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Thomas U. Schwartz - Publications

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

71 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2023 Antoku S, Schwartz TU, Gundersen GG. FHODs: Nuclear tethered formins for nuclear mechanotransduction. Frontiers in Cell and Developmental Biology. 11: 1160219. PMID 37215084 DOI: 10.3389/fcell.2023.1160219  0.316
2021 Lim SM, Cruz VE, Antoku S, Gundersen GG, Schwartz TU. Structures of FHOD1-Nesprin1/2 complexes reveal alternate binding modes for the FH3 domain of formins. Structure (London, England : 1993). PMID 33472039 DOI: 10.1016/j.str.2020.12.013  0.346
2020 Nordeen SA, Andersen KR, Knockenhauer KE, Ingram JR, Ploegh HL, Schwartz TU. A nanobody suite for yeast scaffold nucleoporins provides details of the nuclear pore complex structure. Nature Communications. 11: 6179. PMID 33268786 DOI: 10.1038/s41467-020-19884-6  0.4
2020 Nordeen SA, Turman DL, Schwartz TU. Yeast Nup84-Nup133 complex structure details flexibility and reveals conservation of the membrane anchoring ALPS motif. Nature Communications. 11: 6060. PMID 33247142 DOI: 10.1038/s41467-020-19885-5  0.425
2020 Cruz VE, Esra Demircioglu F, Schwartz TU. Structural analysis of different LINC complexes reveals distinct binding modes. Journal of Molecular Biology. PMID 33058875 DOI: 10.1016/j.jmb.2020.09.019  0.383
2020 Sonn-Segev A, Belacic K, Bodrug T, Young G, VanderLinden RT, Schulman BA, Schimpf J, Friedrich T, Dip PV, Schwartz TU, Bauer B, Peters JM, Struwe WB, Benesch JLP, Brown NG, et al. Quantifying the heterogeneity of macromolecular machines by mass photometry. Nature Communications. 11: 1772. PMID 32286308 DOI: 10.1038/S41467-020-15642-W  0.345
2019 Demircioglu FE, Zheng W, McQuown AJ, Maier NK, Watson N, Cheeseman IM, Denic V, Egelman EH, Schwartz TU. The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn Nature Communications. 10: 3262-3262. DOI: 10.2210/Pdb6Oif/Pdb  0.403
2018 Cruz VE, Schwartz TU. Recombinant Purification of the Periplasmic Portion of the LINC Complex. Methods in Molecular Biology (Clifton, N.J.). 1840: 17-23. PMID 30141034 DOI: 10.1007/978-1-4939-8691-0_2  0.4
2017 Onischenko E, Tang JH, Andersen KR, Knockenhauer KE, Vallotton P, Derrer CP, Kralt A, Mugler CF, Chan LY, Schwartz TU, Weis K. Natively Unfolded FG Repeats Stabilize the Structure of the Nuclear Pore Complex. Cell. PMID 29033133 DOI: 10.1016/J.Cell.2017.09.033  0.487
2017 Hanke L, Schmidt FI, Knockenhauer KE, Morin B, Whelan SP, Schwartz TU, Ploegh HL. Vesicular stomatitis virus N protein-specific single-domain antibody fragments inhibit replication. Embo Reports. PMID 28396572 DOI: 10.15252/Embr.201643764  0.339
2016 Hanke L, Knockenhauer KE, Brewer RC, van Diest E, Schmidt FI, Schwartz TU, Ploegh HL. The Antiviral Mechanism of an Influenza A Virus Nucleoprotein-Specific Single-Domain Antibody Fragment. Mbio. 7. PMID 27965447 DOI: 10.1128/Mbio.01569-16  0.34
2016 Lawrence KS, Tapley EC, Cruz VE, Li Q, Aung K, Hart KC, Schwartz TU, Starr DA, Engebrecht J. LINC complexes promote homologous recombination in part through inhibition of nonhomologous end joining. The Journal of Cell Biology. PMID 27956467 DOI: 10.1083/Jcb.201604112  0.388
2016 Saxton RA, Knockenhauer KE, Schwartz TU, Sabatini DM. The apo-structure of the leucine sensor Sestrin2 is still elusive. Science Signaling. 9: ra92. PMID 27649739 DOI: 10.1126/Scisignal.Aah4497  0.395
