Y. Chook | University of Texas Southwestern Medical Center at Dallas (original) (raw)

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Papers by Y. Chook

Research paper thumbnail of Crystal structure of Karyopherin-beta2 in complex with FUS PY-NLS(P525L)

Research paper thumbnail of Pictures in cell biology. Structures of nuclear-transport components

The past three years have seen the solution of several nuclear transport component structures and... more The past three years have seen the solution of several nuclear transport component structures and recently of the structure of a regulator bound to part of a nuclear pore complex (NPC) protein. These structures have provided a wealth of valuable information about the proteins involved and suggested strategies for further investigation of their properties. We do not have space here to go into detail about this information, so instead we are illustrating the structures and providing primary references enabling interested readers to find further information. On this page, we are concentrating on the GTPase Ran and proteins that modulate its activity, and on the facing page are the other transport factors, some of which also interact directly with Ran. Notably absent at the moment are the nuclear pore complex component s, apart from one domain of RanBP2. Only when theses are characterized fully will we really be able to understand how transport substrates move across the nuclear envelope.

Research paper thumbnail of Crystal Structure of KPT-185 bound to CRM1 (537-DLTVK-541 to GLCEQ)

Research paper thumbnail of Crystal structure of human Karyopherin-beta2 bound to the histone H3 tail

Research paper thumbnail of Karyopherin Beta2/Transportin-hnRNPM NLS Complex

Research paper thumbnail of Crystal structure of CRM1/Snurportin-1 complex

Research paper thumbnail of Structure of the Karyopherin BETA2-RAN GPPNHP Nuclear Transport Complex

Research paper thumbnail of Karyopherin Beta2/Transportin-M9NLS

Research paper thumbnail of Karyopherin beta2/transportin

Research paper thumbnail of Crystal Structure of CPEB4 NES Reverse Mutant Peptide in complex with CRM1-Ran-RanBP1

Research paper thumbnail of Crystal Structure of PKI NES Flip Mutant Peptide in complex with CRM1-Ran-RanBP1

Research paper thumbnail of Crystal structure of CRM1 inhibitor Leptomycin B in complex with CRM1(K541Q,K542Q,R543S,K545Q,K548Q,K579Q)-Ran-RanBP1

Research paper thumbnail of Crystal structure of CRM1(T539S)-Ran-RanBP1 with weakly bound unmodeled Leptomycin B

Research paper thumbnail of Crystal structure of CRM1 inhibitor Leptomycin B in complex with CRM1(537DLTVK541/GLCEQ)-Ran-RanBP1

Research paper thumbnail of Crystal structure of CRM1 inhibitor Leptomycin B in complex with CRM1(K548A)-Ran-RanBP1

Research paper thumbnail of Crystal structure of KPT251 in complex with CRM1-Ran-RanBP1

Research paper thumbnail of Crystal structure of KPT185 in complex with CRM1-Ran-RanBP1

Research paper thumbnail of Crystal structure of KAP beta2-PY-NLS

Research paper thumbnail of Crystal structure of CRM1 inhibitor Leptomycin B in complex with CRM1(R543S,K548E,K579Q)-Ran-RanBP1

Research paper thumbnail of Next-generation XPO1 inhibitor shows improved efficacy and in vivo tolerability in hematological malignancies

Leukemia

The nuclear export receptor, Exportin 1 (XPO1), mediates transport of growth-regulatory proteins ... more The nuclear export receptor, Exportin 1 (XPO1), mediates transport of growth-regulatory proteins including tumor suppressors and is overactive in many cancers, including chronic lymphocytic leukemia (CLL), acute myeloid leukemia (AML), and aggressive lymphomas. Oral Selective Inhibitor of Nuclear Export (SINE) compounds that block XPO1 function were recently identified and hold promise as a new therapeutic paradigm in many neoplasms. One of these compounds, KPT-330 (selinexor), has made progress in Phase I/II clinical trials, but systemic toxicities limit its administration to twice-per-week and requiring supportive care. We designed a new generation SINE compound, KPT-8602, with a similar mechanism of XPO1 inhibition and potency but considerably improved tolerability. Efficacy of KPT-8602 was evaluated in preclinical animal Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:

