東華大學圖書館 |

語系: 繁體中文

說明(常見問題)

回圖書館首頁

手機版館藏查詢

登入

回首頁

切換: 標籤 | MARC模式 | ISBD

Novel interactions between human cel...

Devroe, Eric James.

FindBook

Google Book

Amazon

博客來

Novel interactions between human cell proteins and human immunodeficiency virus type 1.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Novel interactions between human cell proteins and human immunodeficiency virus type 1./
作者:	Devroe, Eric James.
面頁冊數:	173 p.
附註:	Source: Dissertation Abstracts International, Volume: 66-01, Section: B, page: 0101.
Contained By:	Dissertation Abstracts International66-01B.
標題:	Biology, Molecular. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3161171
ISBN:	0496947850

Novel interactions between human cell proteins and human immunodeficiency virus type 1.
Devroe, Eric James.

Novel interactions between human cell proteins and human immunodeficiency virus type 1. - 173 p.

Source: Dissertation Abstracts International, Volume: 66-01, Section: B, page: 0101.

Thesis (Ph.D.)--Harvard University, 2005.

Human immunodeficiency virus type 1 (HIV-1) replication requires a complex series of physical and functional interactions between host cell and viral components. Additional molecular insight into these interactions will yield not only an increased understanding of fundamental retroviral biology, but may also identify new opportunities for therapeutic intervention in the treatment of AIDS.

ISBN: 0496947850Subjects--Topical Terms:

1017719
Biology, Molecular.

Novel interactions between human cell proteins and human immunodeficiency virus type 1.
LDR:03333nmm 2200325 4500 001 1816123
005 20060717151405.5
008 130610s2005 eng d
020 $a 0496947850
035 $a (UnM)AAI3161171
035 $a AAI3161171
040 $a UnM $c UnM
100 1 $a Devroe, Eric James. $3 1905518
245 1 0 $a Novel interactions between human cell proteins and human immunodeficiency virus type 1.
300 $a 173 p.
500 $a Source: Dissertation Abstracts International, Volume: 66-01, Section: B, page: 0101.
500 $a Adviser: Pamela A. Silver.
502 $a Thesis (Ph.D.)--Harvard University, 2005.
520 $a Human immunodeficiency virus type 1 (HIV-1) replication requires a complex series of physical and functional interactions between host cell and viral components. Additional molecular insight into these interactions will yield not only an increased understanding of fundamental retroviral biology, but may also identify new opportunities for therapeutic intervention in the treatment of AIDS.
520 $a One distinctive feature of HIV-1 is its ability to infect non-dividing cells such as macrophages. Recently it was reported that the viral integrase (IN) protein directed HIV-1 preintegration complex (PIC) nuclear import. To gain insight into PIC nuclear import, the intracellular transport of IN was examined. IN was found to be a karyophilic protein in human cells, but not for the reasons previously assumed. Instead, a model is presented in which IN nuclear accumulation results from its cytoplasmic degradation and specific nuclear retention due to strong chromatin interactions.
520 $a To extend these studies, IN-interacting proteins were identified by affinity purification and mass spectrometry. A chromatin-associated protein, p75/LEDGF, was shown to bind wild-type but not a mutant V165A IN protein. To probe the role of p75/LEDGF in HIV-1 replication, RNAi was employed to transiently downregulate p75/LEDGF. A novel retroviral vector was also developed to deliver small hairpin RNA (shRNA) gene cassettes, which enabled generation of stable p75/LEDGF "knock-down" cells. HIV-1 efficiently infected both categories of p75/LEDGF knock-down cells. These results suggest either that p75/LEDGF is not an important determinant of HIV-1 replication in this context, or that the level of p75/LEDGF silencing achieved was insufficient to reveal a replication block.
520 $a In a separate project, a potential connection between human serine-threonine kinases and HIV-1 was investigated. HIV-1 particles were shown to incorporate the related NDR1 and NDR2 kinases. The viral-encoded protease was shown to process NDR1 and NDR2, an event that occurred both within virus particles and the HIV-1 producer cells. Protease processing altered NDR2 subcellular localization and altered the enzymatic activity of both NDR1 and NDR2. The potential roles of the NDR1 and NDR2 kinases in HIV-1 biology are discussed, as are experiments identifying Mob2 as a novel cellular regulator of the NDR kinases.
590 $a School code: 0084.
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biology, Cell. $3 1017686
650 4 $a Biology, Microbiology. $3 1017734
690 $a 0307
690 $a 0379
690 $a 0410
710 2 0 $a Harvard University. $3 528741
773 0 $t Dissertation Abstracts International $g 66-01B.
790 1 0 $a Silver, Pamela A., $e advisor
790 $a 0084
791 $a Ph.D.
792 $a 2005
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3161171