2016 Demircioglu FE, Sosa BA, Ingram J, Ploegh HL, Schwartz TU. Structures of TorsinA and its disease-mutant complexed with an activator reveal the molecular basis for primary dystonia. Elife. 5. PMID 27490483 DOI: 10.7554/Elife.17983  0.438
2016 Saxton RA, Chantranupong L, Knockenhauer KE, Schwartz TU, Sabatini DM. Mechanism of arginine sensing by CASTOR1 upstream of mTORC1. Nature. PMID 27487210 DOI: 10.1038/Nature19079  0.376
2016 Apelt L, Knockenhauer KE, Leksa NC, Benlasfer N, Schwartz TU, Stelzl U. Systematic protein-protein interaction analysis reveals inter-subcomplex contacts in the nuclear pore complex. Molecular & Cellular Proteomics : McP. PMID 27194810 DOI: 10.1074/Mcp.M115.054627  0.491
2016 Truttmann MC, Cruz VE, Guo X, Engert C, Schwartz TU, Ploegh HL. The Caenorhabditis elegans Protein FIC-1 Is an AMPylase That Covalently Modifies Heat-Shock 70 Family Proteins, Translation Elongation Factors and Histones. Plos Genetics. 12: e1006023. PMID 27138431 DOI: 10.1371/Journal.Pgen.1006023  0.374
2016 Schwartz TU. The Structure Inventory of the Nuclear Pore Complex. Journal of Molecular Biology. PMID 27016207 DOI: 10.1016/J.Jmb.2016.03.015  0.473
2016 Knockenhauer KE, Schwartz TU. The Nuclear Pore Complex as a Flexible and Dynamic Gate. Cell. 164: 1162-71. PMID 26967283 DOI: 10.1016/J.Cell.2016.01.034  0.442
2016 Esra Demircioglu F, Cruz VE, Schwartz TU. Purification and Structural Analysis of SUN and KASH Domain Proteins. Methods in Enzymology. 569: 63-78. PMID 26778553 DOI: 10.1016/Bs.Mie.2015.08.011  0.502
2016 Demircioglu FE, Sosa BA, Ingram J, Ploegh HL, Schwartz TU. Author response: Structures of TorsinA and its disease-mutant complexed with an activator reveal the molecular basis for primary dystonia Elife. DOI: 10.7554/Elife.17983.019  0.352
2015 Saxton RA, Knockenhauer KE, Wolfson RL, Chantranupong L, Pacold ME, Wang T, Schwartz TU, Sabatini DM. Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway. Science (New York, N.Y.). PMID 26586190 DOI: 10.1126/Science.Aad2087  0.421
2015 Berchowitz LE, Kabachinski G, Walker MR, Carlile TM, Gilbert WV, Schwartz TU, Amon A. Regulated Formation of an Amyloid-like Translational Repressor Governs Gametogenesis. Cell. PMID 26411291 DOI: 10.1016/J.Cell.2015.08.060  0.328
2015 Ingram JR, Knockenhauer KE, Markus BM, Mandelbaum J, Ramek A, Shan Y, Shaw DE, Schwartz TU, Ploegh HL, Lourido S. Allosteric activation of apicomplexan calcium-dependent protein kinases. Proceedings of the National Academy of Sciences of the United States of America. 112: E4975-84. PMID 26305940 DOI: 10.1073/Pnas.1505914112  0.308
2015 Knockenhauer KE, Schwartz TU. Structural Characterization of Bardet-Biedl Syndrome 9 Protein (BBS9). The Journal of Biological Chemistry. PMID 26085087 DOI: 10.1074/Jbc.M115.649202  0.472
2015 Kabachinski G, Schwartz TU. The nuclear pore complex--structure and function at a glance. Journal of Cell Science. 128: 423-9. PMID 26046137 DOI: 10.1242/Jcs.083246  0.478
2015 Kelley K, Knockenhauer KE, Kabachinski G, Schwartz TU. Atomic structure of the Y complex of the nuclear pore. Nature Structural & Molecular Biology. 22: 425-31. PMID 25822992 DOI: 10.1038/Nsmb.2998  0.466
2014 Schwartz TU. Finding the missing link. Elife. 3: e03128. PMID 24867645 DOI: 10.7554/Elife.03128  0.435
