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Application of Quantitative Cross-Linking Mass Spectrometry Methods to Study Interactome Differences
Application of Quantitative Cross-Linking Mass Spectrometry Methods to Study Interactome Differences
상세정보
- 자료유형
- 학위논문 서양
- 최종처리일시
- 20250211152001
- ISBN
- 9798383228678
- DDC
- 574
- 저자명
- Bakhtina, Anna.
- 서명/저자
- Application of Quantitative Cross-Linking Mass Spectrometry Methods to Study Interactome Differences
- 발행사항
- [Sl] : University of Washington, 2024
- 발행사항
- Ann Arbor : ProQuest Dissertations & Theses, 2024
- 형태사항
- 130 p
- 주기사항
- Source: Dissertations Abstracts International, Volume: 86-01, Section: B.
- 주기사항
- Advisor: Bruce, James E.
- 학위논문주기
- Thesis (Ph.D.)--University of Washington, 2024.
- 초록/해제
- 요약Proteins carry out the vast majority of biological function inside living cells. They do so by changing their shapes, interacting with one another and other molecules such as DNA and RNA. Gaining an understanding of intra and inter molecular protein interactions on a systems-level would allow for much deeper understanding of how biological functions are performed and regulated. Quantitative comparisons of these interactions between different systems or upon perturbations can increase understanding of remodeling associated with the aging, disease, and treatments. Here, cross-linking mass spectrometry is demonstrated with quantitative comparisons of protein interactions within intact systems, such as cells and membrane bound organelles. This work shows that reproducible remodeling of interactomes associated with aging in skeletal muscle mitochondria can be detected with isobaric quantitative protein interaction reporter (iqPIR) technologies. Moreover, changes in the interactome showed correlation with age-associated mitochondrial functional decline. Interactome differences associated with distinct functional differences in different cell types were also observed. Quantitative comparison of interactomes of human cell lines HEK293, HeLa and MCF7 uncovered differences in chromatin remodeling, mitochondrial transport and others that are independent of protein abundance levels. Utilizing a novel genetic mouse model that allows isolation of mitochondria from tubule or podocyte kidney cells, quantitative cross-linking and mass spectrometry enabled identification of differentially regulated proteins and pathways in mitochondria within these cell types that would otherwise remain unknown.
- 일반주제명
- Biochemistry
- 일반주제명
- Cellular biology
- 일반주제명
- Chemistry
- 일반주제명
- Molecular biology
- 일반주제명
- Analytical chemistry
- 키워드
- Cross-linking
- 키워드
- Interactomics
- 키워드
- Proteomics
- 기타저자
- University of Washington Genome Sciences
- 기본자료저록
- Dissertations Abstracts International. 86-01B.
- 전자적 위치 및 접속
- 로그인 후 원문을 볼 수 있습니다.
MARC
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■00520250211152001
■006m o d
■007cr#unu||||||||
■020 ▼a9798383228678
■035 ▼a(MiAaPQ)AAI31329995
■040 ▼aMiAaPQ▼cMiAaPQ
■0820 ▼a574
■1001 ▼aBakhtina, Anna.
■24510▼aApplication of Quantitative Cross-Linking Mass Spectrometry Methods to Study Interactome Differences
■260 ▼a[Sl]▼bUniversity of Washington▼c2024
■260 1▼aAnn Arbor▼bProQuest Dissertations & Theses▼c2024
■300 ▼a130 p
■500 ▼aSource: Dissertations Abstracts International, Volume: 86-01, Section: B.
■500 ▼aAdvisor: Bruce, James E.
■5021 ▼aThesis (Ph.D.)--University of Washington, 2024.
■520 ▼aProteins carry out the vast majority of biological function inside living cells. They do so by changing their shapes, interacting with one another and other molecules such as DNA and RNA. Gaining an understanding of intra and inter molecular protein interactions on a systems-level would allow for much deeper understanding of how biological functions are performed and regulated. Quantitative comparisons of these interactions between different systems or upon perturbations can increase understanding of remodeling associated with the aging, disease, and treatments. Here, cross-linking mass spectrometry is demonstrated with quantitative comparisons of protein interactions within intact systems, such as cells and membrane bound organelles. This work shows that reproducible remodeling of interactomes associated with aging in skeletal muscle mitochondria can be detected with isobaric quantitative protein interaction reporter (iqPIR) technologies. Moreover, changes in the interactome showed correlation with age-associated mitochondrial functional decline. Interactome differences associated with distinct functional differences in different cell types were also observed. Quantitative comparison of interactomes of human cell lines HEK293, HeLa and MCF7 uncovered differences in chromatin remodeling, mitochondrial transport and others that are independent of protein abundance levels. Utilizing a novel genetic mouse model that allows isolation of mitochondria from tubule or podocyte kidney cells, quantitative cross-linking and mass spectrometry enabled identification of differentially regulated proteins and pathways in mitochondria within these cell types that would otherwise remain unknown.
■590 ▼aSchool code: 0250.
■650 4▼aBiochemistry
■650 4▼aCellular biology
■650 4▼aChemistry
■650 4▼aMolecular biology
■650 4▼aAnalytical chemistry
■653 ▼aCross-linking
■653 ▼aInteractomics
■653 ▼aMass spectrometry
■653 ▼aProtein-protein interactions
■653 ▼aProteomics
■690 ▼a0487
■690 ▼a0379
■690 ▼a0485
■690 ▼a0486
■690 ▼a0307
■71020▼aUniversity of Washington▼bGenome Sciences.
■7730 ▼tDissertations Abstracts International▼g86-01B.
■790 ▼a0250
■791 ▼aPh.D.
■792 ▼a2024
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17162344▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.
