Staff View
The BRCA1 ring domain is essential for DNA damage repair and G2/M checkpoint activation

Descriptive

TitleInfo
Title
The BRCA1 ring domain is essential for DNA damage repair and G2/M checkpoint activation
Name (type = personal)
NamePart (type = family)
Al Hamza
NamePart (type = given)
Ali
NamePart (type = date)
1983-
DisplayForm
ALI AL HAMZA
Role
RoleTerm (authority = RULIB)
author
Name (type = personal)
NamePart (type = family)
Bunting
NamePart (type = given)
Samuel F
DisplayForm
Samuel F Bunting
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
chair
Name (type = personal)
NamePart (type = family)
Grant
NamePart (type = given)
Barth D
DisplayForm
Barth D Grant
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Shen
NamePart (type = given)
Zhiyuan
DisplayForm
Zhiyuan Shen
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
outside member
Name (type = corporate)
NamePart
Rutgers University
Role
RoleTerm (authority = RULIB)
degree grantor
Name (type = corporate)
NamePart
Graduate School - New Brunswick
Role
RoleTerm (authority = RULIB)
school
TypeOfResource
Text
Genre (authority = marcgt)
theses
OriginInfo
DateCreated (qualifier = exact)
2014
DateOther (qualifier = exact); (type = degree)
2014-05
Place
PlaceTerm (type = code)
xx
Language
LanguageTerm (authority = ISO639-2b); (type = code)
eng
Abstract (type = abstract)
The BRCA1 (breast cancer 1, early onset) tumor suppressor gene is involved in a variety of cellular pathways, and is an essential factor for normal DNA repair by homologous recombination. The BRCA1 protein has a number of conserved domains, including a coiled-coil domain, two BRCT domains and an N-terminal RING (Really Interesting New Gene) domain. Many cancer-causing mutations have been reported that affect the BRCA1 RING domain, although the exact impact of RING domain mutations on DNA repair is not clear. We characterized a BRCA1-mutant mouse model, BRCA1∆2/∆2 , in which conditional deletion of exon 2 excises a large portion of the RING domain. BRCA1∆2/∆2 cells have a defective G2/M cell cycle checkpoint after IR-induced DNA damage. In addition, BRCA1∆2/∆2 showed a high rate of genomic instability after treatment with agents that cause DNA double strand breaks or DNA interstrand crosslinks. Co-deletion of the 53BP1 (p53 Binding Protein 1) gene rescues some, but not all, phenotypes of mutation of the BRCA1 RING domain. By clarifying the importance of the RING domain in mediating BRCA1 activity, we aim to better understand why patient mutations in the BRCA1 gene cause cancer predisposition and identify new targets for therapeutic intervention.
Subject (authority = RUETD)
Topic
Physiology and Integrative Biology
Subject (authority = ETD-LCSH)
Topic
BRCA genes
Subject (authority = ETD-LCSH)
Topic
Breast--Cancer--Research
RelatedItem (type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier (type = RULIB)
ETD
Identifier
ETD_5576
PhysicalDescription
Form (authority = gmd)
electronic resource
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
ix, 60 p. : ill.
Note (type = degree)
M.S.
Note (type = bibliography)
Includes bibliographical references
Note (type = statement of responsibility)
by Ali Naji Ali Al Hamza
Subject (authority = ETD-LCSH)
Topic
DNA damage
RelatedItem (type = host)
TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier (type = local)
rucore19991600001
Location
PhysicalLocation (authority = marcorg); (displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier (type = doi)
doi:10.7282/T31Z42QT
Genre (authority = ExL-Esploro)
ETD graduate
Back to the top

Rights

RightsDeclaration (ID = rulibRdec0006)
The author owns the copyright to this work.
RightsHolder (type = personal)
Name
FamilyName
AL HAMZA
GivenName
ALI
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2014-04-24 19:42:42
AssociatedEntity
Name
ALI AL HAMZA
Role
Copyright holder
Affiliation
Rutgers University. Graduate School - New Brunswick
AssociatedObject
Type
License
Name
Author Agreement License
Detail
I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
RightsEvent
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2014-05-31
DateTime (encoding = w3cdtf); (qualifier = exact); (point = end)
2014-11-30
Type
Embargo
Detail
Access to this PDF has been restricted at the author's request. It will be publicly available after November 30th, 2014.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
Back to the top

Technical

RULTechMD (ID = TECHNICAL1)
ContentModel
ETD
OperatingSystem (VERSION = 5.1)
windows xp
Back to the top
Version 8.5.5
Rutgers University Libraries - Copyright ©2024