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Towards determining the mechanism of recognition and binding to collagen by alpha 1 beta 1 and alpha 2 beta 1 integrins
Descriptive
TitleInfo
Title
Towards determining the mechanism of recognition and binding to collagen by alpha 1 beta 1 and alpha 2 beta 1 integrins
Name
(type = personal)
NamePart
(type = family)
Sikora
NamePart
(type = given)
Jacqueline
NamePart
(type = date)
1989-
DisplayForm
Jacqueline Sikora
Role
RoleTerm
(authority = RULIB)
author
Name
(type = personal)
NamePart
(type = family)
Baum
NamePart
(type = given)
Jean
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Jean Baum
Affiliation
Advisory Committee
Role
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(authority = RULIB)
chair
Name
(type = personal)
NamePart
(type = family)
Case
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(type = given)
David
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David Case
Affiliation
Advisory Committee
Role
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(authority = RULIB)
internal member
Name
(type = personal)
NamePart
(type = family)
Kalodimos
NamePart
(type = given)
Charalampos
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Charalampos Kalodimos
Affiliation
Advisory Committee
Role
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(authority = RULIB)
internal member
Name
(type = personal)
NamePart
(type = family)
Lee
NamePart
(type = given)
Jeehiun
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Jeehiun Lee
Affiliation
Advisory Committee
Role
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(authority = RULIB)
internal member
Name
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NamePart
Rutgers University
Role
RoleTerm
(authority = RULIB)
degree grantor
Name
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NamePart
Graduate School - New Brunswick
Role
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school
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Text
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theses
OriginInfo
DateCreated
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2014
DateOther
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(type = degree)
2014-10
CopyrightDate
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2014
Place
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(type = code)
xx
Language
LanguageTerm
(authority = ISO639-2b);
(type = code)
eng
Abstract
(type = abstract)
Collagen is the most abundant protein in the human body. There are several collagen‐binding integrins, which exist as transmembrane proteins and serve to transmit cellular signals via inside‐out and outside‐in pathways, via a cascade of conformational changes. Collagen is capable of initiating outside‐in signaling by binding to the extracellular I‐domain of integrin, in a cation‐dependent manner. While much is known about collagen subtype and sequence specificity of varying integrins, the mechanism of binding has yet to be determined. Our lab studies the interaction between collagen and the I‐domains of integrins alpha 1 beta 1 (alpha1I), and alpha 2 beta 1 (alpha2I), via molecular biology and nuclear magnetic resonance (NMR) techniques. We are also investigating recombinant collagen‐like peptides for the purpose of binding assays between collagen and integrin. The goal is to determine a structuralfunctional relationship occurring in the interaction, and to use this in order to determine the mechanism of binding. The interaction of collagen and integrin has roles in cancer cell proliferation and thrombosis, making the determination of this mechanism vital to the generation of future treatments for these diseases.
Subject
(authority = RUETD)
Topic
Chemistry and Chemical Biology
Subject
(authority = ETD-LCSH)
Topic
Integrins
Subject
(authority = ETD-LCSH)
Topic
Collagen
RelatedItem
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TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier
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ETD
Identifier
ETD_5721
PhysicalDescription
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electronic resource
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application/pdf
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text/xml
Extent
1 online resource (iv, 30 p. : ill.)
Note
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M.S.
Note
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Includes bibliographical references
Note
(type = statement of responsibility)
by Jacqueline Sikora
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TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier
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rucore19991600001
Location
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(displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier
(type = doi)
doi:10.7282/T36Q1ZVC
Genre
(authority = ExL-Esploro)
ETD graduate
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Rights
RightsDeclaration
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The author owns the copyright to this work.
RightsHolder
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Name
FamilyName
Sikora
GivenName
Jacqueline
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime
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(qualifier = exact);
(point = start)
2014-06-27 13:43:18
AssociatedEntity
Name
Jacqueline Sikora
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
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(qualifier = exact);
(point = start)
2014-10-31
DateTime
(encoding = w3cdtf);
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(point = end)
2016-10-30
Type
Embargo
Detail
Access to this PDF has been restricted at the author's request. It will be publicly available after October 30th, 2016.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
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Technical
RULTechMD
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ContentModel
ETD
OperatingSystem
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windows xp
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