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The distribution of Moesin (zeige MSN Proteine) in the nucleus suggests a function in transcription and the depletion of mRNA export factors Nup98 or its interacting partner, Rae1 (zeige RAE1 Proteine), leads to the nuclear accumulation of Moesin (zeige MSN Proteine), suggesting that the nuclear function of the protein is linked to mRNA export
Nup98 provides a scaffold for poised genes and mediates Induced enhancer-promoter contacts in genetic transcription.
Nup98 associates and colocalizes with the MBD-R2/NSL and Trx complexes. Nup98 regulates transcription of Trx targets, the Hox genes.
Nup98, a virus-induced gene, was antiviral against a panel of viruses.
Study analyzed genomic interactions of full-length nucleoporins Nup98, Nup50 (zeige NUP50 Proteine), and Nup62 and found that they predominantly interacted with active genes inside the nucleoplasm, particularly those involved in developmental regulation and the cell cycle.
Nup88 (zeige NUP88 Proteine) localizes to silent loci, Sec13 (zeige SEC13 Proteine), Nup98, and a subset of FG-repeat nucleoporins bind to developmentally regulated genes undergoing transcription induction.
We demonstrated that Nup98-TopIIbeta and Nup98-SETBP1 (zeige SETBP1 Proteine) negatively regulate the XPO1 (zeige XPO1 Proteine)-mediated protein export. Our results will contribute to the understanding of the molecular mechanism by which the Nup98-fusion proteins induce tumorigenesis.
The age-associated accumulation of somatic mutations that occurs in the Nup98-HOXD13 (zeige HOXD13 Proteine) (NHD13) mouse model of leukemia progression was significantly elevated by co-expression of a PKR (zeige EIF2AK2 Proteine) transgene.
Nup50 (zeige NUP50 Proteine) dynamics are independent of importin alpha, Nup153 (zeige NUP153 Proteine), and Nup98, even though the latter two proteins also exhibit transcription-dependent mobility.
Data indicate that loss of cyclin-dependent kinase inhibitor p15 (p15Ink4b (zeige CDKN2B Proteine)) collaborates with oncogene (zeige RAB1A Proteine) fusion protein Nup98-HoxD13 (zeige HOXD13 Proteine) transgene in the development of predominantly myeloid neoplasms.
Homeobox (zeige PRRX1 Proteine) partners create more potent NUP98 fusion oncogenes than do non-homeobox (zeige PRRX1 Proteine) partners.
findings show that expression of NUP98-HOXD13 (zeige HOXD13 Proteine) impairs class switch recombination and reduces the antibody-mediated immune response, in addition to its role in leukemia
Mice expressing both the FLT3 (zeige FLT3 Proteine)/ITD and Nup98-HoxD13 (zeige HOXD13 Proteine) (NHD13) fusion gene developed acute myeloid leukemia (zeige BCL11A Proteine) with 100% penetrance
Data show that NUP98-HOXA10HD, a novel, canonical NUP98-Hox fusion, significantly enhances the self-renewal capacity of hematopoietic stem cells.
These results clearly demonstrate that Nup98 functions as a novel shuttling cofactor for Crm1 (zeige XPO1 Proteine)-mediated nuclear export in conjunction with RanBP3 (zeige RANBP3 Proteine).
A mouse model of CML blast crisis induced by cooperation between BCR/ABL (zeige ABL1 Proteine) and NUP98/HOXA9 (zeige HOXA9 Proteine)
data show that a novel nup98 was identified and it serves a role in nucleocytoplasmic trafficking similar to human NUP98.
NHA9 (NUP98-HOXA9 (zeige HOXA9 Proteine) fusion protein) deregulates the expression of key leukemic genes, including MEIS1 (zeige MEIS1 Proteine)-HOXA9 (zeige HOXA9 Proteine)-PBX3 complex, through the enhancer binding and the direct interaction of the fusion protein with HDAC (zeige HDAC3 Proteine) and p300 (zeige EP300 Proteine) transcriptional regulators
human NUP98-IQCG fusion protein could induce fatal and transplantable acute myelomonocytic leukemia in a mouse model
Importantly, binding of Nup98 to DHX9 stimulates the ATPase activity of DHX9, and a transcriptional reporter assay suggests Nup98 supports DHX9-stimulated transcription.
