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  1. Article ; Online: Single-molecule microscopy for in-cell quantification of protein oligomeric stoichiometry.

    Chen, Huanhuan / Xie, Xihong / Chen, Tai-Yen

    Current opinion in structural biology

    2020  Volume 66, Page(s) 112–118

    Abstract: Protein organization modification plays a vital role in initiating signaling pathways, transcriptional regulation, and cell apoptosis regulation. Simultaneous quantification of oligomeric state and cellular parameters in the same cell, even though ... ...

    Abstract Protein organization modification plays a vital role in initiating signaling pathways, transcriptional regulation, and cell apoptosis regulation. Simultaneous quantification of oligomeric state and cellular parameters in the same cell, even though challenging, is required to understand their correlation at the molecular level. Recent advances of fluorescence protein and single-molecule localization microscopy enables the determination of localizations and oligomeric states of target proteins in cells. We reviewed the fluorescence intensity-based, localization-based, and photophysical property-based approaches for in-cell quantification of protein oligomeric stoichiometry. We discussed their working principles, applications, advantages, and limitations. These results also imply the combination of methodologies targeting different biological parameters at the single-cell level is essential to uncover the structure-function relationship at the molecular level.
    MeSH term(s) Microscopy, Fluorescence ; Proteins ; Single Molecule Imaging
    Chemical Substances Proteins
    Language English
    Publishing date 2020-11-23
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1068353-7
    ISSN 1879-033X ; 0959-440X
    ISSN (online) 1879-033X
    ISSN 0959-440X
    DOI 10.1016/j.sbi.2020.10.022
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3206: Show issues Location:
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  2. Article ; Online: Crossroads between membrane trafficking machinery and copper homeostasis in the nerve system.

    Wen, Meng-Hsuan / Xie, Xihong / Huang, Pei-San / Yang, Karen / Chen, Tai-Yen

    Open biology

    2021  Volume 11, Issue 12, Page(s) 210128

    Abstract: Imbalanced copper homeostasis and perturbation of membrane trafficking are two common symptoms that have been associated with the pathogenesis of neurodegenerative and neurodevelopmental diseases. Accumulating evidence from biophysical, cellular ... ...

    Abstract Imbalanced copper homeostasis and perturbation of membrane trafficking are two common symptoms that have been associated with the pathogenesis of neurodegenerative and neurodevelopmental diseases. Accumulating evidence from biophysical, cellular and
    MeSH term(s) Animals ; Copper/metabolism ; Copper Transport Proteins/metabolism ; Gene Expression Regulation ; Homeostasis ; Humans ; Nervous System/metabolism ; Nervous System Diseases/metabolism ; Parkinson Disease/metabolism ; Signal Transduction
    Chemical Substances Copper Transport Proteins ; Copper (789U1901C5)
    Language English
    Publishing date 2021-12-01
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2630944-0
    ISSN 2046-2441 ; 2046-2441
    ISSN (online) 2046-2441
    ISSN 2046-2441
    DOI 10.1098/rsob.210128
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Generation of a homozygous knock-in human embryonic stem cell line expressing SNAP-tagged SOD1.

    Huang, Pei-San / Wen, Meng-Hsuan / Xie, Xihong / Xu, An / Lee, Dung-Fang / Chen, Tai-Yen

    Stem cell research

    2021  Volume 54, Page(s) 102415

    Abstract: Superoxide Dismutase 1 (SOD1) is an antioxidant enzyme that protects the cells from radical oxygen species. To study the behavior of endogenous SOD1 under a microscope, we genetically modified H1 human embryonic stem cells (hESCs) to express SOD1 fused ... ...

    Abstract Superoxide Dismutase 1 (SOD1) is an antioxidant enzyme that protects the cells from radical oxygen species. To study the behavior of endogenous SOD1 under a microscope, we genetically modified H1 human embryonic stem cells (hESCs) to express SOD1 fused with a SNAP-tag, a protein tag that can be covalently labeled with a variety of synthetic probes. The engineered homozygous clone expressing SOD1-SNAP fusion proteins has normal stem cell morphology and karyotype, expresses pluripotency markers, and can be differentiated into all three germ layers in vitro, providing a versatile platform for imaging-based studies of SOD1.
    MeSH term(s) Cell Line ; Cells, Cultured ; Human Embryonic Stem Cells ; Humans ; Superoxide Dismutase/genetics ; Superoxide Dismutase-1/genetics
    Chemical Substances SOD1 protein, human ; Superoxide Dismutase (EC 1.15.1.1) ; Superoxide Dismutase-1 (EC 1.15.1.1)
    Language English
    Publishing date 2021-06-06
    Publishing country England
    Document type Journal Article
    ZDB-ID 2393143-7
    ISSN 1876-7753 ; 1873-5061
    ISSN (online) 1876-7753
    ISSN 1873-5061
    DOI 10.1016/j.scr.2021.102415
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Corrigendum to "Generation of a homozygous knock-in human embryonic stem cell line expressing SNAP-tagged SOD1" [Stem Cell Res. 54 (2021) 102415].

    Huang, Pei-San / Wen, Meng-Hsuan / Xie, Xihong / Xu, An / Lee, Dung-Fang / Chen, Tai-Yen

    Stem cell research

    2021  Volume 55, Page(s) 102483

    Language English
    Publishing date 2021-07-27
    Publishing country England
    Document type Published Erratum
    ZDB-ID 2393143-7
    ISSN 1876-7753 ; 1873-5061
    ISSN (online) 1876-7753
    ISSN 1873-5061
    DOI 10.1016/j.scr.2021.102483
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Generation of a genetically modified human embryonic stem cells expressing fluorescence tagged ATOX1.

