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Glycomic approaches to study post-translational modification by O-linked beta-N-acetylglucosamine (O-GlcNAc).

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
書名/作者:	Glycomic approaches to study post-translational modification by O-linked beta-N-acetylglucosamine (O-GlcNAc).
作者:	Wang, Zihao.
面頁冊數:	207 p.
附註:	Source: Dissertation Abstracts International, Volume: 69-12, Section: B, page: 7306.
Contained By:	Dissertation Abstracts International69-12B.
標題:	Biology, Molecular.
標題:	Chemistry, Biochemistry.
ISBN:	9780549939337
摘要、提要註:	The overall goal of my research projects is to understand the complex interplay between post-translational O-GlcNAc and O-Phosphate modifications. Like phosphorylation, O-GlcNAcylation is a one of the major forms of post-translational modification (PTM), and it has been found on numerous nuclear and cytoplasmic proteins that are involved in diverse cellular metabolism and function. Similar to phosphorylation, O-GlcNAcylation occurs on serine or threonine residues of the polypeptide backbones. O-GlcNAcylation is dynamic and has a high cycling rate on many proteins in response to various environmental stimuli. So far, many proteins have been found to be both O-GlcNAcylated and phosphorylated. The "yin-yang" hypothesis states that competition of O-GlcNAc and O-phosphate on the same serine or threonine residue may modulate the function of the protein. However, accumulating evidence has suggested this hypothesis as over-simplified. Global and systematic studies have been proposed and performed using mass spectrometry-based proteomics approaches in order to elucidate the complex interplay between the two abundant post translational modifications. An important aspect of studying post-translational modifications is to map the exact sites of the modifications. Mapping O-GlcNAc sites has been extremely difficult due to their intrinsic lability in the gas phase, low stoichiometry, and signal suppression. To solve this problem, new methods for O-GlcNAc enrichment and site-mapping are developed and optimized.
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3340017

Glycomic approaches to study post-translational modification by O-linked beta-N-acetylglucosamine (O-GlcNAc).
Wang, Zihao.

Glycomic approaches to study post-translational modification by O-linked beta-N-acetylglucosamine (O-GlcNAc). - 207 p.

Source: Dissertation Abstracts International, Volume: 69-12, Section: B, page: 7306.

Thesis (Ph.D.)--The Johns Hopkins University, 2009.

The overall goal of my research projects is to understand the complex interplay between post-translational O-GlcNAc and O-Phosphate modifications. Like phosphorylation, O-GlcNAcylation is a one of the major forms of post-translational modification (PTM), and it has been found on numerous nuclear and cytoplasmic proteins that are involved in diverse cellular metabolism and function. Similar to phosphorylation, O-GlcNAcylation occurs on serine or threonine residues of the polypeptide backbones. O-GlcNAcylation is dynamic and has a high cycling rate on many proteins in response to various environmental stimuli. So far, many proteins have been found to be both O-GlcNAcylated and phosphorylated. The "yin-yang" hypothesis states that competition of O-GlcNAc and O-phosphate on the same serine or threonine residue may modulate the function of the protein. However, accumulating evidence has suggested this hypothesis as over-simplified. Global and systematic studies have been proposed and performed using mass spectrometry-based proteomics approaches in order to elucidate the complex interplay between the two abundant post translational modifications. An important aspect of studying post-translational modifications is to map the exact sites of the modifications. Mapping O-GlcNAc sites has been extremely difficult due to their intrinsic lability in the gas phase, low stoichiometry, and signal suppression. To solve this problem, new methods for O-GlcNAc enrichment and site-mapping are developed and optimized.

ISBN: 9780549939337Subjects--Topical Terms:

422925
Biology, Molecular.

Glycomic approaches to study post-translational modification by O-linked beta-N-acetylglucosamine (O-GlcNAc).
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