2014 Ulrich A, Partridge JR, Schwartz TU. The stoichiometry of the nucleoporin 62 subcomplex of the nuclear pore in solution. Molecular Biology of the Cell. 25: 1484-92. PMID 24574455 DOI: 10.1091/Mbc.E13-12-0745  0.523
2014 Schwartz TU. Finding the missing link: The discovery of an ancient protein complex reveals the evolutionary relationships between the proteins that help to form vesicles Elife. 2014. DOI: 10.7554/eLife.03128  0.329
2013 Andersen KR, Onischenko E, Tang JH, Kumar P, Chen JZ, Ulrich A, Liphardt JT, Weis K, Schwartz TU. Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors. Elife. 2: e00745. PMID 23795296 DOI: 10.7554/Elife.00745  0.475
2013 Schwartz T. Functional insights from studies on the structure of the nuclear pore and coat protein complexes Cold Spring Harbor Perspectives in Biology. 5. PMID 23709684 DOI: 10.1101/Cshperspect.A013375  0.494
2013 Sosa BA, Kutay U, Schwartz TU. Structural insights into LINC complexes. Current Opinion in Structural Biology. 23: 285-91. PMID 23597672 DOI: 10.1016/J.Sbi.2013.03.005  0.489
2013 Bilokapic S, Schwartz TU. Structural and functional studies of the 252 kDa nucleoporin ELYS reveal distinct roles for its three tethered domains. Structure (London, England : 1993). 21: 572-80. PMID 23499022 DOI: 10.1016/J.Str.2013.02.006  0.425
2013 Rothballer A, Schwartz TU, Kutay U. LINCing complex functions at the nuclear envelope: what the molecular architecture of the LINC complex can reveal about its function. Nucleus (Austin, Tex.). 4: 29-36. PMID 23324460 DOI: 10.4161/Nucl.23387  0.527
2013 Andersen KR, Onischenko E, Tang JH, Kumar P, Chen JZ, Ulrich A, Liphardt JT, Weis K, Schwartz TU. Author response: Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors Elife. DOI: 10.7554/Elife.00745.016  0.331
2012 Bilokapic S, Schwartz TU. Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex. Proceedings of the National Academy of Sciences of the United States of America. 109: 15241-6. PMID 22955883 DOI: 10.1073/Pnas.1205151109  0.548
2012 Sosa BA, Rothballer A, Kutay U, Schwartz TU. LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins. Cell. 149: 1035-47. PMID 22632968 DOI: 10.1016/J.Cell.2012.03.046  0.508
2012 Bilokapic S, Schwartz TU. 3D ultrastructure of the nuclear pore complex. Current Opinion in Cell Biology. 24: 86-91. PMID 22244612 DOI: 10.1016/J.Ceb.2011.12.011  0.429
2011 Feng S, Li H, Zhao J, Pervushin K, Lowenhaupt K, Schwartz TU, Dröge P. Alternate rRNA secondary structures as regulators of translation. Nature Structural & Molecular Biology. 18: 169-76. PMID 21217697 DOI: 10.1038/Nsmb.1962  0.367
2010 Leksa NC, Schwartz TU. Membrane-coating lattice scaffolds in the nuclear pore and vesicle coats: commonalities, differences, challenges. Nucleus (Austin, Tex.). 1: 314-8. PMID 21327078 DOI: 10.4161/Nucl.1.4.11798  0.503
2010 Whittle JR, Schwartz TU. Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat. The Journal of Cell Biology. 190: 347-61. PMID 20696705 DOI: 10.1083/Jcb.201003092  0.47
2010 Pandya RK, Partridge JR, Love KR, Schwartz TU, Ploegh HL. A structural element within the HUWE1 HECT domain modulates self-ubiquitination and substrate ubiquitination activities. The Journal of Biological Chemistry. 285: 5664-73. PMID 20007713 DOI: 10.1074/Jbc.M109.051805  0.384
2009 Brohawn SG, Schwartz TU. Molecular architecture of the Nup84-Nup145C-Sec13 edge element in the nuclear pore complex lattice. Nature Structural & Molecular Biology. 16: 1173-7. PMID 19855394 DOI: 10.1038/Nsmb.1713  0.737
