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Thomas U. Schwartz

Affiliations: 
Biology Massachusetts Institute of Technology, Cambridge, MA, United States 
Area:
cellular transport processes
Website:
https://biology.mit.edu/people/thomas_schwartz
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"Thomas U. Schwartz"
Bio:

http://schwartzlab.mit.edu/site/Welcome.html
http://www.diss.fu-berlin.de/diss/servlets/MCRFileNodeServlet/FUDISS_derivate_000000000335/00_Schwartz.pdf
Thomas U. Schwartz, Ph.D., received a doctorate in biochemistry from the Free University of Berlin, Germany, in 2000. He engaged in postdoctoral research at the Rockefeller University from 2000 to 2004, and then accepted a position as an assistant professor of biology at the Massachusetts Institute of Technology. Dr. Schwartz hopes to unravel the three-dimensional structure of the nuclear pore complex that regulates the transport of molecules into and out of the cell nucleus. This large protein complex both enables the nucleus to communicate with the rest of the cell and allows certain viruses, such as HIV and hepatitis B, to enter the nucleus. Using state-of-the-art microscopic, biochemical and structural biological techniques, Dr. Schwartz proposes to purify the components of the nuclear pore complex in three subsets, then determine the shape of the overall complex by putting the three subsets together. He has already purified one of the three subcomplexes and is working on purifying the second. His results could help scientists understand how traffic moves in and out of the cell nucleus and how viruses can hijack the process, which could someday lead to new antiviral therapies.
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Mean distance: 7.93
 
SNBCP
Cross-listing: Cell Biology Tree

Parents

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Alexander Rich grad student 1996-1999 FU Berlin
 (the thesis was prepared at MIT under Alexander Rich, but submitted to the Free University of Berlin; Gutachter were Udo Heinemann and Volker A. Erdmann)
Günter Blobel post-doc 2000-2004 Rockefeller

Children

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Stephen G. Brohawn grad student 2004-2010 MIT (Neurotree)
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Publications

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Antoku S, Schwartz TU, Gundersen GG. (2023) FHODs: Nuclear tethered formins for nuclear mechanotransduction. Frontiers in Cell and Developmental Biology. 11: 1160219
Lim SM, Cruz VE, Antoku S, et al. (2021) Structures of FHOD1-Nesprin1/2 complexes reveal alternate binding modes for the FH3 domain of formins. Structure (London, England : 1993)
Nordeen SA, Andersen KR, Knockenhauer KE, et al. (2020) A nanobody suite for yeast scaffold nucleoporins provides details of the nuclear pore complex structure. Nature Communications. 11: 6179
Nordeen SA, Turman DL, Schwartz TU. (2020) Yeast Nup84-Nup133 complex structure details flexibility and reveals conservation of the membrane anchoring ALPS motif. Nature Communications. 11: 6060
Cruz VE, Esra Demircioglu F, Schwartz TU. (2020) Structural analysis of different LINC complexes reveals distinct binding modes. Journal of Molecular Biology
Sonn-Segev A, Belacic K, Bodrug T, et al. (2020) Quantifying the heterogeneity of macromolecular machines by mass photometry. Nature Communications. 11: 1772
Demircioglu FE, Zheng W, McQuown AJ, et al. (2019) The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn Nature Communications. 10: 3262-3262
Cruz VE, Schwartz TU. (2018) Recombinant Purification of the Periplasmic Portion of the LINC Complex. Methods in Molecular Biology (Clifton, N.J.). 1840: 17-23
Onischenko E, Tang JH, Andersen KR, et al. (2017) Natively Unfolded FG Repeats Stabilize the Structure of the Nuclear Pore Complex. Cell
Hanke L, Schmidt FI, Knockenhauer KE, et al. (2017) Vesicular stomatitis virus N protein-specific single-domain antibody fragments inhibit replication. Embo Reports
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