Results 61 to 70 of about 10,117 (175)
The FEBS Journal, EarlyView.Human SART3 has two RRM domains to engage with U6 snRNA for spliceosome recycling. This study reports solution structures of SART3 RRM domains and investigates the interaction between RRM and U6 snRNA. SART3 binds to the asymmetric bulge of U6 snRNA as a dimer via conserved positively charged surfaces.
Iktae Kim +8 more
wiley +1 more source
Combined Biochemical and Electron Microscopic Analyses Reveal the Architecture of the Mammalian U2 snRNP [PDF]
, 1999 The 17S U2 small nuclear ribonucleoprotein particle (snRNP) represents the active form of U2 snRNP that binds to the pre-mRNA during spliceosome assembly.
Gröning, Karsten +3 more
core +3 more sources
New Phytologist, EarlyView.Summary Circular RNAs (circRNAs) are single‐stranded, covalently closed RNA molecules that arise from exon back‐splicing. The identification and function investigation of circRNAs have been comprehensively explored in plants, however, the regulatory mechanisms are largely unknown.
Yi Ren +14 more
wiley +1 more source
Purification and characterization of pre-mRNA splicing factor SF2 from HeLa cells [PDF]
, 1990 SF2, an activity necessary for 5' splice site cleavage and lariat formation during pre-mRNA splicing in vitro, has been purified to near homogeneity from HeLa cells. The purest fraction contains only two related polypeptides of 33 kD.
Conway, G. C. +2 more
core +1 more source
Solution structures of the first and second RNA-binding domains of human U2 small nuclear ribonucleoprotein particle auxiliary factor (U2AF65) [PDF]
The EMBO Journal, 1999 The large subunit of the human U2 small nuclear ribonucleoprotein particle auxiliary factor (hU2AF(65)) is an essential RNA-splicing factor required for the recognition of the polypyrimidine tract immediately upstream of the 3' splice site. In the present study, we determined the solution structures of two hU2AF(65) fragments, corresponding to the ...
T, Ito, Y, Muto, M R, Green, S, Yokoyama
openaire +2 more sources
Angewandte Chemie, Volume 138, Issue 5, 28 January 2026.Proteolysis‐targeting Chimeras (PROTACs) ermöglichen die gezielte Degradation bislang als „undruggable“ geltende Proteine über das zelluläre Ubiquitin–Proteasom‐System. In dieser Studie identifizieren Schäfer et al. thiazolbasierte niedermolekulare Liganden, die allosterisch an die Zinkfinger‐Domäne der Ubiquitin‐spezifischen Protease 39 (USP39) binden
Daniel Schäfer +11 more
wiley +1 more source
Journal of Biological Chemistry, 1984 Autoantibodies directed against the U2 small nuclear ribonucleoprotein (snRNP) have been found in the serum of a patient with scleroderma-polymyositis overlap syndrome. This specificity, called anti-(U2)-RNP, is distinct from all previously described autoantibodies, including those that precipitate related snRNPs: anti-Sm antibodies, which react with ...
T, Mimori +3 more
openaire +2 more sources
An ATP-independent U2 small nuclear ribonucleoprotein particle/precursor mRNA complex requires both splice sites and the polypyrimidine tract. [PDF]
Proceedings of the National Academy of Sciences, 1992 A complex is formed upon incubation of a precursor mRNA (pre-mRNA) with HeLA cell nuclear extract in the absence of added ATP (-ATP complex). Pre-mRNAs with mutations in the 5' splice site, the 3' splice site, or the polypyrimidine tract did not form this complex. Once formed, the -ATP complex was stable to competition by excess pre-mRNA.
S F, Jamison, M A, Garcia-Blanco
openaire +2 more sources
Targeting the Spliceosomal Protein USP39 Through Allosteric Ligands and PROTAC‐Induced Degradation
Angewandte Chemie International Edition, Volume 65, Issue 5, 28 January 2026.Proteolysis‐targeting chimeras (PROTACs) enable degradation of proteins previously considered undruggable by harnessing the cellular ubiquitin–proteasome system. In this study, Schäfer et al. identify thiazole‐based small molecules that allosterically bind the zinc finger domain of ubiquitin‐specific protease 39 (USP39), a non‐enzymatic scaffold ...
Daniel Schäfer +11 more
wiley +1 more source
Clinical and Translational Medicine, Volume 16, Issue 1, January 2026.LncAPAT interacted with the promoter region of RPL22 to inhibit RPL22 transcriptional activity and increase the expression of MCP‐1, thereby contributing to plaque instability. Abstract Background Long non‐coding RNAs (lncRNAs) regulate macrophage inflammation and atherosclerotic plaque stability, but mechanisms need comprehensive investigations ...
Rongxia Li +8 more
wiley +1 more source