دورية أكاديمية
أعرض في EDS

Affinity and chemical enrichment strategies for mapping low-abundance protein modifications and protein-interaction networks.

التفاصيل البيبلوغرافية
العنوان: Affinity and chemical enrichment strategies for mapping low-abundance protein modifications and protein-interaction networks.
المؤلفون: Zacharias AO; Department of Chemistry and Biochemistry, University of Texas at Arlington, Arlington, Texas, USA., Fang Z; Department of Chemistry and Biochemistry, University of Texas at Arlington, Arlington, Texas, USA., Rahman A; Department of Chemistry and Biochemistry, University of Texas at Arlington, Arlington, Texas, USA., Talukder A; Department of Chemistry and Biochemistry, University of Texas at Arlington, Arlington, Texas, USA., Cornelius S; Department of Chemistry and Biochemistry, University of Texas at Arlington, Arlington, Texas, USA., Chowdhury SM; Department of Chemistry and Biochemistry, University of Texas at Arlington, Arlington, Texas, USA.
المصدر: Journal of separation science [J Sep Sci] 2021 Jan; Vol. 44 (1), pp. 310-322. Date of Electronic Publication: 2020 Dec 14.
نوع المنشور: Journal Article; Review
اللغة: English
بيانات الدورية: Publisher: Wiley-VCH Country of Publication: Germany NLM ID: 101088554 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1615-9314 (Electronic) Linking ISSN: 16159306 NLM ISO Abbreviation: J Sep Sci Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Weinheim, Germany : Wiley-VCH, c2001-
مواضيع طبية MeSH: Protein Interaction Maps*, Proteins/*chemistry , Proteins/*metabolism, Arginine/chemistry ; Arginine/metabolism ; Protein Processing, Post-Translational
مستخلص: Protein post-translational modifications and protein interactions are the central research areas in mass-spectrometry-based proteomics. Protein post-translational modifications affect protein structures, stabilities, activities, and all cellular processes are achieved by interactions among proteins and protein complexes. With the continuing advancements of mass spectrometry instrumentations of better sensitivity, speed, and performance, selective enrichment of modifications/interactions of interest from complex cellular matrices during the sample preparation has become the overwhelming bottleneck in the proteomics workflow. Therefore, many strategies have been developed to address this issue by targeting specific modifications/interactions based on their physical properties or chemical reactivities, but only a few have been successfully applied for systematic proteome-wide study. In this review, we summarized the highlights of recent developments in the affinity enrichment methods focusing mainly on low stoichiometric protein lipidations. Besides, to identify potential glyoxal modified arginines, a small part was added for profiling reactive arginine sites using an enrichment reagent. A detailed section was provided for the enrichment of protein interactions by affinity purification and chemical cross-linking, to shed light on the potentials of different enrichment strategies, along with the unique challenges in investigating individual protein post-translational modification or protein interaction network.
(© 2020 Wiley-VCH GmbH.)
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فهرسة مساهمة: Keywords: Affinity Purification-Mass Spectrometry; Cross-linking Mass Spectrometry; Post-translational modifications; Prenylations; Protein Interaction Networks
المشرفين على المادة: 0 (Proteins)
94ZLA3W45F (Arginine)
تواريخ الأحداث: Date Created: 20201208 Date Completed: 20210920 Latest Revision: 20210920
رمز التحديث: 20240628
DOI: 10.1002/jssc.202000930
PMID: 33289315
قاعدة البيانات: MEDLINE
الوصف
تدمد:1615-9314
DOI:10.1002/jssc.202000930