東華大學圖書館 |

Language: English

Help

回圖書館首頁

手機版館藏查詢

Back

Switch To: Labeled | MARC Mode | ISBD

Identification and Characterization ...

Schneider, Kyle D.

Linked to FindBook

Google Book

Amazon

博客來

Identification and Characterization of Kinase-Docking Interactions.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Identification and Characterization of Kinase-Docking Interactions./
Author:	Schneider, Kyle D.
Description:	122 p.
Notes:	Source: Dissertation Abstracts International, Volume: 77-05(E), Section: B.
Contained By:	Dissertation Abstracts International77-05B(E).
Subject:	Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3741344
ISBN:	9781339336251

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:

518028
Biochemistry.

Identification and Characterization of Kinase-Docking Interactions.
LDR:02597nmm a2200289 4500 001 2068143
005 20160422125051.5
008 170521s2015 ||||||||||||||||| ||eng d
020 $a 9781339336251
035 $a (MiAaPQ)AAI3741344
035 $a AAI3741344
040 $a MiAaPQ $c MiAaPQ
100 1 $a Schneider, Kyle D. $3 3183055
245 1 0 $a Identification and Characterization of Kinase-Docking Interactions.
300 $a 122 p.
500 $a Source: Dissertation Abstracts International, Volume: 77-05(E), Section: B.
500 $a Adviser: Eric L. Weiss.
502 $a Thesis (Ph.D.)--Northwestern University, 2015.
520 $a 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.
590 $a School code: 0163.
650 4 $a Biochemistry. $3 518028
650 4 $a Cellular biology. $3 3172791
650 4 $a Biology. $3 522710
690 $a 0487
690 $a 0379
690 $a 0306
710 2 $a Northwestern University. $b Integrated Graduate Program in the Life Sciences. $3 1682749
773 0 $t Dissertation Abstracts International $g 77-05B(E).
790 $a 0163
791 $a Ph.D.
792 $a 2015
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3741344