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Integrative Mass Spectrometry Strategies for Mapping Protein Structural Variation and Modifications in Human Biofluids Under Disease Conditions
Integrative Mass Spectrometry Strategies for Mapping Protein Structural Variation and Modifications in Human Biofluids Under Disease Conditions
상세정보
- 자료유형
- 학위논문 서양
- 최종처리일시
- 20260202105652
- ISBN
- 9798270253844
- DDC
- 615
- 저자명
- Zhu, Zexin.
- 서명/저자
- Integrative Mass Spectrometry Strategies for Mapping Protein Structural Variation and Modifications in Human Biofluids Under Disease Conditions
- 발행사항
- [Sl] : The University of Wisconsin - Madison, 2026
- 발행사항
- Ann Arbor : ProQuest Dissertations & Theses, 2026
- 형태사항
- 283 p
- 주기사항
- Source: Dissertations Abstracts International, Volume: 87-07, Section: B.
- 주기사항
- Advisor: Li, Lingjun.
- 학위논문주기
- Thesis (Ph.D.)--The University of Wisconsin - Madison, 2026.
- 초록/해제
- 요약Proteins are key building blocks of living creatures. These organic molecules may exhibit various structural modifications and changes in abundance under different conditions. They may undergo post-translational modifications (PTMs) catalyzed by multiple enzymes, and they can also experience structural alterations upon exposure to pathogens or stimulants associated with specific diseases. Mass spectrometry (MS) has evolved into a powerful and robust analytical tool for elucidating subtle mass shifts induced by PTMs. It enables fast and accurate analysis with high resolution, facilitating systematic and in-depth proteomic profiling.This dissertation employs multiple MS-based strategies to characterize protein PTMs and perform structural analyses of essential biomarker proteins. Built upon our lab's previous work on the design and synthesis of a unique biotin-thiol tag that enables targeted analysis of protein citrullination, I applied this enrichment strategy to track citrullination variations in plasma proteins involved in autoimmune diseases. Through this approach, citrullination associated with rheumatoid arthritis (RA) and Sjogren syndrome (SS) was mapped across different biofluids and organs. Furthermore, this dissertation investigates the subsequent structural effects of this modification.
- 일반주제명
- Pharmaceutical sciences
- 일반주제명
- Analytical chemistry
- 일반주제명
- Biochemistry
- 키워드
- Proteomics
- 키워드
- Quantification
- 기타저자
- The University of Wisconsin - Madison Pharmaceutical Sciences
- 기본자료저록
- Dissertations Abstracts International. 87-07B.
- 전자적 위치 및 접속
- 로그인 후 원문을 볼 수 있습니다.
MARC
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■040 ▼aMiAaPQ▼cMiAaPQ
■0820 ▼a615
■1001 ▼aZhu, Zexin.
■24510▼aIntegrative Mass Spectrometry Strategies for Mapping Protein Structural Variation and Modifications in Human Biofluids Under Disease Conditions
■260 ▼a[Sl]▼bThe University of Wisconsin - Madison▼c2026
■260 1▼aAnn Arbor▼bProQuest Dissertations & Theses▼c2026
■300 ▼a283 p
■500 ▼aSource: Dissertations Abstracts International, Volume: 87-07, Section: B.
■500 ▼aAdvisor: Li, Lingjun.
■5021 ▼aThesis (Ph.D.)--The University of Wisconsin - Madison, 2026.
■520 ▼aProteins are key building blocks of living creatures. These organic molecules may exhibit various structural modifications and changes in abundance under different conditions. They may undergo post-translational modifications (PTMs) catalyzed by multiple enzymes, and they can also experience structural alterations upon exposure to pathogens or stimulants associated with specific diseases. Mass spectrometry (MS) has evolved into a powerful and robust analytical tool for elucidating subtle mass shifts induced by PTMs. It enables fast and accurate analysis with high resolution, facilitating systematic and in-depth proteomic profiling.This dissertation employs multiple MS-based strategies to characterize protein PTMs and perform structural analyses of essential biomarker proteins. Built upon our lab's previous work on the design and synthesis of a unique biotin-thiol tag that enables targeted analysis of protein citrullination, I applied this enrichment strategy to track citrullination variations in plasma proteins involved in autoimmune diseases. Through this approach, citrullination associated with rheumatoid arthritis (RA) and Sjogren syndrome (SS) was mapped across different biofluids and organs. Furthermore, this dissertation investigates the subsequent structural effects of this modification.
■590 ▼aSchool code: 0262.
■650 4▼aPharmaceutical sciences
■650 4▼aAnalytical chemistry
■650 4▼aBiochemistry
■653 ▼aAutoimmune disease
■653 ▼aMass spectrometry
■653 ▼aPost-translational modifications
■653 ▼aProteomics
■653 ▼aQuantification
■653 ▼aStructural biology
■690 ▼a0572
■690 ▼a0486
■690 ▼a0487
■71020▼aThe University of Wisconsin - Madison▼bPharmaceutical Sciences.
■7730 ▼tDissertations Abstracts International▼g87-07B.
■790 ▼a0262
■791 ▼aPh.D.
■792 ▼a2026
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17361014▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.