Research paper thumbnail of Crystal structure of Karyopherin-beta2 in complex with FUS PY-NLS(P525L)

Research paper thumbnail of Pictures in cell biology. Structures of nuclear-transport components

The past three years have seen the solution of several nuclear transport component structures and... more The past three years have seen the solution of several nuclear transport component structures and recently of the structure of a regulator bound to part of a nuclear pore complex (NPC) protein. These structures have provided a wealth of valuable information about the proteins involved and suggested strategies for further investigation of their properties. We do not have space here to go into detail about this information, so instead we are illustrating the structures and providing primary references enabling interested readers to find further information. On this page, we are concentrating on the GTPase Ran and proteins that modulate its activity, and on the facing page are the other transport factors, some of which also interact directly with Ran. Notably absent at the moment are the nuclear pore complex component s, apart from one domain of RanBP2. Only when theses are characterized fully will we really be able to understand how transport substrates move across the nuclear envelope.

Research paper thumbnail of Crystal Structure of KPT-185 bound to CRM1 (537-DLTVK-541 to GLCEQ)

Research paper thumbnail of Crystal structure of human Karyopherin-beta2 bound to the histone H3 tail

Research paper thumbnail of Karyopherin Beta2/Transportin-hnRNPM NLS Complex

Research paper thumbnail of Crystal structure of CRM1/Snurportin-1 complex

Research paper thumbnail of Structure of the Karyopherin BETA2-RAN GPPNHP Nuclear Transport Complex

Research paper thumbnail of Karyopherin Beta2/Transportin-M9NLS

Research paper thumbnail of Karyopherin beta2/transportin

Research paper thumbnail of Crystal Structure of CPEB4 NES Reverse Mutant Peptide in complex with CRM1-Ran-RanBP1

Research paper thumbnail of Crystal Structure of PKI NES Flip Mutant Peptide in complex with CRM1-Ran-RanBP1

Research paper thumbnail of Crystal structure of CRM1 inhibitor Leptomycin B in complex with CRM1(K541Q,K542Q,R543S,K545Q,K548Q,K579Q)-Ran-RanBP1

Research paper thumbnail of Crystal structure of CRM1(T539S)-Ran-RanBP1 with weakly bound unmodeled Leptomycin B

Research paper thumbnail of Crystal structure of CRM1 inhibitor Leptomycin B in complex with CRM1(537DLTVK541/GLCEQ)-Ran-RanBP1

Research paper thumbnail of Crystal structure of CRM1 inhibitor Leptomycin B in complex with CRM1(K548A)-Ran-RanBP1

Research paper thumbnail of Crystal structure of KPT251 in complex with CRM1-Ran-RanBP1

Research paper thumbnail of Crystal structure of KPT185 in complex with CRM1-Ran-RanBP1

Research paper thumbnail of Crystal structure of KAP beta2-PY-NLS

Research paper thumbnail of Crystal structure of CRM1 inhibitor Leptomycin B in complex with CRM1(R543S,K548E,K579Q)-Ran-RanBP1

Research paper thumbnail of Next-generation XPO1 inhibitor shows improved efficacy and in vivo tolerability in hematological malignancies

Leukemia

The nuclear export receptor, Exportin 1 (XPO1), mediates transport of growth-regulatory proteins ... more The nuclear export receptor, Exportin 1 (XPO1), mediates transport of growth-regulatory proteins including tumor suppressors and is overactive in many cancers, including chronic lymphocytic leukemia (CLL), acute myeloid leukemia (AML), and aggressive lymphomas. Oral Selective Inhibitor of Nuclear Export (SINE) compounds that block XPO1 function were recently identified and hold promise as a new therapeutic paradigm in many neoplasms. One of these compounds, KPT-330 (selinexor), has made progress in Phase I/II clinical trials, but systemic toxicities limit its administration to twice-per-week and requiring supportive care. We designed a new generation SINE compound, KPT-8602, with a similar mechanism of XPO1 inhibition and potency but considerably improved tolerability. Efficacy of KPT-8602 was evaluated in preclinical animal Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:

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