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Active nuclear import and passive nuclear export are the primary determinants of TDP-43 localization

Scientific reports, 2018-05, Vol.8 (1), p.7083-16, Article 7083

2018

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Mechanism of karyopherin-β2 binding and nuclear import of ALS variants FUS(P525L) and FUS(R495X)

Scientific reports, 2021-02, Vol.11 (1), p.3754-3754, Article 3754

2021

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Nuclear export receptor CRM1 recognizes diverse conformations in nuclear export signals

eLife, 2017-03, Vol.6 (3, 2017)

2017

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Structural prerequisites for CRM1-dependent nuclear export signaling peptides: accessibility, adapting conformation, and the stability at the binding site

Scientific reports, 2019-04, Vol.9 (1), p.6627-6627, Article 6627

2019

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Nuclear localization signals for four distinct karyopherin-β nuclear import systems

Biochemical journal, 2015-06, Vol.468 (3), p.353-362

2015

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Importin-9 wraps around the H2A-H2B core to act as nuclear importer and histone chaperone

eLife, 2019-03, Vol.8 (3, 2019)

2019

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Karyopherin-mediated nucleocytoplasmic transport

Nature reviews. Molecular cell biology, 2022-05, Vol.23 (5), p.307

2022

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Atomic basis of CRM1-cargo recognition, release and inhibition

Seminars in cancer biology, 2014-08, Vol.27, p.52-61

2014

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Karyopherin-β2 Recognition of a PY-NLS Variant that Lacks the Proline-Tyrosine Motif

Structure (London), 2016-10, Vol.24 (10), p.1802-1809

2016

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Nuclear import of histones

Biochemical Society transactions, 2020-12, Vol.48 (6), p.2753-2767

2020

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Structural and energetic basis of ALS-causing mutations in the atypical proline–tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS)

Proceedings of the National Academy of Sciences - PNAS, 2012-07, Vol.109 (30), p.12017-12021

2012

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NESdb: a database of NES-containing CRM1 cargoes

Molecular biology of the cell, 2012-09, Vol.23 (18), p.3673-3676

2012

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Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites

Cell, 2018-04, Vol.173 (3), p.693-705.e22

2018

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Nuclear export inhibition through covalent conjugation and hydrolysis of Leptomycin B by CRM1

Proceedings of the National Academy of Sciences - PNAS, 2013-01, Vol.110 (4), p.1303-1308

2013

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Selective inhibitors of nuclear export show that CRM1/XPO1 is a target in chronic lymphocytic leukemia

Blood, 2012-11, Vol.120 (23), p.4621-4634

2012

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LocNES: a computational tool for locating classical NESs in CRM1 cargo proteins

Bioinformatics, 2015-05, Vol.31 (9), p.1357-1365

2015

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Structural basis for leucine-rich nuclear export signal recognition by CRM1

Nature (London), 2009-04, Vol.458 (7242), p.1136-1141

2009

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Structural basis for assembly and disassembly of the CRM1 nuclear export complex

Nature structural & molecular biology, 2009-05, Vol.16 (5), p.558-560

2009

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Structural determinants of nuclear export signal orientation in binding to exportin CRM1

eLife, 2015-09, Vol.4

2015

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A murine model of hnRNPH2-related neurodevelopmental disorder reveals a mechanism for genetic compensation by Hnrnph1

The Journal of clinical investigation, 2023-07, Vol.133 (14)

2023

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Nuclear export inhibitors avert progression in preclinical models of inflammatory demyelination

Nature neuroscience, 2015-04, Vol.18 (4), p.511-520

2015

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Modular organization and combinatorial energetics of proline-tyrosine nuclear localization signals

PLoS biology, 2008-06, Vol.6 (6), p.e137-e137

2008

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Recurrent XPO1 mutations alter pathogenesis of chronic lymphocytic leukemia

Journal of hematology and oncology, 2021-01, Vol.14 (1), p.17-21, Article 17

2021

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Structure of the nuclear transport complex karyopherin-β2-Ran GppNHp

Nature (London), 1999-05, Vol.399 (6733), p.230-237

1999

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Structure-based design of a pathway-specific nuclear import inhibitor

Nature structural & molecular biology, 2007-05, Vol.14 (5), p.452-454

2007

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Protein Binding
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Biochemistry & Molecular Biology
(25)
Cell Biology
(24)
Cell Nucleus - Metabolism
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Active Transport, Cell Nucleus
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Amino Acid Sequence
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Karyopherins - Chemistry
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Exportin 1 Protein
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Proteins
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Active nuclear import and passive nuclear export are the primary determinants of TDP-43 localization

Mechanism of karyopherin-β2 binding and nuclear import of ALS variants FUS(P525L) and FUS(R495X)

Nuclear export receptor CRM1 recognizes diverse conformations in nuclear export signals

Structural prerequisites for CRM1-dependent nuclear export signaling peptides: accessibility, adapting conformation, and the stability at the binding site

Nuclear localization signals for four distinct karyopherin-β nuclear import systems

Importin-9 wraps around the H2A-H2B core to act as nuclear importer and histone chaperone

Karyopherin-mediated nucleocytoplasmic transport

Atomic basis of CRM1-cargo recognition, release and inhibition

Karyopherin-β2 Recognition of a PY-NLS Variant that Lacks the Proline-Tyrosine Motif

Nuclear import of histones

Structural and energetic basis of ALS-causing mutations in the atypical proline–tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS)

NESdb: a database of NES-containing CRM1 cargoes

Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites

Nuclear export inhibition through covalent conjugation and hydrolysis of Leptomycin B by CRM1

Selective inhibitors of nuclear export show that CRM1/XPO1 is a target in chronic lymphocytic leukemia

LocNES: a computational tool for locating classical NESs in CRM1 cargo proteins

Structural basis for leucine-rich nuclear export signal recognition by CRM1

Structural basis for assembly and disassembly of the CRM1 nuclear export complex

Structural determinants of nuclear export signal orientation in binding to exportin CRM1

A murine model of hnRNPH2-related neurodevelopmental disorder reveals a mechanism for genetic compensation by Hnrnph1

Nuclear export inhibitors avert progression in preclinical models of inflammatory demyelination

Modular organization and combinatorial energetics of proline-tyrosine nuclear localization signals

Recurrent XPO1 mutations alter pathogenesis of chronic lymphocytic leukemia

Structure of the nuclear transport complex karyopherin-β2-Ran GppNHp

Structure-based design of a pathway-specific nuclear import inhibitor

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