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

S-nitrosylated glyceraldehyde-3-phos...

Hara, Makoto.

Linked to FindBook

Google Book

Amazon

博客來

S-nitrosylated glyceraldehyde-3-phosphate dehydrogenase initiates apoptotic cell death by nuclear translocation following Siah1 binding.

Record Type:	Electronic resources : Monograph/item
Title/Author:	S-nitrosylated glyceraldehyde-3-phosphate dehydrogenase initiates apoptotic cell death by nuclear translocation following Siah1 binding./
Author:	Hara, Makoto.
Description:	78 p.
Notes:	Source: Dissertation Abstracts International, Volume: 66-11, Section: B, page: 5836.
Contained By:	Dissertation Abstracts International66-11B.
Subject:	Biology, Neuroscience. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3197160
ISBN:	9780542429729

S-nitrosylated glyceraldehyde-3-phosphate dehydrogenase initiates apoptotic cell death by nuclear translocation following Siah1 binding.
Hara, Makoto.

S-nitrosylated glyceraldehyde-3-phosphate dehydrogenase initiates apoptotic cell death by nuclear translocation following Siah1 binding. - 78 p.

Source: Dissertation Abstracts International, Volume: 66-11, Section: B, page: 5836.

Thesis (Ph.D.)--The Johns Hopkins University, 2006.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a classical glycolytic protein known for its pivotal role in energy production. Recent evidence demonstrates that mammalian GAPDH displays a number of diverse activities unrelated to its glycolytic function, including its possible role in apoptosis. Our laboratory has found that GAPDH translocates to the nucleus following a wide range of apoptotic stimuli1. Antisense oligonucleotides targeted to GAPDH decrease nuclear GAPDH and prevent cell death. This thesis attempts to study a mechanism underlying this nuclear translocation and cytotoxicity. GAPDH, which lacks a nuclear localization signal (NLS), bind to the NLS-containing protein Siahl (an E3-ubiquitin-ligase), which mediates GAPDH's nuclear translocation. Nitric oxide (NO) generation following apoptotic stimulation elicits S-nitrosylation of GAPDH, which augments its binding to Siahl. GAPDH stabilizes Siahl facilitating its degradation of nuclear proteins. Activation of macrophages by endotoxin and of neurons by glutamate elicits GAPDH-Siahl binding, nuclear translocation and apoptosis, which are prevented by NO deletion. The NO-S-nitrosylation-GAPDH-Siahl cascade may represent a major molecular mechanism of cytotoxicity.

ISBN: 9780542429729Subjects--Topical Terms:

1017680
Biology, Neuroscience.

S-nitrosylated glyceraldehyde-3-phosphate dehydrogenase initiates apoptotic cell death by nuclear translocation following Siah1 binding.
LDR:02246nmm 2200301 4500 001 1824127
005 20061128082943.5
008 130610s2006 eng d
020 $a 9780542429729
035 $a (UnM)AAI3197160
035 $a AAI3197160
040 $a UnM $c UnM
100 1 $a Hara, Makoto. $3 1913218
245 1 0 $a S-nitrosylated glyceraldehyde-3-phosphate dehydrogenase initiates apoptotic cell death by nuclear translocation following Siah1 binding.
300 $a 78 p.
500 $a Source: Dissertation Abstracts International, Volume: 66-11, Section: B, page: 5836.
500 $a Adviser: Solomon H. Snyder.
502 $a Thesis (Ph.D.)--The Johns Hopkins University, 2006.
520 $a Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a classical glycolytic protein known for its pivotal role in energy production. Recent evidence demonstrates that mammalian GAPDH displays a number of diverse activities unrelated to its glycolytic function, including its possible role in apoptosis. Our laboratory has found that GAPDH translocates to the nucleus following a wide range of apoptotic stimuli1. Antisense oligonucleotides targeted to GAPDH decrease nuclear GAPDH and prevent cell death. This thesis attempts to study a mechanism underlying this nuclear translocation and cytotoxicity. GAPDH, which lacks a nuclear localization signal (NLS), bind to the NLS-containing protein Siahl (an E3-ubiquitin-ligase), which mediates GAPDH's nuclear translocation. Nitric oxide (NO) generation following apoptotic stimulation elicits S-nitrosylation of GAPDH, which augments its binding to Siahl. GAPDH stabilizes Siahl facilitating its degradation of nuclear proteins. Activation of macrophages by endotoxin and of neurons by glutamate elicits GAPDH-Siahl binding, nuclear translocation and apoptosis, which are prevented by NO deletion. The NO-S-nitrosylation-GAPDH-Siahl cascade may represent a major molecular mechanism of cytotoxicity.
590 $a School code: 0098.
650 4 $a Biology, Neuroscience. $3 1017680
650 4 $a Biology, Cell. $3 1017686
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Health Sciences, Pathology. $3 1017854
690 $a 0317
690 $a 0379
690 $a 0307
690 $a 0571
710 2 0 $a The Johns Hopkins University. $3 1017431
773 0 $t Dissertation Abstracts International $g 66-11B.
790 1 0 $a Snyder, Solomon H., $e advisor
790 $a 0098
791 $a Ph.D.
792 $a 2006
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3197160