Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Jaclyn Tetenbaum-Novatt"'
Autor:
Loren E Hough, Kaushik Dutta, Samuel Sparks, Deniz B Temel, Alia Kamal, Jaclyn Tetenbaum-Novatt, Michael P Rout, David Cowburn
Publikováno v:
eLife, Vol 4 (2015)
Nuclear pore complexes (NPCs) form a selective filter that allows the rapid passage of transport factors (TFs) and their cargoes across the nuclear envelope, while blocking the passage of other macromolecules. Intrinsically disordered proteins (IDPs)
Externí odkaz:
https://doaj.org/article/4ededb97a7ec4287865fadfd89ee7512
Autor:
Jaclyn Tetenbaum-Novatt
Publikováno v:
Reference Module in Biomedical Sciences ISBN: 9780128012383
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::77bef4870d4e315d350334113254f4a0
https://doi.org/10.1016/b978-0-12-824315-2.00635-7
https://doi.org/10.1016/b978-0-12-824315-2.00635-7
Autor:
Shannon Kinney, Kristin M. Janzen, Kelly M. Shields, Jaclyn Tetenbaum-Novatt, Manas Mandal, Ryan E. Owens, Christina M. Seeger, Susan Smith, Emmeline Tran, Jamie L. Wagner, Kimberly Zitko, Justin Kinney, Lea S. Eiland
Publikováno v:
American Journal of Pharmaceutical Education. 87:100049
Autor:
Oliver I. Fregoso, Mohammad Alinoor Rahman, Jaclyn Tetenbaum-Novatt, Adrian R. Krainer, Tomoki T. Nomakuchi, Holly A. Rees, Isabel Aznarez
Publikováno v:
Cell reports
SUMMARY The splicing factor SRSF1 promotes nonsense-mediated mRNA decay (NMD), a quality control mechanism that degrades mRNAs with premature termination codons (PTCs). Here we show that transcript-bound SRSF1 increases the binding of NMD factor UPF1
Autor:
Laura Maguire, Kaushik Dutta, Michael P. Rout, Deniz B. Temel, Alia Kamal, Kathryn P. Wall, Jaclyn Tetenbaum-Novatt, Geoff Armstrong, Loren E. Hough, Samuel Sparks, David Cowburn
Publikováno v:
Biophysical Journal. 110(3)
Nuclear pore complexes form a selective filter that allows the rapid passage of transport factors and their cargoes across the nuclear envelope, while blocking the passage of other macromolecules. Intrinsically disordered proteins (IDPs) containing p
Publikováno v:
Cold Spring Harbor Symposia on Quantitative Biology. 75:567-584
The nuclear pore complex (NPC) mediates all transport between the nucleus and cytoplasm. Passage through the NPC is highly selective, yet the same channel must allow rapid specific transport of a wide range of cargoes. This chapter focuses mainly on
Autor:
Jaclyn Tetenbaum-Novatt, Samuel Sparks, Kaushik Dutta, Deniz B. Temel, Alia Kamal, Loren E. Hough, Michael P. Rout, David Cowburn
Publikováno v:
eLife, Vol 4 (2015)
eLife
eLife
Nuclear pore complexes (NPCs) form a selective filter that allows the rapid passage of transport factors (TFs) and their cargoes across the nuclear envelope, while blocking the passage of other macromolecules. Intrinsically disordered proteins (IDPs)
Autor:
Wenzhu Zhang, Brian T. Chait, Jaclyn Tetenbaum-Novatt, Michael P. Rout, Rosemary Williams, Benjamin L. Timney, Diana S. Agate
Publikováno v:
The Journal of Cell Biology
Many cargoes destined for nuclear import carry nuclear localization signals that are recognized by karyopherins (Kaps). We present methods to quantitate import rates and measure Kap and cargo concentrations in single yeast cells in vivo, providing ne
Autor:
Jaclyn Tetenbaum-Novatt, Brian T. Chait, Brian S. Imai, Caterina Strambio-De-Castillia, Michael P. Rout
Publikováno v:
Journal of Proteome Research. 4:2250-2256
A problem faced in proteomics studies is the recovery of tagged protein complexes in their native and active form. Here we describe a peptide, Bio-Ox, that mimics the immunoglobulin G (IgG) binding interface of Staphylococcus aureus Protein A, and co