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Super-resolution Fluorescence Micros...

Vissa, Adrian Alexei.

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Super-resolution Fluorescence Microscopy Studies of Protein Association and Higher-order Structure.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Super-resolution Fluorescence Microscopy Studies of Protein Association and Higher-order Structure./
Author:	Vissa, Adrian Alexei.
Published:	Ann Arbor : ProQuest Dissertations & Theses, : 2018,
Description:	186 p.
Notes:	Source: Dissertations Abstracts International, Volume: 80-02, Section: B.
Contained By:	Dissertations Abstracts International80-02B.
Subject:	Cellular biology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10688336
ISBN:	9780438189553

Super-resolution Fluorescence Microscopy Studies of Protein Association and Higher-order Structure.
Vissa, Adrian Alexei.

Super-resolution Fluorescence Microscopy Studies of Protein Association and Higher-order Structure. - Ann Arbor : ProQuest Dissertations & Theses, 2018 - 186 p.

Source: Dissertations Abstracts International, Volume: 80-02, Section: B.

Thesis (Ph.D.)--University of Toronto (Canada), 2018.

This item must not be sold to any third party vendors.

The spatial organization and interaction of proteins within cells fuels a myriad of biological processes. Protein modification, transport, signaling, polymerization and membrane remodeling are just a few examples. In cellular pathways, such as the endocytic membrane transport pathway, the recruitment of specific proteins and protein complexes to the membrane are hallmarks of the maturation and progression of the process. Interaction of membrane proteins from different organelles is of great importance as well. Recent discoveries have suggested that organelles may communicate with each other and exchange lipids and metabolites through the association of tethering proteins. Their proliferation may also be directly dependent on inter-organelle cooperativity such as the interaction of the endoplasmic reticulum with mitochondria and peroxisomes. Protein polymerization allows the creation of large macromolecular foundations that are mediators of diffusion and compartmentalization. The organizational motifs by which these assemblies are built are of interest for structure-function relationships. The interaction and association of protein complexes as described above takes place at the nanoscale, below the optical diffraction limit. Although the colocalization of proteins can be visualized via traditional forms of fluorescence microscopy, many biological questions require a finer level of resolution. Super-resolution fluorescence microscopy has revolutionized optical imaging by harnessing advances in hardware, software and the modulation of light. Variations in illumination and emission can be used to break the diffraction limit and observe a new level of detail in the cell. This thesis focuses on two of these techniques, Structured Illumination Microscopy and Single-Molecule Localization Microscopy, and their application to questions of nanoscale protein interactions in the endomembrane system, peroxisomal division and the supramolecular arrangement of septin proteins. The work concludes with a novel technological extension of Single-Molecule Localization Microscopy.

ISBN: 9780438189553Subjects--Topical Terms:

3172791
Cellular biology.
Subjects--Index Terms:

Hyperspectral imaging

Super-resolution Fluorescence Microscopy Studies of Protein Association and Higher-order Structure.
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500 $a Source: Dissertations Abstracts International, Volume: 80-02, Section: B.
500 $a Publisher info.: Dissertation/Thesis.
500 $a Advisor: Yip, Christopher M.;Kim, Peter K.
502 $a Thesis (Ph.D.)--University of Toronto (Canada), 2018.
506 $a This item must not be sold to any third party vendors.
520 $a The spatial organization and interaction of proteins within cells fuels a myriad of biological processes. Protein modification, transport, signaling, polymerization and membrane remodeling are just a few examples. In cellular pathways, such as the endocytic membrane transport pathway, the recruitment of specific proteins and protein complexes to the membrane are hallmarks of the maturation and progression of the process. Interaction of membrane proteins from different organelles is of great importance as well. Recent discoveries have suggested that organelles may communicate with each other and exchange lipids and metabolites through the association of tethering proteins. Their proliferation may also be directly dependent on inter-organelle cooperativity such as the interaction of the endoplasmic reticulum with mitochondria and peroxisomes. Protein polymerization allows the creation of large macromolecular foundations that are mediators of diffusion and compartmentalization. The organizational motifs by which these assemblies are built are of interest for structure-function relationships. The interaction and association of protein complexes as described above takes place at the nanoscale, below the optical diffraction limit. Although the colocalization of proteins can be visualized via traditional forms of fluorescence microscopy, many biological questions require a finer level of resolution. Super-resolution fluorescence microscopy has revolutionized optical imaging by harnessing advances in hardware, software and the modulation of light. Variations in illumination and emission can be used to break the diffraction limit and observe a new level of detail in the cell. This thesis focuses on two of these techniques, Structured Illumination Microscopy and Single-Molecule Localization Microscopy, and their application to questions of nanoscale protein interactions in the endomembrane system, peroxisomal division and the supramolecular arrangement of septin proteins. The work concludes with a novel technological extension of Single-Molecule Localization Microscopy.
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