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Tytuł pozycji:

Detection and Analysis of Proteins Modified by O-Linked N-Acetylglucosamine.

Tytuł:
Detection and Analysis of Proteins Modified by O-Linked N-Acetylglucosamine.
Autorzy:
Fahie K; The Johns Hopkins University School of Medicine, Baltimore, Maryland.
Narayanan B; The Johns Hopkins University School of Medicine, Baltimore, Maryland.
Zahra F; The Johns Hopkins University School of Medicine, Baltimore, Maryland.
Reeves R; The Johns Hopkins University School of Medicine, Baltimore, Maryland.; Current address: Department of Radiology, Thomas Jefferson University Hospital, Philadelphia, Pennsylvania.
Fernandes SM; The Johns Hopkins University School of Medicine, Baltimore, Maryland.
Hart GW; Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia.
Zachara NE; The Johns Hopkins University School of Medicine, Baltimore, Maryland.
Źródło:
Current protocols [Curr Protoc] 2021 May; Vol. 1 (5), pp. e129.
Typ publikacji:
Journal Article
Język:
English
Imprint Name(s):
Original Publication: Hoboken, NJ : John Wiley & Sons, [2021]-
MeSH Terms:
Acetylglucosamine*/metabolism
Diabetes Mellitus, Type 2*/metabolism
Cell Nucleus/metabolism ; Glycosylation ; Humans ; Protein Processing, Post-Translational
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Grant Information:
U01 CA230978 United States CA NCI NIH HHS; K12 HL141952 United States HL NHLBI NIH HHS; K12HL141952 United States NH NIH HHS; RO1HL139640 United States NH NIH HHS; R01 HL139640 United States HL NHLBI NIH HHS; U01 CA230978 United States NH NIH HHS
Contributed Indexing:
Keywords: O-GlcNAc; O-linked; analysis; detection; galactosyltransferase; glycosylation; signal transduction
Substance Nomenclature:
V956696549 (Acetylglucosamine)
Entry Date(s):
Date Created: 20210518 Date Completed: 20210616 Latest Revision: 20220503
Update Code:
20240104
PubMed Central ID:
PMC8862748
DOI:
10.1002/cpz1.129
PMID:
34004049
Czasopismo naukowe
O-GlcNAc is a common post-translational modification of nuclear, mitochondrial, and cytoplasmic proteins that regulates normal physiology and the cell stress response. Dysregulation of O-GlcNAc cycling is implicated in the etiology of type II diabetes, heart failure, hypertension, and Alzheimer's disease, as well as cardioprotection. These protocols cover simple and comprehensive techniques for detecting proteins modified by O-GlcNAc and studying the enzymes that add or remove O-GlcNAc. © 2021 The Authors. Current Protocols published by Wiley Periodicals LLC. Basic Protocol 1: Increasing the stoichiometry of O-GlcNAc on proteins before analysis Basic Protocol 2: Detection of proteins modified by O-GlcNAc using antibodies Basic Protocol 3: Detection of proteins modified by O-GlcNAc using the lectin sWGA Support Protocol 1: Control for O-linked glycosylation Basic Protocol 4: Detection and enrichment of proteins using WGA-agarose Support Protocol 2: Digestion of proteins with hexosaminidase Alternate Protocol: Detection of proteins modified by O-GlcNAc using galactosyltransferase Support Protocol 3: Autogalactosylation of galactosyltransferase Support Protocol 4: Assay of galactosyltransferase activity Basic Protocol 5: Characterization of labeled glycans by β-elimination and chromatography Basic Protocol 6: Detection of O-GlcNAc in 96-well plates Basic Protocol 7: Assay for OGT activity Support Protocol 5: Desalting of O-GlcNAc transferase Basic Protocol 8: Assay for O-GlcNAcase activity.
(© 2021 The Authors. Current Protocols published by Wiley Periodicals LLC.)

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