2009 Brohawn SG, Partridge JR, Whittle JR, Schwartz TU. The nuclear pore complex has entered the atomic age. Structure (London, England : 1993). 17: 1156-68. PMID 19748337 DOI: 10.1016/J.Str.2009.07.014  0.719
2009 Whittle JR, Schwartz TU. Architectural nucleoporins Nup157/170 and Nup133 are structurally related and descend from a second ancestral element. The Journal of Biological Chemistry. 284: 28442-52. PMID 19674973 DOI: 10.1074/Jbc.M109.023580  0.503
2009 Brohawn SG, Schwartz TU. A lattice model of the nuclear pore complex. Communicative & Integrative Biology. 2: 205-7. PMID 19641729 DOI: 10.4161/Cib.2.3.7873  0.74
2009 Leksa NC, Brohawn SG, Schwartz TU. The structure of the scaffold nucleoporin Nup120 reveals a new and unexpected domain architecture. Structure (London, England : 1993). 17: 1082-91. PMID 19576787 DOI: 10.1016/J.Str.2009.06.003  0.753
2009 Partridge JR, Schwartz TU. Crystallographic and biochemical analysis of the Ran-binding zinc finger domain. Journal of Molecular Biology. 391: 375-89. PMID 19505478 DOI: 10.1016/J.Jmb.2009.06.011  0.48
2008 Brohawn SG, Leksa NC, Spear ED, Rajashankar KR, Schwartz TU. Structural evidence for common ancestry of the nuclear pore complex and vesicle coats. Science (New York, N.Y.). 322: 1369-73. PMID 18974315 DOI: 10.1126/Science.1165886  0.741
2008 Boehmer T, Jeudy S, Berke IC, Schwartz TU. Structural and functional studies of Nup107/Nup133 interaction and its implications for the architecture of the nuclear pore complex. Molecular Cell. 30: 721-31. PMID 18570875 DOI: 10.1016/J.Molcel.2008.04.022  0.553
2007 Schwartz TU. Origins and evolution of cotranslational transport to the ER. Advances in Experimental Medicine and Biology. 607: 52-60. PMID 17977458 DOI: 10.1007/978-0-387-74021-8_4  0.427
2007 Jeudy S, Schwartz TU. Crystal structure of nucleoporin Nic96 reveals a novel, intricate helical domain architecture. The Journal of Biological Chemistry. 282: 34904-12. PMID 17897938 DOI: 10.1074/Jbc.M705479200  0.504
2007 Boehmer T, Schwartz TU. Purification, crystallization and preliminary X-ray analysis of a Nup107-Nup133 heterodimeric nucleoporin complex. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 63: 816-8. PMID 17768364 DOI: 10.1107/S1744309107040523  0.447
2007 Drin G, Casella JF, Gautier R, Boehmer T, Schwartz TU, Antonny B. A general amphipathic alpha-helical motif for sensing membrane curvature. Nature Structural & Molecular Biology. 14: 138-46. PMID 17220896 DOI: 10.1038/Nsmb1194  0.344
2006 Kastenholz MA, Schwartz TU, Hünenberger PH. The transition between the B and Z conformations of DNA investigated by targeted molecular dynamics simulations with explicit solvation. Biophysical Journal. 91: 2976-90. PMID 16998239 DOI: 10.1529/Biophysj.106.083667  0.309
2006 Schwartz TU, Schmidt D, Brohawn SG, Blobel G. Homodimerization of the G protein SRbeta in the nucleotide-free state involves proline cis/trans isomerization in the switch II region. Proceedings of the National Academy of Sciences of the United States of America. 103: 6823-8. PMID 16627619 DOI: 10.1073/Pnas.0602083103  0.734
2005 Schwartz TU. Modularity within the architecture of the nuclear pore complex. Current Opinion in Structural Biology. 15: 221-6. PMID 15837182 DOI: 10.1016/J.Sbi.2005.03.003  0.486
2004 Berke IC, Boehmer T, Blobel G, Schwartz TU. Structural and functional analysis of Nup133 domains reveals modular building blocks of the nuclear pore complex. The Journal of Cell Biology. 167: 591-7. PMID 15557116 DOI: 10.1083/Jcb.200408109  0.658
