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Identification and Characterization of Kinase-Docking Interactions.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
書名/作者:	Identification and Characterization of Kinase-Docking Interactions.
作者:	Schneider, Kyle D.
面頁冊數:	122 p.
附註:	Source: Dissertation Abstracts International, Volume: 77-05(E), Section: B.
Contained By:	Dissertation Abstracts International77-05B(E).
標題:	Biochemistry.
標題:	Cellular biology.
標題:	Biology.
ISBN:	9781339336251
摘要、提要註:	Cell signaling networks coordinate the proper function and processes of living cells. When these systems are disrupted severe diseases such as cancer can result, highlighting the importance of understanding them in healthy and diseased cells. An incompletely understood component underlying cell signaling networks is a class of physical interactions in which stably folded protein domains associate with short amino acid motifs in other proteins. While a number of well-studied cases show that such short linear motifs ("SLiMs") can coordinate the proper function of signaling systems, it is unclear how many kinds of motifs eukaryotic cells use. My research explores the hypothesis that as-yet unrecognized SLiM associations are widespread in signaling pathways. I describe identification and biochemical characterization of a peptide motif that engages in docking interaction with a highly conserved budding yeast protein kinase. This docking motif is present in the kinase's known in vivo phosphorylation targets, and it predicts previously uncharacterized substrates involved in the process of cell separation. I also describe proteome-scale phage display technologies to identify novel linear motif interactions with a diverse set of yeast and human kinases. Experiments using this approach identified potential peptide motif docking interactions for several of these kinases, and demonstrated that peptide phage display can detect interactions of modest affinity. This work has helped to identify and characterize elusive, transient linear motif interactions between kinases and substrates, and developed a high-throughput approach for the identification of micromolar affinity protein-peptide interactions.
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3741344

Identification and Characterization of Kinase-Docking Interactions.
Schneider, Kyle D.

Identification and Characterization of Kinase-Docking Interactions. - 122 p.

Source: Dissertation Abstracts International, Volume: 77-05(E), Section: B.

Thesis (Ph.D.)--Northwestern University, 2015.

Cell signaling networks coordinate the proper function and processes of living cells. When these systems are disrupted severe diseases such as cancer can result, highlighting the importance of understanding them in healthy and diseased cells. An incompletely understood component underlying cell signaling networks is a class of physical interactions in which stably folded protein domains associate with short amino acid motifs in other proteins. While a number of well-studied cases show that such short linear motifs ("SLiMs") can coordinate the proper function of signaling systems, it is unclear how many kinds of motifs eukaryotic cells use. My research explores the hypothesis that as-yet unrecognized SLiM associations are widespread in signaling pathways. I describe identification and biochemical characterization of a peptide motif that engages in docking interaction with a highly conserved budding yeast protein kinase. This docking motif is present in the kinase's known in vivo phosphorylation targets, and it predicts previously uncharacterized substrates involved in the process of cell separation. I also describe proteome-scale phage display technologies to identify novel linear motif interactions with a diverse set of yeast and human kinases. Experiments using this approach identified potential peptide motif docking interactions for several of these kinases, and demonstrated that peptide phage display can detect interactions of modest affinity. This work has helped to identify and characterize elusive, transient linear motif interactions between kinases and substrates, and developed a high-throughput approach for the identification of micromolar affinity protein-peptide interactions.

ISBN: 9781339336251Subjects--Topical Terms:

183428
Biochemistry.

Identification and Characterization of Kinase-Docking Interactions.
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