Christine S. Weirich, Ph.D.
Affiliations: | 2005 | University of California, Berkeley, Berkeley, CA, United States |
Area:
Nuclear transportGoogle:
"Christine Weirich"Mean distance: 10.61 | S | N | B | C | P |
Parents
Sign in to add mentor| Karsten Weis | grad student | 2005 | UC Berkeley | |
| (The function of the DExD/H -box protein Dbp5 in mRNA export.) | ||||
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Publications
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| Cruz VE, Weirich CS, Peddada N, et al. (2023) The DEAD-box ATPase Dbp10/DDX54 initiates peptidyl transferase center formation during 60S ribosome biogenesis. Biorxiv : the Preprint Server For Biology |
| Sekulski K, Cruz VE, Weirich CS, et al. (2023) rRNA methylation by Spb1 regulates the GTPase activity of Nog2 during 60S ribosomal subunit assembly. Nature Communications. 14: 1207 |
| Cruz VE, Sekulski K, Peddada N, et al. (2022) Sequence-specific remodeling of a topologically complex RNP substrate by Spb4. Nature Structural & Molecular Biology |
| Nerurkar P, Altvater M, Gerhardy S, et al. (2015) Eukaryotic Ribosome Assembly and Nuclear Export. International Review of Cell and Molecular Biology. 319: 107-40 |
| Nerurkar P, Altvater M, Gerhardy S, et al. (2015) Eukaryotic Ribosome Assembly and Nuclear Export International Review of Cell and Molecular Biology |
| Dossani ZY, Weirich CS, Erzberger JP, et al. (2009) Structure of the C-terminus of the mRNA export factor Dbp5 reveals the interaction surface for the ATPase activator Gle1. Proceedings of the National Academy of Sciences of the United States of America. 106: 16251-6 |
| Weirich CS, Erzberger JP, Barral Y. (2008) The septin family of GTPases: architecture and dynamics. Nature Reviews. Molecular Cell Biology. 9: 478-89 |
| John CM, Hite RK, Weirich CS, et al. (2007) The Caenorhabditis elegans septin complex is nonpolar. The Embo Journal. 26: 3296-307 |
| Weirich CS, Erzberger JP, Flick JS, et al. (2006) Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export. Nature Cell Biology. 8: 668-76 |
| Weirich CS, Erzberger JP, Berger JM, et al. (2004) The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore. Molecular Cell. 16: 749-60 |