語系:
繁體中文
English
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
Functions of nuclear inner membrane ...
~
Lee, Kenneth K.
FindBook
Google Book
Amazon
博客來
Functions of nuclear inner membrane proteins in humans and Caenorhabditis elegans.
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
Functions of nuclear inner membrane proteins in humans and Caenorhabditis elegans./
作者:
Lee, Kenneth K.
面頁冊數:
218 p.
附註:
Adviser: Katherine L. Wilson.
Contained By:
Dissertation Abstracts International63-03B.
標題:
Biology, Cell. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3046491
ISBN:
0493606815
Functions of nuclear inner membrane proteins in humans and Caenorhabditis elegans.
Lee, Kenneth K.
Functions of nuclear inner membrane proteins in humans and Caenorhabditis elegans.
- 218 p.
Adviser: Katherine L. Wilson.
Thesis (Ph.D.)--The Johns Hopkins University, 2002.
Proteins of the inner nuclear membrane are fundamentally important for nuclear structure and function. Three such proteins, named LAP2, emerin and MAN1, share the 43-residue ‘LEM’ domain. Loss of emerin causes Emery-Dreifuss muscular dystrophy (EDMD), in humans, through unknown mechanisms. To understand this disease, I characterized the functions of human emerin. I first tested the hypothesis that emerin binds barrier-to-autointegration factor (BAF), an essential, conserved DNA-bridging protein in multicellular eukaryotes, with potential roles in nuclear assembly and chromatin organization. Binding was tested biochemically, and domains mapped using 17 alanine-substitution mutants of emerin. This work identified two functional domains in human emerin: the LEM-domain, which is required to bind BAF, and a central domain required to bind lamin A. These results are significant; they suggest that BAF is a binding partner for all LEM-domain proteins, and led me to discover that two disease-causing mutations map outside the BAF- and lamin A-binding regions, potentially defining additional or unique functional domains in emerin that relate directly to the EDMD disease mechanism. I also used <italic>C. elegans </italic> to determine if emerin function is conserved in a genetically tractable system. After identifying and cloning the three LEM-domain genes in <italic> C. elegans</italic>, I showed that the biochemical properties, localization and loss-of-function phenotype of <italic>C. elegans</italic> emerin parallel human emerin. I am currently determining which biochemical functions of human emerin are shared with <italic>C. elegans</italic> emerin, for future genetic analysis of emerin function.
ISBN: 0493606815Subjects--Topical Terms:
1017686
Biology, Cell.
Functions of nuclear inner membrane proteins in humans and Caenorhabditis elegans.
LDR
:02606nam 2200265 a 45
001
927695
005
20110425
008
110425s2002 eng d
020
$a
0493606815
035
$a
(UnM)AAI3046491
035
$a
AAI3046491
040
$a
UnM
$c
UnM
100
1
$a
Lee, Kenneth K.
$3
1007934
245
1 0
$a
Functions of nuclear inner membrane proteins in humans and Caenorhabditis elegans.
300
$a
218 p.
500
$a
Adviser: Katherine L. Wilson.
500
$a
Source: Dissertation Abstracts International, Volume: 63-03, Section: B, page: 1121.
502
$a
Thesis (Ph.D.)--The Johns Hopkins University, 2002.
520
$a
Proteins of the inner nuclear membrane are fundamentally important for nuclear structure and function. Three such proteins, named LAP2, emerin and MAN1, share the 43-residue ‘LEM’ domain. Loss of emerin causes Emery-Dreifuss muscular dystrophy (EDMD), in humans, through unknown mechanisms. To understand this disease, I characterized the functions of human emerin. I first tested the hypothesis that emerin binds barrier-to-autointegration factor (BAF), an essential, conserved DNA-bridging protein in multicellular eukaryotes, with potential roles in nuclear assembly and chromatin organization. Binding was tested biochemically, and domains mapped using 17 alanine-substitution mutants of emerin. This work identified two functional domains in human emerin: the LEM-domain, which is required to bind BAF, and a central domain required to bind lamin A. These results are significant; they suggest that BAF is a binding partner for all LEM-domain proteins, and led me to discover that two disease-causing mutations map outside the BAF- and lamin A-binding regions, potentially defining additional or unique functional domains in emerin that relate directly to the EDMD disease mechanism. I also used <italic>C. elegans </italic> to determine if emerin function is conserved in a genetically tractable system. After identifying and cloning the three LEM-domain genes in <italic> C. elegans</italic>, I showed that the biochemical properties, localization and loss-of-function phenotype of <italic>C. elegans</italic> emerin parallel human emerin. I am currently determining which biochemical functions of human emerin are shared with <italic>C. elegans</italic> emerin, for future genetic analysis of emerin function.
590
$a
School code: 0098.
650
4
$a
Biology, Cell.
$3
1017686
690
$a
0379
710
2 0
$a
The Johns Hopkins University.
$3
1017431
773
0
$t
Dissertation Abstracts International
$g
63-03B.
790
$a
0098
790
1 0
$a
Wilson, Katherine L.,
$e
advisor
791
$a
Ph.D.
792
$a
2002
856
4 0
$u
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3046491
筆 0 讀者評論
館藏地:
全部
電子資源
出版年:
卷號:
館藏
1 筆 • 頁數 1 •
1
條碼號
典藏地名稱
館藏流通類別
資料類型
索書號
使用類型
借閱狀態
預約狀態
備註欄
附件
W9099554
電子資源
11.線上閱覽_V
電子書
EB W9099554
一般使用(Normal)
在架
0
1 筆 • 頁數 1 •
1
多媒體
評論
新增評論
分享你的心得
Export
取書館
處理中
...
變更密碼
登入