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Interaction of the components in human and escherichia coli pyruvate dehydrogenase multienzyme complexes

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TitleInfo
Title
Interaction of the components in human and escherichia coli pyruvate dehydrogenase multienzyme complexes
Name (type = personal)
NamePart (type = family)
Wang
NamePart (type = given)
Junjie
NamePart (type = date)
1983-
DisplayForm
Junjie Wang
Role
RoleTerm (authority = RULIB)
author
Name (type = personal)
NamePart (type = family)
Jordan
NamePart (type = given)
Frank
DisplayForm
Frank Jordan
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
chair
Name (type = personal)
NamePart (type = family)
Huskey
NamePart (type = given)
Phillip
DisplayForm
Phillip Huskey
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Lalancette
NamePart (type = given)
Roger
DisplayForm
Roger Lalancette
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Mendelsohn
NamePart (type = given)
Richard
DisplayForm
Richard Mendelsohn
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Farinas
NamePart (type = given)
Edgardo T.
DisplayForm
Edgardo T. Farinas
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 - Newark
Role
RoleTerm (authority = RULIB)
school
TypeOfResource
Text
Genre (authority = marcgt)
theses
OriginInfo
DateCreated (qualifier = exact)
2014
DateOther (qualifier = exact); (type = degree)
2014-01
Place
PlaceTerm (type = code)
xx
Language
LanguageTerm (authority = ISO639-2b); (type = code)
eng
Abstract (type = abstract)
The pyruvate dehydrogenase multienzyme complex (PDHc) plays crucial physiological roles in human. Structural study of this complex with traditional methods is highly challenging due to its large size (> 10 M Da). In this thesis, the Hydrogen/Deuterium Exchange Mass Spectrometry (HDX-MS) method was employed to study the protein-protein interactions of the components in both E. coli and human PDHc, which successfully revealed their binding loci, as well as the active center coupling, the substrate coupling, the allosteric regulation, and the catalytic mechanisms. The findings greatly improved the current understanding of the PDHc model, creating opportunities for designing new drugs targeting protein-protein interactions.
Subject (authority = RUETD)
Topic
Chemistry
RelatedItem (type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier (type = RULIB)
ETD
Identifier
ETD_5250
PhysicalDescription
Form (authority = gmd)
electronic resource
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
xxvi, 283 p. : ill.
Note (type = degree)
Ph.D.
Note (type = bibliography)
Includes bibliographical references
Note (type = vita)
Includes vita
Note (type = statement of responsibility)
by Junjie Wang
Subject (authority = ETD-LCSH)
Topic
Pyruvates
Subject (authority = ETD-LCSH)
Topic
Escherichia coli
RelatedItem (type = host)
TitleInfo
Title
Graduate School - Newark Electronic Theses and Dissertations
Identifier (type = local)
rucore10002600001
Location
PhysicalLocation (authority = marcorg); (displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier (type = doi)
doi:10.7282/T3FX77J5
Genre (authority = ExL-Esploro)
ETD doctoral
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Rights

RightsDeclaration (ID = rulibRdec0006)
The author owns the copyright to this work.
RightsHolder (type = personal)
Name
FamilyName
Wang
GivenName
Junjie
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2013-12-23 16:25:58
AssociatedEntity
Name
Junjie Wang
Role
Copyright holder
Affiliation
Rutgers University. Graduate School - Newark
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)
2014-01-31
DateTime (encoding = w3cdtf); (qualifier = exact); (point = end)
2016-01-31
Type
Embargo
Detail
Access to this PDF has been restricted at the author's request. It will be publicly available after January 31st, 2016.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
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Technical

RULTechMD (ID = TECHNICAL1)
ContentModel
ETD
OperatingSystem (VERSION = 5.1)
windows xp
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