دورية أكاديمية

Glycosort: A Computational Solution to Post-process Quantitative Large-Scale Intact Glycopeptide Analyses.

التفاصيل البيبلوغرافية
العنوان: Glycosort: A Computational Solution to Post-process Quantitative Large-Scale Intact Glycopeptide Analyses.
المؤلفون: Lazari LC; Department of Parasitology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil., Santiago VF; Department of Parasitology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil., de Oliveira GS; Department of Parasitology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil., Mule SN; Department of Parasitology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil., Angeli CB; Department of Parasitology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil., Rosa-Fernandes L; Department of Parasitology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil.; Centre for Motor Neuron Disease Research, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University, Sydney, Australia., Palmisano G; Department of Parasitology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil. palmisano.gp@usp.br.; School of Natural Sciences, Faculty of Science and Engineering, Sydney, Australia. palmisano.gp@usp.br.
المصدر: Advances in experimental medicine and biology [Adv Exp Med Biol] 2024; Vol. 1443, pp. 23-32.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Kluwer Academic/Plenum Publishers Country of Publication: United States NLM ID: 0121103 Publication Model: Print Cited Medium: Print ISSN: 0065-2598 (Print) Linking ISSN: 00652598 NLM ISO Abbreviation: Adv Exp Med Biol Subsets: MEDLINE
أسماء مطبوعة: Publication: 1998- : New York : Kluwer Academic/Plenum Publishers
Original Publication: New York, Plenum Press.
مواضيع طبية MeSH: Glycopeptides* , Tandem Mass Spectrometry*, Software ; Glycosylation ; Polysaccharides/chemistry
مستخلص: Protein glycosylation is a post-translational modification involving the addition of carbohydrates to proteins and plays a crucial role in protein folding and various biological processes such as cell recognition, differentiation, and immune response. The vast array of natural sugars available allows the generation of plenty of unique glycan structures in proteins, adding complexity to the regulation and biological functions of glycans. The diversity is further increased by enzymatic site preferences and stereochemical conjugation, leading to an immense amount of different glycan structures. Understanding glycosylation heterogeneity is vital for unraveling the impact of glycans on different biological functions. Evaluating site occupancies and structural heterogeneity aids in comprehending glycan-related alterations in biological processes. Several software tools are available for large-scale glycoproteomics studies; however, integrating identification and quantitative data to assess heterogeneity complexity often requires extensive manual data processing. To address this challenge, we present a python script that automates the integration of Byonic and MaxQuant outputs for glycoproteomic data analysis. The script enables the calculation of site occupancy percentages by glycans and facilitates the comparison of glycan structures and site occupancies between two groups. This automated tool offers researchers a means to organize and interpret their high-throughput quantitative glycoproteomic data effectively.
(© 2024. The Author(s), under exclusive license to Springer Nature Switzerland AG.)
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فهرسة مساهمة: Keywords: Computational platform; Glycans; Glycoproteomics; Mass spectrometry; Quantitative analysis
المشرفين على المادة: 0 (Glycopeptides)
0 (Polysaccharides)
تواريخ الأحداث: Date Created: 20240227 Date Completed: 20240228 Latest Revision: 20240228
رمز التحديث: 20240228
DOI: 10.1007/978-3-031-50624-6_2
PMID: 38409414
قاعدة البيانات: MEDLINE
الوصف
تدمد:0065-2598
DOI:10.1007/978-3-031-50624-6_2