    Wen, Meng-Hsuan / Xie, Xihong / Tu, Jian / Lee, Dung-Fang / Chen, Tai-Yen

    Stem cell research

    2019  Volume 41, Page(s) 101631

    Abstract: ATOX1 is a copper chaperone involved in intracellular copper homeostasis, cell proliferation, and tumor progression. To investigate the physiologically relevant molecular mechanism of ATOX1 by using imaging-based approaches, we genetically modified ATOX1 ...

    Abstract ATOX1 is a copper chaperone involved in intracellular copper homeostasis, cell proliferation, and tumor progression. To investigate the physiologically relevant molecular mechanism of ATOX1 by using imaging-based approaches, we genetically modified ATOX1 in H1 hESCs to express mCherry-ATOX1 fusion protein under endogenous regulatory machinery. The fluorescence engineered hESC clone maintains characteristic stem cell features and can differentiate to all three germ layers, serving as a unique tool to dissect the role of ATOX1 in various cellular processes.
    MeSH term(s) Base Sequence ; Cell Culture Techniques/methods ; Copper Transport Proteins/genetics ; Fluorescent Dyes/metabolism ; Human Embryonic Stem Cells/cytology ; Human Embryonic Stem Cells/metabolism ; Humans ; Male ; Molecular Chaperones/genetics ; Reproducibility of Results
    Chemical Substances ATOX1 protein, human ; Copper Transport Proteins ; Fluorescent Dyes ; Molecular Chaperones
    Language English
    Publishing date 2019-10-16
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 1876-7753
    ISSN (online) 1876-7753
    DOI 10.1016/j.scr.2019.101631
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Quantifying the Oligomeric States of Membrane Proteins in Cells through Super-Resolution Localizations

    Xie, Xihong / Aparna Calindi / Chi-Wei Chiu / Karen Yang / Meng-Hsuan Wen / Tai-Yen Chen / Yu-Shan Cheng

    Journal of physical chemistry. 2018 Nov. 01, v. 122, no. 46

    2018  

    Abstract: Transitions between different oligomeric states of membrane proteins are essential for proper cellular functions. However, the quantification of their oligomeric states in cells is technically challenging. Here we developed a new method to quantify ... ...

    Abstract Transitions between different oligomeric states of membrane proteins are essential for proper cellular functions. However, the quantification of their oligomeric states in cells is technically challenging. Here we developed a new method to quantify oligomeric state(s) of highly expressed membrane proteins using the probability density function of molecule density (PDFMD) calculated from super-resolution localizations. We provided the theoretical model of PDFMD, discussed the effects of protein concentration, cell geometry, and photophysics of fluorescent proteins on PDFMD, and provided experimental criteria for proper quantification of oligomeric states. This method was further validated using simulated single-molecule fluorescent movies and applied to two membrane proteins, UhpT and SbmA in E. coli. The study shows that PDFMD is useful in quantifying oligomeric states of membrane proteins in cells that can help in understanding cellular tasks. Potential applications to proteins with higher oligomeric states under high concentration and limitations of our methodology were also discussed.
    Keywords Escherichia coli ; fluorescence ; fluorescent proteins ; geometry ; membrane proteins ; physical chemistry ; probability distribution ; theoretical models
    Language English
    Dates of publication 2018-1101
    Size p. 10496-10504.
    Publishing place American Chemical Society
    Document type Article
    ISSN 1520-5207
    DOI 10.1021/acs.jpcb.8b10402
    Database NAL-Catalogue (AGRICOLA)

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  7. Article ; Online: Quantifying the Oligomeric States of Membrane Proteins in Cells through Super-Resolution Localizations.

    Xie, Xihong / Cheng, Yu-Shan / Wen, Meng-Hsuan / Calindi, Aparna / Yang, Karen / Chiu, Chi-Wei / Chen, Tai-Yen

    The journal of physical chemistry. B

    2018  Volume 122, Issue 46, Page(s) 10496–10504

    Abstract: Transitions between different oligomeric states of membrane proteins are essential for proper cellular functions. However, the quantification of their oligomeric states in cells is technically challenging. Here we developed a new method to quantify ... ...

    Abstract Transitions between different oligomeric states of membrane proteins are essential for proper cellular functions. However, the quantification of their oligomeric states in cells is technically challenging. Here we developed a new method to quantify oligomeric state(s) of highly expressed membrane proteins using the probability density function of molecule density ( PDF
    MeSH term(s) Escherichia coli/chemistry ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/metabolism ; Membrane Transport Proteins/chemistry ; Membrane Transport Proteins/metabolism ; Microscopy ; Models, Chemical ; Models, Theoretical ; Monosaccharide Transport Proteins/chemistry ; Monosaccharide Transport Proteins/metabolism ; Protein Multimerization
    Chemical Substances Escherichia coli Proteins ; Membrane Transport Proteins ; Monosaccharide Transport Proteins ; SbmA protein, E coli ; UhpT protein, E coli
    Language English
    Publishing date 2018-11-12
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1520-5207
    ISSN (online) 1520-5207
    DOI 10.1021/acs.jpcb.8b10402
    Database MEDical Literature Analysis and Retrieval System OnLINE

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