Author

T. U. Schwartz

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell type annotation· 2 Research Focus:protein structure prediction· 2 Assay:structural biology· 2 Organism:yeast· 2 Assay:cryo-EM· 1 Organism:human· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

S. A. Nordeen· 2 shared A. J. McQuown· 1 shared D. L. Turman· 1 shared E. Demircioglu· 1 shared E. H. Egelman· 1 shared F. E. Demircioglu· 1 shared H. Ploegh· 1 shared I. M. Cheeseman· 1 shared

Activity by Year

2019-2020 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 13 mutual co-author links

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2 shared papersBiochemistry

S. A. Nordeen

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4 papers

Recent·Most cited

Structure of the yeast Nup84-Nup133 complex details flexibility and reveals universal conservation of the membrane anchoring ALPS motif

S. A. Nordeen, D. L. Turman, T. U. Schwartz

The paper reports two structures of the yeast Nup84-Nup133 complex, revealing flexibility and a conserved ALPS motif involved in membrane anchoring.

bioRxiv · Jun 19, 2020Biochemistry

A nanobody suite for yeast scaffold nucleoporins provides details of the Nuclear Pore Complex structure

S. A. Nordeen, K. R. Andersen, K. E. Knockenhauer, J. R. Ingram, H. Ploegh, T. U. Schwartz

The paper develops a set of nanobodies to study yeast nuclear pore complex subcomplexes, revealing their structures and accessible surfaces.

bioRxiv · Jun 19, 2020Biochemistry

Structural analysis of different LINC complexes reveals distinct binding modes

V. E. Cruz, F. E. Demircioglu, T. U. Schwartz

The paper solves high-resolution crystal structures of human SUN2 complexes with different KASH peptides, revealing distinct binding modes and structural elements critical for KASH interaction.

bioRxiv · Jun 19, 2020Biochemistry

The AAA+ ATPase TorsinA polymerizes into hollow tubes with a helical periodicity of 8.5 subunits per turn

E. Demircioglu, W. Zheng, A. J. McQuown, N. Maier, N. Watson, I. M. Cheeseman, V. Denic, E. H. Egelman, T. U. Schwartz

This study characterizes the oligomerization of TorsinA, revealing helical filaments with a 8.5 subunit per turn periodicity and membrane tubulation activity.

bioRxiv · Mar 4, 2019Biochemistry