Results 1 to 10 of about 11,620 (128)

R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2 to regulate assembly of U5 small nuclear ribonucleoprotein [PDF]

open access: yesNature Communications, 2017
The R2TP/Prefoldin-like cochaperone complex is involved in the assembly of a number of protein complexes. Here the authors provide evidence that RUVBL1/RUVBL2, subunits of that cochaperone complex, directly interact with ZNHIT2 to regulate assembly of U5
Philippe Cloutier   +8 more
doaj   +3 more sources

Addressing the tissue specificity of U5 snRNP spliceosomopathies [PDF]

open access: yesFrontiers in Cell and Developmental Biology
Precursor mRNA (pre-mRNA) must undergo splicing to remove intron sequences and join exons. This splicing process is catalysed by an RNA/protein complex called the spliceosome.
Rahmat Azhari Kemal   +2 more
doaj   +2 more sources

Alternative splicing regulation by tumor suppressing subtransferable candidate 4: a pathway to tumor suppression [PDF]

open access: yesFrontiers in Immunology
IntroductionRNA splicing is a crucial posttranscriptional process that governs gene expression, and defects in alternative splicing contribute to various diseases, including cancer.
Haiping Zhao   +10 more
doaj   +2 more sources

Nuclear Condensates of WW Domain‐Containing Adaptor With Coiled‐Coil Regulate Mitophagy via Alternative Splicing [PDF]

open access: yesAdvanced Science
Biomolecular condensates segregate nuclei into discrete regions, facilitating the execution of distinct biological functions. Here, it is identified that the WW domain containing adaptor with coiled‐coil (WAC) is localized to nuclear speckles via its WW ...
Jiahe Wang   +13 more
doaj   +2 more sources

Interaction of Newcastle disease virus V protein with EFTUD2 modulates MDA5 pathway to suppress viral replication [PDF]

open access: yesPoultry Science
Elongation factor Tu GTP-binding domain-containing protein 2 (EFTUD2), a core component of U5 small nuclear ribonucleoprotein particles (snRNPs), recently emerged as a novel innate immune regulator.
Yin Han   +4 more
doaj   +2 more sources

U5 snRNP Core Proteins Are Key Components of the Defense Response against Viral Infection through Their Roles in Programmed Cell Death and Interferon Induction

open access: yesViruses, 2022
The spliceosome is a massive ribonucleoprotein structure composed of five small nuclear ribonucleoprotein (snRNP) complexes that catalyze the removal of introns from pre-mature RNA during constitutive and alternative splicing. EFTUD2, PRPF8, and SNRNP200
Simon Boudreault   +2 more
doaj   +1 more source

New insights into trypanosomatid U5 small nuclear ribonucleoproteins [PDF]

open access: yesMemórias do Instituto Oswaldo Cruz, 2011
Several protozoan parasites exist in the Trypanosomatidae family, including various agents of human diseases. Multiple lines of evidence suggest that important differences are present between the translational and mRNA processing (trans splicing) systems of trypanosomatids and other eukaryotes.
da Silva, Marco Tulio A.   +8 more
openaire   +6 more sources

20S small nuclear ribonucleoprotein U5 shows a surprisingly complex protein composition. [PDF]

open access: yesProceedings of the National Academy of Sciences, 1989
U5 small nuclear ribonucleoprotein (snRNP), purified from HeLa nuclear extracts (splicing extracts), shows a complex protein composition. In addition to the snRNP proteins B', B, D, D', E, F, and G, which are present in each of the major snRNPs U1, U2, U4/U6, and U5, U5 snRNP contains a number of unique proteins characterized by apparent molecular ...
M, Bach, G, Winkelmann, R, Lührmann
openaire   +2 more sources

U5 small nuclear ribonucleoprotein: RNA structure analysis and ATP-dependent interaction with U4/U6. [PDF]

open access: yesMolecular and Cellular Biology, 1989
To understand how the U5 small nuclear ribonucleoprotein (snRNP) interacts with other spliceosome components, its structure and binding to the U4/U6 snRNP were analyzed. The interaction of the U5 snRNP with the U4/U6 snRNP was studied by separating the snRNPs in HeLa cell nuclear extracts on glycerol gradients.
D L, Black, A L, Pinto
openaire   +2 more sources

SPF30 Is an Essential Human Splicing Factor Required for Assembly of the U4/U5/U6 Tri-small Nuclear Ribonucleoprotein into the Spliceosome [PDF]

open access: yesJournal of Biological Chemistry, 2001
Spliceosome assembly involves the sequential recruitment of small nuclear ribonucleoproteins (snRNPs) onto a pre-mRNA substrate. Although several non-snRNP proteins function during the binding of U1 and U2 snRNPs, little is known about the subsequent binding of the U4/U5/U6 tri-snRNP.
Rappsilber, Juri   +3 more
openaire   +5 more sources

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