2004 Schwartz TU, Walczak R, Blobel G. Circular permutation as a tool to reduce surface entropy triggers crystallization of the signal recognition particle receptor beta subunit. Protein Science : a Publication of the Protein Society. 13: 2814-8. PMID 15340174 DOI: 10.1110/Ps.04917504  0.572
2003 Helmers J, Schmidt D, Glavy JS, Blobel G, Schwartz T. The beta-subunit of the protein-conducting channel of the endoplasmic reticulum functions as the guanine nucleotide exchange factor for the beta-subunit of the signal recognition particle receptor. The Journal of Biological Chemistry. 278: 23686-90. PMID 12750387 DOI: 10.1074/Jbc.C300180200  0.75
2003 Schwartz T, Blobel G. Structural basis for the function of the beta subunit of the eukaryotic signal recognition particle receptor. Cell. 112: 793-803. PMID 12654246 DOI: 10.1016/S0092-8674(03)00161-2  0.571
2002 Rothenburg S, Schwartz T, Koch-Nolte F, Haag F. Complex regulation of the human gene for the Z-DNA binding protein DLM-1 Nucleic Acids Research. 30: 993-1000. PMID 11842111 DOI: 10.1093/Nar/30.4.993  0.427
2001 Schwartz T, Behlke J, Lowenhaupt K, Heinemann U, Rich A. Structure of the DLM-1-Z-DNA complex reveals a conserved family of Z-DNA-binding proteins. Nature Structural Biology. 8: 761-5. PMID 11524677 DOI: 10.1038/Nsb0901-761  0.575
2000 Kim YG, Lowenhaupt K, Maas S, Herbert A, Schwartz T, Rich A. The Zab domain of the human RNA editing enzyme ADAR1 recognizes Z-DNA when surrounded by B-DNA Journal of Biological Chemistry. 275: 26828-26833. PMID 10843996 DOI: 10.1074/Jbc.M003477200  0.503
1999 Schwartz T, Shafer K, Lowenhaupt K, Hanlon E, Herbert A, Rich A. Crystallization and preliminary studies of the DNA-binding domain Za from ADAR1 complexed to lefthanded DNA Acta Crystallographica Section D: Biological Crystallography. 55: 1362-1364. PMID 10393308 DOI: 10.1107/S090744499900582X  0.549
1999 Kim YG, Lowenhaupt K, Schwartz T, Rich A. The interaction between Z-DNA and the Zab domain of double-stranded RNA adenosine deaminase characterized using fusion nucleases Journal of Biological Chemistry. 274: 19081-19086. PMID 10383410 DOI: 10.1074/Jbc.274.27.19081  0.523
1999 Schwartz T, Rould MA, Lowenhaupt K, Herbert A, Rich A. Crystal structure of the Zα domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA Science. 284: 1841-1845. PMID 10364558 DOI: 10.1126/Science.284.5421.1841  0.513
1999 Schwartz T, Lowenhaupt K, Kim YG, Li L, Brown BA, Herbert A, Rich A. Proteolytic dissection of Zab, the Z-DNA-binding domain of human ADAR1 Journal of Biological Chemistry. 274: 2899-2906. PMID 9915827 DOI: 10.1074/Jbc.274.5.2899  0.558
1998 Berber I, Winston W, Manoharan R, Schwartz T, Alfken J, Kim YG, Lowenhaupt K, Herbert A, Rich A. Spectroscopic characterization of a DNA-binding domain, Zα, from the editing enzyme, dsRNA adenosine deaminase: Evidence for left-handed Z-DNA in the Zα-DNA complex Biochemistry. 37: 13313-13321. PMID 9748339 DOI: 10.1021/Bi9813126  0.506
1998 Herbert A, Schade M, Lowenhaupt K, Alfken J, Schwartz T, Shlyakhtenko LS, Lyubchenko YL, Rich A. The Zalpha domain from human ADAR1 binds to the Z-DNA conformer of many different sequences. Nucleic Acids Research. 26: 3486-93. PMID 9671809 DOI: 10.1093/Nar/26.15.3486  0.509
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