國立高雄大學圖資館 |

登入

回首頁

UsingcDNA phage display for the direct cloning of cellular proteins and functional identification of natural product receptors.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	UsingcDNA phage display for the direct cloning of cellular proteins and functional identification of natural product receptors.
作者:	Sche, Paul Puh.
面頁冊數:	263 p.
附註:	Director: David J. Austin.
附註:	Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1233.
Contained By:	Dissertation Abstracts International64-03B.
標題:	Chemistry, Biochemistry.
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3084366
ISBN:	0496321730

UsingcDNA phage display for the direct cloning of cellular proteins and functional identification of natural product receptors.
Sche, Paul Puh.

UsingcDNA phage display for the direct cloning of cellular proteins and functional identification of natural product receptors. [electronic resource] - 263 p.

Director: David J. Austin.

Thesis (Ph.D.)--Yale University, 2003.

A procedure for the direct cloning of cellular proteins, based on their affinity for natural products, using cDNA phage display has been developed. The technique is referred to as Display Cloning because it involves the cloning of proteins displayed on the surface of a bacteriophage particle. The approach has been established by isolating a full-length gene clone of FKBP12 (FK506-binding protein) from a human brain cDNA library using a biotinylated FK506 probe molecule.

ISBN: 0496321730Subjects--Topical Terms:

226900
Chemistry, Biochemistry.

UsingcDNA phage display for the direct cloning of cellular proteins and functional identification of natural product receptors.
LDR:03203nmm _2200289 _450 001 161886
005 20051017073348.5
008 230606s2003 eng d
020 $a 0496321730
035 $a 00148387
035 $a 161886
040 $a UnM $c UnM
100 0 $a Sche, Paul Puh. $3 226974
245 1 0 $a UsingcDNA phage display for the direct cloning of cellular proteins and functional identification of natural product receptors. $h [electronic resource]
300 $a 263 p.
500 $a Director: David J. Austin.
500 $a Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1233.
502 $a Thesis (Ph.D.)--Yale University, 2003.
520 # $a A procedure for the direct cloning of cellular proteins, based on their affinity for natural products, using cDNA phage display has been developed. The technique is referred to as Display Cloning because it involves the cloning of proteins displayed on the surface of a bacteriophage particle. The approach has been established by isolating a full-length gene clone of FKBP12 (FK506-binding protein) from a human brain cDNA library using a biotinylated FK506 probe molecule.
520 # $a Many techniques have been developed to better understand biological mechanisms. Among them, cDNA Phage Display combines vitro genetic expression with traditional affinity chromatography and results in a direct link between the function of a protein and its gene sequence. To elucidate natural product receptors by utilizing their affinity towards their respective binding partners, Phage Display is a procedure that uses the expression, selection, and amplification of cDNA libraries of proteins on the surface coat protein of the bacteriophage, thus a direct linkage of phenotype to genotype is achieved.
520 # $a The development of Display Cloning greatly facilitates the investigation of ligand-receptor interaction biology and natural product mode of action studies. This procedure utilizes heterologous protein display on infectious phage, which allows the amplification and repeated selection of putative sequences, leading to unambiguous target identification. This direct connection of a functional protein to its gene sequence eliminates the subsequent cloning step required with tissue homogenate or cell lysate affinity methods, allowing direct isolation of an expressible gene sequence.
520 # $a The identification of cellular targets has traditionally been the starting point for natural product mode of action studies and has subsequently led to the understanding of many biological processes. Conventional experimental approaches have depended on cell-based screening and/or affinity chromatography. Although both of these techniques aid in the discovery of protein cellular targets, a method that couples both protein identification and gene isolation would be extremely valuable.
590 $a School code: 0265.
650 # 0 $a Chemistry, Biochemistry. $3 226900
710 0 # $a Yale University. $3 212430
773 0 # $g 64-03B. $t Dissertation Abstracts International
790 $a 0265
790 1 0 $a Austin, David J., $e advisor
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://libsw.nuk.edu.tw/login?url=http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3084366 $z http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3084366