Results 121 to 130 of about 9,261 (202)

CRM1 inhibition induces tumor cell cytotoxicity and impairs osteoclastogenesis in multiple myeloma:molecular mechanisms and therapeutic implications

, 2014
The key nuclear export protein CRM1/XPO1 may represent a promising novel therapeutic target in human multiple myeloma (MM). Here we showed that chromosome region maintenance 1 (CRM1) is highly expressed in patients with MM, plasma cell leukemia cells and
Ghobrial, I, Anderson, K C, Zhan, F, Saint Martin, J. R., Calle, Y, Gu, Y, Cea, M, Anderson, K. C., Zhan, F., Tannenbaum, D, Zhong, M. Y., Schey, S. A., Zhong, M Y, Kung, A. L., Ghobrial, I., Schey, S A, Shacham, S, Gu, Y., Calle, Y., Munshi, N. C., Acharya, C., Kauffman, M., Acharya, C, Cagnetta, A, Senapedis, W, Kashyap, T, Wu, L, Munshi, A. A., Kauffman, M, Kashyap, T., Senapedis, W., Richardson, P, Landesman, Y., Shacham, S., Wu, L., Tai, Y. T, Richardson, P., Kung, A L, Munshi, N C, Tai, Y-T, Reagan, M, Munshi, A A, Reagan, M., Tannenbaum, D., Saint-Martin, J R, CAGNETTA, ANTONIA, CEA, MICHELE, Landesman, Y   +47 more
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Crm1 locks up replication factors

The Journal of Cell Biology, 2003
![Graphic][1] Crm1 in the cell cycle. Yamaguchi/Elsevier Limiting replication to a single round per division is critical for cells, but the proteins that control the process in metazoans have remained obscure.
openaire   +2 more sources

CRM1 is a nucleocytoplasmic transport factor for HBV RNAs.

(A) HepG2-NTCP cell lysates were incubated with wide-type or mutant biotinylated pgRNA or its mutant coated magnetic beads to pull down binding proteins. Levels of CRM1 in beads elutes were detected by WB. (B) His-CRM1 and pcDNA3.1-pgRNA were transfected
Chuanjian Wu (15877596), Jingjing Wang (140791), Xiaoming Cheng (556761), Jiatong Yin (17896706), Xiyu Hu (3385730), Yurong Duan (362841), Guoguo Zhu (719139), Kaitao Zhao (3617825), Mengfei Wang (4899196), Yanan Bu (15877590), Quan Chen (163802), Yanping Xu (788986), Rong Hua (325799), Lu Zhang (50563), Yuchen Xia (9287840), Zaichao Xu (15877593), Yingcheng Zheng (8381655)   +16 more
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CRM1/XPO1 expression in pancreatic adenocarcinoma correlates with survivin expression and the proliferative activity

, 2018
© Saulino et al. CRM1/XPO1 (CRM1) is a nuclear export chaperone that mediates the export of proteins essential to growth regulation and tumor suppression. Its overexpression in tumors was found to be associated with poor prognosis.
Pamela S. Younes, Younes, Mamoun, Jennifer M. Bailey, Bailey, Jennifer M., Mamoun Younes, Younes, Pamela S., Saulino, David M., David M. Saulino   +7 more
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Nuclear Export Receptor CRM1 Recognizes Nuclear Export Signals with Diverse Conformations [PDF]

, 2019
The Chromosome Region of Maintenance 1 or CRM1 protein facilitates export of hundreds of proteins and RNA molecules from eukaryotic cell nuclei. CRM1 recognizes its protein cargoes by their 8-15 residues-long nuclear export signals or NESs, which bind to
Fung, Ho Yee Joyce
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TNF stimulates nuclear export and secretion of IL-15 by acting on CRM1 and ARF6.

PLoS ONE, 2013
Interleukin (IL)-15 is a ubiquitously expressed cytokine that in the basal state is mainly localized intracellularly, including the nucleus. Unexpectedly, tumor necrosis factor-α (TNF) time-dependently induced nuclear export of IL-15Rα and IL15.
Suidong Ouyang, Hung Hsuchou, Abba J Kastin, Weihong Pan   +3 more
doaj   +1 more source

Immunosuppressive Yersinia Effector YopM Binds DEAD Box Helicase DDX3 to Control Ribosomal S6 Kinase in the Nucleus of Host Cells.

PLoS Pathogens, 2016
Yersinia outer protein M (YopM) is a crucial immunosuppressive effector of the plaque agent Yersinia pestis and other pathogenic Yersinia species. YopM enters the nucleus of host cells but neither the mechanisms governing its nucleocytoplasmic shuttling ...
Laura Berneking, Marie Schnapp, Andreas Rumm, Claudia Trasak, Klaus Ruckdeschel, Malik Alawi, Adam Grundhoff, Alexey G Kikhney, Friedrich Koch-Nolte, Friedrich Buck, Markus Perbandt, Christian Betzel, Dmitri I Svergun, Moritz Hentschke, Martin Aepfelbacher   +14 more
doaj   +1 more source

The interaction of RNA helicase DDX3 with HIV-1 Rev-CRM1-RanGTP complex during the HIV replication cycle.

PLoS ONE, 2015
Molecular traffic between the nucleus and the cytoplasm is regulated by the nuclear pore complex (NPC), which acts as a highly selective channel perforating the nuclear envelope in eukaryotic cells.
Seyed Hanif Mahboobi, Alex A Javanpour, Mohammad R K Mofrad   +2 more
doaj   +1 more source

HIV-1 Rev/Crm1 Contacts in a Cellular Context [PDF]

, 2014
HIV-1 Rev is a protein responsible for transporting partially spliced and fully unspliced HIV-1 RNA from the nucleus. HIV-1 hijacks the cellular nuclear export factor Crm1, recruiting it to partially spliced and fully unspliced HIV-1 RNA, which contains ...
Yonis, Naomi Deena
core  

RanGTP-regulated interactions of CRM1 with nucleoporins and a shuttling DEAD-box helicase

, 1999
CRM1 is an export receptor mediating rapid nuclear exit of proteins and RNAs to the cytoplasm. CRM1 export cargoes include proteins with a leucine- rich nuclear export signal (NES) that bind directly to CRM1 in a trimeric complex with RanGTP.
Kjems, Jørgen, Bischoff, F. Ralf, Wilm, Matthias, Askjaer, Peter, Fornerod, Maarten, Ogniewski, Vera, Niehrs, Christof, Weeks, Daniel L., Ohno, Mutsuhito, Bachi, Angela, Mattaj, Iain W.   +10 more
core   +1 more source