دورية أكاديمية
أعرض في EDS

A metabolic alkene reporter for spatiotemporally controlled imaging of newly synthesized proteins in Mammalian cells.

التفاصيل البيبلوغرافية
العنوان: A metabolic alkene reporter for spatiotemporally controlled imaging of newly synthesized proteins in Mammalian cells.
المؤلفون: Song W; Department of Chemistry, State University of New York at Buffalo, 14260, USA., Wang Y, Yu Z, Vera CI, Qu J, Lin Q
المصدر: ACS chemical biology [ACS Chem Biol] 2010 Sep 17; Vol. 5 (9), pp. 875-85.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: American Chemical Society Country of Publication: United States NLM ID: 101282906 Publication Model: Print Cited Medium: Internet ISSN: 1554-8937 (Electronic) Linking ISSN: 15548929 NLM ISO Abbreviation: ACS Chem Biol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, D.C. : American Chemical Society, c2006-
مواضيع طبية MeSH: Protein Biosynthesis*, Allylglycine/*analysis , Allylglycine/*metabolism , Proteins/*analysis , Proteins/*metabolism, Allylglycine/chemistry ; Amino Acid Sequence ; Animals ; Flow Cytometry ; HeLa Cells ; Humans ; Microscopy, Fluorescence ; Molecular Sequence Data ; Proteins/chemistry
مستخلص: The nonsymmetrical spatial distribution of newly synthesized proteins in animal cells plays a central role in many cellular processes. Here, we report that a simple alkene tag, homoallylglycine (HAG), was co-translationally incorporated into a recombinant protein as well as endogenous, newly synthesized proteins in mammalian cells with high efficiency. In conjunction with a photoinduced tetrazole-alkene cycloaddition reaction ("photoclick chemistry"), this alkene tag further served as a bioorthogonal chemical reporter both for the selective protein functionalization in vitro and for a spatiotemporally controlled imaging of the newly synthesized proteins in live mammalian cells. This two-step metabolic alkene tagging-photocontrolled chemical functionalization approach may offer a potentially useful tool to study the role of spatiotemporally regulated protein synthesis in mammalian cells.
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معلومات مُعتمدة: R01 GM085092 United States GM NIGMS NIH HHS; R01 GM085092-02 United States GM NIGMS NIH HHS; GM85092 United States GM NIGMS NIH HHS
المشرفين على المادة: 0 (Proteins)
1069-48-3 (Allylglycine)
تواريخ الأحداث: Date Created: 20100730 Date Completed: 20110118 Latest Revision: 20211020
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC2942984
DOI: 10.1021/cb100193h
PMID: 20666508
قاعدة البيانات: MEDLINE
الوصف
تدمد:1554-8937
DOI:10.1021/cb100193h