User profiles for Yuh Min Chook
Yuh Min ChookUniversity of Texas Southwestern Medical Center at Dallas Verified email at utsouthwestern.edu Cited by 8472 |
Karyopherin-mediated nucleocytoplasmic transport
Efficient and regulated nucleocytoplasmic trafficking of macromolecules to the correct
subcellular compartment is critical for proper functions of the eukaryotic cell. The majority of the …
subcellular compartment is critical for proper functions of the eukaryotic cell. The majority of the …
[HTML][HTML] Nuclear import by karyopherin-βs: recognition and inhibition
YM Chook, KE Süel - Biochimica et Biophysica Acta (BBA)-Molecular Cell …, 2011 - Elsevier
Proteins in the karyopherin-β family mediate the majority of macromolecular transport between
the nucleus and the cytoplasm. Eleven of the 19 known human karyopherin-βs and 10 of …
the nucleus and the cytoplasm. Eleven of the 19 known human karyopherin-βs and 10 of …
Recognition of nuclear targeting signals by Karyopherin-β proteins
D Xu, A Farmer, YM Chook - Current opinion in structural biology, 2010 - Elsevier
The Karyopherin-β family of nuclear transport factors mediates the majority of nucleocytoplasmic
transport. Although each of the 19 Karyopherin-βs transports unique sets of cargos, …
transport. Although each of the 19 Karyopherin-βs transports unique sets of cargos, …
[HTML][HTML] Rules for nuclear localization sequence recognition by karyopherinβ2
…, KE Süel, TH Louis, Z Zhang, YM Chook - Cell, 2006 - cell.com
Karyopherinβ (Kapβ) proteins bind nuclear localization and export signals (NLSs and NESs)
to mediate nucleocytoplasmic trafficking, a process regulated by Ran GTPase through its …
to mediate nucleocytoplasmic trafficking, a process regulated by Ran GTPase through its …
Structure of the nuclear transport complex karyopherin-β2–Ran GppNHp
YM Chook, G Blobel - Nature, 1999 - nature.com
Transport factors in the karyopherin-β (also called importin-β) family mediate the movement
of macromolecules in nuclear–cytoplasmic transport pathways. Karyopherin-β2 (transportin) …
of macromolecules in nuclear–cytoplasmic transport pathways. Karyopherin-β2 (transportin) …
[PDF][PDF] Nuclear-import receptors reverse aberrant phase transitions of RNA-binding proteins with prion-like domains
RNA-binding proteins (RBPs) with prion-like domains (PrLDs) phase transition to functional
liquids, which can mature into aberrant hydrogels composed of pathological fibrils that …
liquids, which can mature into aberrant hydrogels composed of pathological fibrils that …
Selective inhibitors of nuclear export show that CRM1/XPO1 is a target in chronic lymphocytic leukemia
…, S Shacham, M Kauffman, YM Chook… - Blood, The Journal …, 2012 - ashpublications.org
The nuclear export protein XPO1 is overexpressed in cancer, leading to the cytoplasmic
mislocalization of multiple tumor suppressor proteins. Existing XPO1-targeting agents lack …
mislocalization of multiple tumor suppressor proteins. Existing XPO1-targeting agents lack …
Structural basis for leucine-rich nuclear export signal recognition by CRM1
…, KE Süel, LK Jackson, R Martinez, H Gu, YM Chook - Nature, 2009 - nature.com
CRM1 (also known as XPO1 and exportin 1) mediates nuclear export of hundreds of
proteins through the recognition of the leucine-rich nuclear export signal (LR-NES). Here we …
proteins through the recognition of the leucine-rich nuclear export signal (LR-NES). Here we …
[PDF][PDF] Nuclear import receptor inhibits phase separation of FUS through binding to multiple sites
Liquid-liquid phase separation (LLPS) is believed to underlie formation of biomolecular
condensates, cellular compartments that concentrate macromolecules without surrounding …
condensates, cellular compartments that concentrate macromolecules without surrounding …
Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog.
YM Chook, H Ke, WN Lipscomb - Proceedings of the …, 1993 - National Acad Sciences
We have solved the structure of a chorismate mutase (chorismate pyruvatemutase, EC 5.4.99.5),
the 1.9-A crystal structure of the monofunctional enzyme from Bacillus subtilis. The …
the 1.9-A crystal structure of the monofunctional enzyme from Bacillus subtilis. The …