The second FG repeat domain of the NUP98 moiety of the NUP98-HOXA9 (zeige HOXA9 Proteine) fusion protein is important for its cell immortalization and leukemogenesis activities. NUP98-HOXA9 (zeige HOXA9 Proteine) interacts with mixed lineage leukemia (MLL (zeige MLL Proteine)) via this FG repeat domain and that, in MLL (zeige MLL Proteine)-null mice, NUP98-HOXA9 (zeige HOXA9 Proteine)-induced cell immortalization and leukemogenesis are severely inhibited.
DYNLT1 (zeige DYNLT1 Proteine) interacts with nucleoporins and plays a role in the dysregulation of gene expression and induction of hematopoietic cell proliferation by the leukemogenic nucleoporin (zeige AGFG2 Proteine) fusion, NUP98-HOXA9 (zeige HOXA9 Proteine)
the mutation order in the NUP98-rearranged pediatric AML (zeige RUNX1 Proteine) begins with the NUP98 rearrangement leading to epigenetic dysregulations then followed by mutations of critical hematopoietic transcription factors and finally, activation of the FLT3 (zeige FLT3 Proteine) signaling pathway.
These results provide novel insight into the mechanisms underlying the aberrant capability of NUP98 oncoproteins to interact with APC (zeige APC Proteine)/C(Cdc20 (zeige CDC20 Proteine)) and to interfere with its function.
Our results suggest that NA10HD increases the number of gamma-globin-transduced HSCs that engraft, leading to an elevated number of fetal hemoglobin-containing red cells.
NUP98-HOXA9 (zeige HOXA9 Proteine) ability to induce blood cell expansion is evolutionarily conserved.
The study demonstrated the association of NUP98-IQCG with CRM1, and found that NUP98-IQCG expression inhibits the CRM1-mediated nuclear export of p65 and enhances the transcriptional activity of nuclear factor-kappaB. Moreover, IQCG could be entrapped in the nucleus by NUP98-IQCG, and the fusion protein interacts with calmodulin via the IQ motif in a calcium-independent manner.
These data support a model in which Nup98 interacts with microtubules and antagonizes MCAK (zeige KIF2C Proteine) activity, thus promoting bipolar spindle assembly.
Signal-mediated nuclear import and export proceed through the nuclear pore complex (NPC), which is comprised of approximately 50 unique proteins collectively known as nucleoporins. The 98 kDa nucleoporin is generated through a biogenesis pathway that involves synthesis and proteolytic cleavage of a 186 kDa precursor protein. This cleavage results in the 98 kDa nucleoporin as well as a 96 kDa nucleoporin, both of which are localized to the nucleoplasmic side of the NPC. Rat studies show that the 98 kDa nucleoporin functions as one of several docking site nucleoporins of transport substrates. The human gene has been shown to fuse to several genes following chromosome translocations in acute myelogenous leukemia (AML) and T-cell acute lymphocytic leukemia (T-ALL). This gene is one of several genes located in the imprinted gene domain of 11p15.5, an important tumor-suppressor gene region. Alterations in this region have been associated with the Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocortical carcinoma, and lung, ovarian, and breast cancer. Alternative splicing of this gene results in several transcript variants\; however, not all variants have been fully described.
, nucleoporin 98
, nucleoporin 98-96
, nucleoporin 98kD
, nucleoporin 98kDa
, nuclear pore complex protein Nup98-Nup96-like
, nuclear pore complex protein Nup98-Nup96
, 98 kDa nucleoporin
, nuclear pore complex protein Nup98
, nucleoporin Nup98
, GLFG-repeat containing nucleoporin