ArticleMolecular & cellular proteomics : MCP2009
Proline-rich sequence recognition: I. Marking GYF and WW domain assembly sites in early spliceosomal complexes.
Article in Molecular & cellular proteomics : MCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 31 citations in OpenAlex.
- Genome-wide identification and expression profiling of theFrontiers in plant science · 2026Article
- Review
- The nuclear GYF protein CD2BP2/U5-52K is required for T cell homeostasis.Frontiers in immunology · 2024Article
- Characterization of GEXP15 as a Potential Regulator of Protein Phosphatase 1 inInternational journal of molecular sciences · 2023Article
- A translational regulator MHZ9 modulates ethylene signaling in rice.Nature communications · 2023Article
- Large Rab GTPases: Novel Membrane Trafficking Regulators with a Calcium Sensor and Functional Domains.International journal of molecular sciences · 2021Review
- Intersectin associates with synapsin and regulates its nanoscale localization and function.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The GYF domain protein PSIG1 dampens the induction of cell death during plant-pathogen interactions.PLoS genetics · 2017Article
- Nuclear cyclophilins affect spliceosome assembly and function in vitro.The Biochemical journal · 2015Article
- Peptide-polymer ligands for a tandem WW-domain, an adaptive multivalent protein-protein interaction: lessons on the thermodynamic fitness of flexible ligands.Beilstein journal of organic chemistry · 2015Article
- Functional mammalian spliceosomal complex E contains SMN complex proteins in addition to U1 and U2 snRNPs.Nucleic acids research · 2012Article
- Article
- Intrinsic disorder in the human spliceosomal proteome.PLoS computational biology · 2012Article
- Multivalent binding of formin-binding protein 21 (FBP21)-tandem-WW domains fosters protein recognition in the pre-spliceosome.The Journal of biological chemistry · 2011Article
- Proline-rich sequence recognition: II. Proteomics analysis of Tsg101 ubiquitin-E2-like variant (UEV) interactions.Molecular & cellular proteomics : MCP · 2009Article
- Chromosome Translocation t(10;19)(q26;q13) in a CIC-sarcoma.In vivo (Athens, Greece)Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proline-rich sequences (PRS) and their recognition domains have emerged as transposable protein interaction modules during eukaryotic evolution. They are especially abundant in proteins associated with pre-mRNA splicing and likely assist in the formation of the spliceosome by binding to GYF and WW domains. Here we profile PRS-mediated interactions of the CD2BP2/52K GYF domain by a site-specific peptide inhibitor and stable isotope labeling/mass spectrometry analysis. Several PRS hubs with multiple proline-rich motifs exist that can recruit GYF and/or WW domains. Saturating the PRS sites by an isolated GYF domain inhibited splicing at the level of A complex formation. The interactions mediated by PRS are therefore important to the early phases of spliceosomal assembly.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.