Results 81 to 90 of about 13,335 (199)

Architecture of the U6 snRNP reveals specific recognition of 3′-end processed U6 snRNA

open access: yesNature Communications, 2018
The spliceosome removes introns from precursor messenger RNAs to produce mature mRNAs. Here the authors report a U6 snRNP crystal structure that provides insight on how the 3′ phosphate of U6 snRNA is recognized by the Lsm2–8 complex and how the U6 snRNP
Eric J. Montemayor   +5 more
doaj   +1 more source

Genome-wide analysis of KAP1, the 7SK snRNP complex, and RNA polymerase II

open access: yesGenomics Data, 2016
The transition of RNA polymerase II (Pol II) from transcription initiation into productive elongation in eukaryotic cells is regulated by the P-TEFb kinase, which phosphorylates the C-terminal domain of paused Pol II at promoter-proximal regions.
Ryan P. McNamara   +3 more
doaj   +1 more source

QTL analysis of high thermotolerance with superior and downgraded parental yeast strains reveals new minor QTLs and converges on novel causative alleles involved in RNA processing [PDF]

open access: yes, 2013
Revealing QTLs with a minor effect in complex traits remains difficult. Initial strategies had limited success because of interference by major QTLs and epistasis. New strategies focused on eliminating major QTLs in subsequent mapping experiments.
Clement, Lieven   +7 more
core   +3 more sources

Targeting the Spliceosomal Protein USP39 Through Allosteric Ligands and PROTAC‐Induced Degradation

open access: yesAngewandte 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

Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis [PDF]

open access: yesNature, 2011
The spliceosome is a dynamic macromolecular machine that assembles on pre-messenger RNA substrates and catalyses the excision of non-coding intervening sequences (introns). Four of the five major components of the spliceosome, U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), contain seven Sm proteins (SmB/B', SmD1, SmD2, SmD3, SmE, SmF and ...
Leung, Adelaine K. W.   +2 more
openaire   +2 more sources

An in vivo genetic screen for genes involved in spliced leader trans-splicing indicates a crucial role for continuous de novo spliced leader RNP assembly [PDF]

open access: yes, 2017
ACKNOWLEDGEMENTS Some strains were provided by the CGC, which is funded by NIH Office of Research Infrastructure Programs (P40 OD010440). We would also like to thank Prof.
Albrecht   +54 more
core   +1 more source

A Stable Bioisostere of Ester‐Linked Ubiquitin Chains Enables Decoding of Protein Interactors

open access: yesChemBioChem, Volume 27, Issue 1, January 2026.
An ester‐to‐amide analog of an ester‐linked ubiquitin dimer is chemically synthesized through a convergent approach involving the sequential chemoselective ligation of three peptide fragments generated through Fmoc‐based solid‐phase peptide synthesis. The hydrolysis‐resistant ubiquitin dimer served as a chemical probe in the identification of potential
Yoshinori Taguchi   +9 more
wiley   +1 more source

Interaction of 7SK with the Smn complex modulates snRNP production [PDF]

open access: gold, 2021
Changhe Ji   +9 more
openalex   +1 more source

Effects of the therapeutic correction of U1 snRNP complex on Alzheimer’s disease

open access: yesScientific Reports
The U1 snRNP complex recognizes pre-mRNA splicing sites in the early stages of spliceosome assembly and suppresses premature cleavage and polyadenylation. Its dysfunction may precede Alzheimer’s disease (AD) hallmarks.
Caio Bruno Q. S. Leal   +11 more
doaj   +1 more source

Activation of autophagy reverses progressive and deleterious protein aggregation in PRPF31 patient‐induced pluripotent stem cell‐derived retinal pigment epithelium cells

open access: yesClinical and Translational Medicine, 2022
Introduction Mutations in pre‐mRNA processing factor 31 (PRPF31), a core protein of the spliceosomal tri‐snRNP complex, cause autosomal‐dominant retinitis pigmentosa (adRP).
Maria Georgiou   +19 more
doaj   +1 more source

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