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

TorsinA Expression in Budding Yeast ...

Chalfant, Madeleine Carol.

Linked to FindBook

Google Book

Amazon

博客來

TorsinA Expression in Budding Yeast Points to Missing LINC in DYT1 Dystonia Pathogenesis.

Record Type:	Electronic resources : Monograph/item
Title/Author:	TorsinA Expression in Budding Yeast Points to Missing LINC in DYT1 Dystonia Pathogenesis./
Author:	Chalfant, Madeleine Carol.
Published:	Ann Arbor : ProQuest Dissertations & Theses, : 2019,
Description:	134 p.
Notes:	Source: Dissertations Abstracts International, Volume: 81-10, Section: B.
Contained By:	Dissertations Abstracts International81-10B.
Subject:	Cellular biology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=13810091
ISBN:	9781658491723

TorsinA Expression in Budding Yeast Points to Missing LINC in DYT1 Dystonia Pathogenesis.
Chalfant, Madeleine Carol.

TorsinA Expression in Budding Yeast Points to Missing LINC in DYT1 Dystonia Pathogenesis. - Ann Arbor : ProQuest Dissertations & Theses, 2019 - 134 p.

Source: Dissertations Abstracts International, Volume: 81-10, Section: B.

Thesis (Ph.D.)--Yale University, 2019.

This item must not be sold to any third party vendors.

DYT1 dystonia, a debilitating neuro-muscular disorder with few treatment options, is caused by an in-frame deletion of a single amino acid in the gene encoding the AAA+ ATPase TorsinA. TorsinA localizes to the contiguous endoplasmic reticulum / nuclear envelope lumen and can only hydrolyze ATP after binding one of its two transmembrane activating partners, LAP1 or LULL1. TorsinA function is unknown, as its substrate is elusive. However, recent work suggests TorsinA likely participates in complex and poorly understood nuclear envelope remodeling events. Because the complexity of TorsinA's native cellular environment complicates experimental analysis, I assessed TorsinA function in the similar yet significantly simpler cellular environment of budding yeast. While yeast lack TorsinA, LAP1, and LULL1 homologs, yeast cellular machinery can interact with non-conserved human proteins and provide insight into cellular function. Here, I identified relationships between TorA and two yeast nuclear envelope proteins with structurally similar orthologs in mammalian cells. My results point to a putative TorsinA substrate and suggest strategies to interrogate TorA dysfunction in the future.

ISBN: 9781658491723Subjects--Topical Terms:

3172791
Cellular biology.
Subjects--Index Terms:

Gene encoding

TorsinA Expression in Budding Yeast Points to Missing LINC in DYT1 Dystonia Pathogenesis.
LDR:02308nmm a2200337 4500 001 2272414
005 20201105110050.5
008 220629s2019 ||||||||||||||||| ||eng d
020 $a 9781658491723
035 $a (MiAaPQ)AAI13810091
035 $a AAI13810091
040 $a MiAaPQ $c MiAaPQ
100 1 $a Chalfant, Madeleine Carol. $3 3549852
245 1 0 $a TorsinA Expression in Budding Yeast Points to Missing LINC in DYT1 Dystonia Pathogenesis.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 2019
300 $a 134 p.
500 $a Source: Dissertations Abstracts International, Volume: 81-10, Section: B.
500 $a Advisor: Lusk, Patrick.
502 $a Thesis (Ph.D.)--Yale University, 2019.
506 $a This item must not be sold to any third party vendors.
506 $a This item must not be added to any third party search indexes.
520 $a DYT1 dystonia, a debilitating neuro-muscular disorder with few treatment options, is caused by an in-frame deletion of a single amino acid in the gene encoding the AAA+ ATPase TorsinA. TorsinA localizes to the contiguous endoplasmic reticulum / nuclear envelope lumen and can only hydrolyze ATP after binding one of its two transmembrane activating partners, LAP1 or LULL1. TorsinA function is unknown, as its substrate is elusive. However, recent work suggests TorsinA likely participates in complex and poorly understood nuclear envelope remodeling events. Because the complexity of TorsinA's native cellular environment complicates experimental analysis, I assessed TorsinA function in the similar yet significantly simpler cellular environment of budding yeast. While yeast lack TorsinA, LAP1, and LULL1 homologs, yeast cellular machinery can interact with non-conserved human proteins and provide insight into cellular function. Here, I identified relationships between TorA and two yeast nuclear envelope proteins with structurally similar orthologs in mammalian cells. My results point to a putative TorsinA substrate and suggest strategies to interrogate TorA dysfunction in the future.
590 $a School code: 0265.
650 4 $a Cellular biology. $3 3172791
650 4 $a Pathology. $3 643180
653 $a Gene encoding
653 $a TorsinA
690 $a 0379
690 $a 0571
710 2 $a Yale University. $b Cell Biology. $3 2101675
773 0 $t Dissertations Abstracts International $g 81-10B.
790 $a 0265
791 $a Ph.D.
792 $a 2019
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=13810091