multistep processes involving liquid chromatography. Here, we present an integrated N-terminal peptide enrichment method (iNrich) that can handle as little as 25 μg of cell lysate via a single-stage encapsulated solid-phase extraction column. iNrich enables simple, rapid, and reproducible sample processing, treatment of a wide range of protein amounts (25 μg ∼ 1 mg), multiplexed parallel sample prepa ...[more]

PMID: 32267142

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N-terminome Method Development (Discovery)

Project description:Developed a method to enrich N-terminome. Several parameters were change to optimization. This project focused on the discovery of N-terminome.

2020-05-25 | PXD011141 | Pride

Naa10 mutant mouse N-terminome LC-MS

Project description:This project have LC-MSMS analysis results of label free quantitation of N-terminome enrichment of mouse proteome. N-terminal modification of mouse embryonic fibroblasts (MEFs) lacking Naa10 show negligible difference between wild-type and Naa10 mutant.

2021-08-18 | PXD026410 | Pride

tipNrich, a tip-based N-terminal proteome enrichment method

Project description:Protein N-termini provide valuable information such as half-life of protein, but one of hurdles to study N-terminome is that it requires large amount of sample, but this requirement might be problematic for analyzing the limited samples such as low number of cells of clinical biopsies. In this regard, we developed tip-based N-terminome enrichment method, tipNrich. Our method, the scale-down version of our previously introduced N-terminome enrichment method iNrich, provides simple and fast N-terminone analysis platform even for analyzing small amount of protein. Our method could be utilized either for quality check of protein products or as a diagnostic tool for human diseases related to N-terminal proteoforms. We applied our method to various recombinant single proteins, protein mixture, and plasma samples of wild-type transthyretin amyloidosis (WTTA) patients.

2022-12-05 | PXD027961 | Pride

Venom profiling of the insular species Bothrops alcatraz: characterization of proteome, glycoproteome, and N-terminome using Terminal Amine Isotopic Labeling of Substrates.

Project description:In this study we applied mass spectrometric approaches to characterize the proteome and glycoproteome of B. alcatraz venom, and to show for the first time the use of the TAILS method to profile a snake venom N-terminome.

2021-01-13 | PXD021561 | Pride

Hydrophobic tagging-assisted N-termini enrichment (HYTANE) for in-depth N-terminome analysis

Project description:The analysis of protein N-termini is of great importance for understanding the protein function and elucidating the proteolytic processing. Herein, we develop a negative enrichment strategy, termed as hydrophobic tagging-assisted N-termini enrichment (HYTANE) to achieve a global N-terminome analysis. The HYTANE strategy showed a high efficiency in hydrophobic tagging and C18 material-assisted depletion using bovine serum albumin (BSA) as the sample. Furthermore, this strategy was also applied to N-termini profiling from S. cerevisiaecell lysates and enabled the identification of 1096 protein N-termini, representing the largest N-terminome dataset of S. cerevisiae. The identified N-terminal peptides accounted for 99% of all identified peptides and no deficiency in acidic and histidine-containing N-terminal peptides was observed. The presented HYTANE strategy is therefore a highly selective, efficient and unbiased strategy for the large scale N-terminome analysis.

2016-08-19 | PXD004690 | Pride

Human “free-N-terminome” analysis

Project description:The high throughput characterization of protein N-termini is becoming an emerging challenge in the proteomics and proteogenomics fields. The present study describes the N-terminal oriented analysis of human mitochondria enriched samples by the trimethoxyphenyl phosphonium (TMPP) labeling approach (N-TOP and dN-TOP approaches (Gallien et al, 2009, Bertaccini et al. 2013)). The dN-TOP strategy based on a double light/heavy TMPP labeling has been optimized in order to improve and automate the workflow for efficient, fast and reliable high throughput N-terminome analysis.

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Human “free-N-terminome” analysis

2015-06-02 | PXD001521 | Pride

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2015-06-02 | PXD001523 | Pride

SAPT, a fast and efficient approach for simultaneous profiling of protein N- and C-terminome

Project description:Protein termini play pivotal roles in various biological processes. Although a series of terminomic strategies have been proposed for the analysis of protein N-termini or protein C-termini separately, few can analyze both ends of proteins at the same time. Herein, we developed a workflow, termed Simultaneous Analysis of Protein N- and C- Terminome (SAPT) based on strong cation exchange chromatography (SCX) to study protein terminome simultaneously.

2021-07-29 | PXD024573 | Pride

Human “free-N-terminome” analysis

| MSV000080204 | MassIVE