Zhou Y, Ahsan F, Soukas A
bioRxiv. 2025; .
PMID: 40027662
PMC: 11870510.
DOI: 10.1101/2025.02.17.638704.
Mishra A, Van der Giessen E, Onck P
Biophys J. 2024; 124(2):215-226.
PMID: 39600095
PMC: 11788480.
DOI: 10.1016/j.bpj.2024.11.3313.
Nissen S, Weiner A, Suyama K, Bosch P, Yu M, Song S
bioRxiv. 2024; .
PMID: 39484486
PMC: 11526938.
DOI: 10.1101/2024.10.21.619498.
Panagaki F, Tapia-Rojo R, Zhu T, Milmoe N, Paracuellos P, Board S
Nat Phys. 2024; 20(7):1180-1193.
PMID: 39036650
PMC: 11254768.
DOI: 10.1038/s41567-024-02438-8.
Zheng T, Zilman A
Biophys J. 2024; 123(9):1085-1097.
PMID: 38640928
PMC: 11079998.
DOI: 10.1016/j.bpj.2024.03.027.
The nuclear pore protein NUP98 impedes LTR-driven basal gene expression of HIV-1, viral propagation, and infectivity.
Chintala K, Yandrapally S, Faiz W, Kispotta C, Sarkar S, Mishra K
Front Immunol. 2024; 15:1330738.
PMID: 38449868
PMC: 10914986.
DOI: 10.3389/fimmu.2024.1330738.
Nuclear pore dysfunction and disease: a complex opportunity.
Fare C, Rothstein J
Nucleus. 2024; 15(1):2314297.
PMID: 38383349
PMC: 10883112.
DOI: 10.1080/19491034.2024.2314297.
Nuclear-import receptors as gatekeepers of pathological phase transitions in ALS/FTD.
Khalil B, Linsenmeier M, Smith C, Shorter J, Rossoll W
Mol Neurodegener. 2024; 19(1):8.
PMID: 38254150
PMC: 10804745.
DOI: 10.1186/s13024-023-00698-1.
Structural basis for nuclear import of hepatitis B virus (HBV) nucleocapsid core.
Yang R, Ko Y, Li F, Lokareddy R, Hou C, Kim C
Sci Adv. 2024; 10(2):eadi7606.
PMID: 38198557
PMC: 10780889.
DOI: 10.1126/sciadv.adi7606.
Human RTEL1 Interacts with KPNB1 (Importin β) and NUP153 and Connects Nuclear Import to Nuclear Envelope Stability in S-Phase.
Schertzer M, Jullien L, Pinto A, Calado R, Revy P, Londono-Vallejo A
Cells. 2023; 12(24).
PMID: 38132118
PMC: 10741959.
DOI: 10.3390/cells12242798.
3D photopolymerized microstructured scaffolds influence nuclear deformation, nucleo/cytoskeletal protein organization, and gene regulation in mesenchymal stem cells.
Donnaloja F, Raimondi M, Messa L, Barzaghini B, Carnevali F, Colombo E
APL Bioeng. 2023; 7(3):036112.
PMID: 37692376
PMC: 10491463.
DOI: 10.1063/5.0153215.
Mechanisms of NURR1 Regulation: Consequences for Its Biological Activity and Involvement in Pathology.
Garcia-Yague A, Cuadrado A
Int J Mol Sci. 2023; 24(15).
PMID: 37569656
PMC: 10419244.
DOI: 10.3390/ijms241512280.
A survey of the specificity and mechanism of 1,6 hexanediol-induced disruption of nuclear transport.
Barrientos E, Otto T, Mouton S, Steen A, Veenhoff L
Nucleus. 2023; 14(1):2240139.
PMID: 37498221
PMC: 10376917.
DOI: 10.1080/19491034.2023.2240139.
Pitstop-2 and its novel derivative RVD-127 disrupt global cell dynamics and nuclear pores integrity by direct interaction with small GTPases.
Liashkovich I, Stefanello S, Vidyadharan R, Haufe G, Erofeev A, Gorelkin P
Bioeng Transl Med. 2023; 8(4):e10425.
PMID: 37476059
PMC: 10354767.
DOI: 10.1002/btm2.10425.
Augmin is a Ran-regulated spindle assembly factor.
Kraus J, Travis S, King M, Petry S
J Biol Chem. 2023; 299(6):104736.
PMID: 37086784
PMC: 10318467.
DOI: 10.1016/j.jbc.2023.104736.
Self-regulation of the nuclear pore complex enables clogging-free crowded transport.
Zheng T, Zilman A
Proc Natl Acad Sci U S A. 2023; 120(7):e2212874120.
PMID: 36757893
PMC: 9963888.
DOI: 10.1073/pnas.2212874120.
Nanoscopic investigation of C9orf72 poly-GA oligomers on nuclear membrane disruption by a photoinducible platform.
Chien H, He R, Lee C, Huang Y, Hung I, Hou K
Commun Chem. 2023; 4(1):111.
PMID: 36697556
PMC: 9814621.
DOI: 10.1038/s42004-021-00547-6.
A mass spectrometry-based approach for the identification of Kpnβ1 binding partners in cancer cells.
Okpara M, Hermann C, van der Watt P, Garnett S, Blackburn J, Leaner V
Sci Rep. 2022; 12(1):20171.
PMID: 36418423
PMC: 9684564.
DOI: 10.1038/s41598-022-24194-6.
Calcineurin dephosphorylates topoisomerase IIβ and regulates the formation of neuronal-activity-induced DNA breaks.
Delint-Ramirez I, Konada L, Heady L, Rueda R, Jacome A, Marlin E
Mol Cell. 2022; 82(20):3794-3809.e8.
PMID: 36206766
PMC: 9990814.
DOI: 10.1016/j.molcel.2022.09.012.
Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex.
Sharma A, Chowdhury R, Musser S
Commun Biol. 2022; 5(1):988.
PMID: 36123532
PMC: 9485244.
DOI: 10.1038/s42003-022-03952-2.