Results 61 to 70 of about 4,164,069 (213)

Proteomic identification of heterogeneous nuclear ribonucleoprotein L as a novel component of SLM/Sam68 nuclear bodies [PDF]

, 2009
Background: Active pre-mRNA splicing occurs co-transcriptionally, and takes place throughout the nucleoplasm of eukaryotic cells. Splicing decisions are controlled by networks of nuclear RNA-binding proteins and their target sequences, sometimes in ...
Rajan, P., Heiner, M., Leung, Hing, Dalgliesh, C., Bindereif, A, David J Elliott, Dalgliesh, C, Craig N Robson, Dalgliesh Caroline, Elliott, David, Kaveh Emami, Bindereif, A., Heiner Monika, Emami, K, Clark, E.L., Hing Y Leung, Elliott, D.J., Elliott, DJ, Rajan, Prabhakar, Leung Hing Y, Heiner, M, Bourgeois, C.F., Rajan, P, Prabhakar Rajan, Emami, K., Leung, H.Y., Elliott David J, Stevenin James, Stevenin, J., Clark Emma L, Emami, Kaveh, Bindereif, Albrecht, Bourgeois, CF, Bindereif Albrecht, Cyril F Bourgeois, Robson, C.N., Bourgeois, Cyril F, Prabhakar Rajan, Albrecht Bindereif, Heiner, Monika, Caroline Dalgliesh, Robson Craig N, Robson, Craig, Emma L Clark, Clark, EL, Dalgliesh, Caroline, Stevenin, J, Leung, HY, Stevenin, James, Robson, CN, Rajan Prabhakar, Bourgeois Cyril F, Emami Kaveh, Monika Heiner, James Stevenin, Clark, Emma   +55 more
core   +1 more source

Oncogenic DMTF1β promotes cancer cell motility by regulating autophagy through ULK1 stabilization

Molecular Oncology, EarlyView.
In the current study, we demonstrate that the oncogene DMTF1β regulates ULK1 stability by reducing its proteasomal degradation in cancer cells. This stabilization enables ULK1 to induce autophagy, which in turn facilitates cancer cell migration. Consequently, reduced DMTF1β levels lead to decreased autophagy and impaired cancer cell migration.
Jun Xu, Nicolas J. Niklaus, Anna M. Schläfli, Igor Tokarchuk, Magali Humbert, Federico La Manna, Bich Vu, David Maul, Ramin Radpour, Marianna Kruithof‐de Julio, Inti Zlobec, Jörn Dengjel, Bruce E. Torbett, Mario P. Tschan   +13 more
wiley   +1 more source

Disruption of pre-mRNA splicing in vivo results in reorganization of splicing factors [PDF]

The Journal of cell biology, 1994
We have examined the functional significance of the organization of pre-mRNA splicing factors in a speckled distribution in the mammalian cell nucleus. Upon microinjection into living cells of oligonucleotides or antibodies that inhibit pre-mRNA splicing in vitro, we observed major changes in the organization of splicing factors in vivo. Interchromatin
O'Keefe, Raymond T.; id_orcid 0000-0001-8764-1289, Mayeda, Akila, Sadowski, Cynthia L., Krainer, Adrian R., Spector, David L.   +4 more
openaire   +2 more sources

CEACAM1 participation in breast cancer progression

Molecular Oncology, EarlyView.
In invasive breast cancer (BC), CEACAM1 shifts from an apical to a uniform membranous/cytoplasmic pattern, or is lost, as tumors dedifferentiate, inversely tracking the Ki‐67 proliferative index. In MCF‐7 cells, only CEACAM1‐4L suppresses proliferation, repressing cell cycle and growth factor genes.
Mykola Lyndin, Irina Kube‐Golovin, Anatolii Romaniuk, Gunther Wennemuth   +3 more
wiley   +1 more source

An overview of RNA splicing and functioning of splicing factors in land plant chloroplasts

RNA Biology, 2022
RNA splicing refers to a process by which introns of a pre-mRNA are excised and the exons at both ends are joined together. Chloroplast introns are inherently self-splicing ribozymes, but over time, they have lost self-splicing ability due to the degeneration of intronic elements.
Xuemei Wang, Jingyi Wang, Simin Li, Congming Lu, Na Sui   +4 more
openaire   +3 more sources

Pharmacological chromatin remodeling enhances response to estrogen therapy in ER+ breast cancer

Molecular Oncology, EarlyView.
Estrogen therapy elicits clinical benefit in ~ 30% of patients with endocrine‐resistant estrogen receptor (ER)‐positive breast cancer. Based on findings that ER transcriptional activation underlies response to estrogen therapy, we tested the effects of epigenetic dysregulation via pharmacological inhibition of histone deacetylases (HDACi).
Anneka L. Johnson Thomas, Barbara Karakyriakou, Patricia C. Muskus, Alyssa M. Roberts, Justin Rendleman, Alexa Warren, Hanxu Lu, Kimberly A. Birmingham, Malone K. Friedman, Abigail E. Goen, Huijuan Yang, Owen M. Wilkins, Fred W. Kolling, Eugene Demidenko, Julie M. Jorns, Brock C. Christensen, Todd W. Miller   +16 more
wiley   +1 more source

Identifying differential exon splicing using linear models and correlation coefficients [PDF]

, 2009
Background: With the availability of the Affymetrix exon arrays a number of tools have been developed to enable the analysis. These however can be expensive or have several pre-installation requirements.
Pallas Jacqueline A, Shah, SH, Shah Sonia H, Sonia H Shah, Jacqueline A Pallas, Shah, Sonia H., Pallas, JA, Pallas, Jacqueline A.   +7 more
core   +1 more source

PANoptosis in the pathogenesis of myelodysplastic syndromes

Molecular Oncology, EarlyView.
PANoptosis, a combination of three types of programmed cell death, is mediated by a large protein complex called a PANoptosome. In healthy bone marrow hematopoietic cells, PANoptosis is restricted by inhibitory signaling. In MDS, bone marrow cells become sensitive to the PANoptotic stimuli due to the aberrant inactivation of inhibitory signaling or ...
Rohit Thalla, Jyoti Lamichhane, Cameron Lewis, Peter Breslin, Jiwang Zhang   +4 more
wiley   +1 more source

Splicing Site Recognition by Synergy of Three Domains in Splicing Factor RBM10 [PDF]

Biochemistry, 2018
Splicing factor RBM10 and its close homologues RBM5 and RBM6 govern the splicing of oncogenes such as Fas, NUMB, and Bcl-X. The molecular architecture of these proteins includes zinc fingers (ZnFs) and RNA recognition motifs (RRMs). Three of these domains in RBM10 that constitute the RNA binding part of this splicing factor were found to individually ...
Pedro Serrano, John A. Hammond, Michael Geralt, Kurt Wüthrich   +3 more
openaire   +2 more sources

Splicing-associated epitopes identified using ≤300nM.

, 2021
(A) Distribution of the number of candidate tumor-specific splicing-derived neoepitopes (splicing-epitopes) and splicing-affected self-epitopes that would be depleted in the altered isoform (self-epitopes) using ≤300nM to define candidate epitopes.
Judith Pérez-Granado (11442479), Juan L. Trincado (11442473), Ferran Sanz (89706), Marina Reixachs-Solé (11442476), Tim Fugmann (11442482), Eduardo Eyras (3024), Jun Yokota (133873)   +6 more
core   +1 more source