Search Results - "Loughlin, Fionna E"
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Tandem RNA binding sites induce self-association of the stress granule marker protein TIA-1
Published in Nucleic acids research (18-03-2021)“…Abstract TIA-1 is an RNA-binding protein that sequesters target RNA into stress granules under conditions of cellular stress. Promotion of stress granule…”
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Aberrant interaction of FUS with the U1 snRNA provides a molecular mechanism of FUS induced amyotrophic lateral sclerosis
Published in Nature communications (11-12-2020)“…Mutations in the RNA-binding protein Fused in Sarcoma (FUS) cause early-onset amyotrophic lateral sclerosis (ALS). However, a detailed understanding of central…”
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Structural basis of pre-let-7 miRNA recognition by the zinc knuckles of pluripotency factor Lin28
Published in Nature structural & molecular biology (01-01-2012)“…Lin28 prevents the processing of pre-let-7 RNAs, but it is not clear where the Lin28 RNA binding domains interact with the RNA. The NMR structure of the Lin28…”
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The solution structure of Dead End bound to AU-rich RNA reveals an unusual mode of tandem RRM-RNA recognition required for mRNA regulation
Published in Nature communications (06-10-2022)“…Dead End (DND1) is an RNA-binding protein essential for germline development through its role in post-transcriptional gene regulation. The molecular mechanisms…”
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Regulation of TIA-1 Condensates: Zn2+ and RGG Motifs Promote Nucleic Acid Driven LLPS and Inhibit Irreversible Aggregation
Published in Frontiers in molecular biosciences (14-07-2022)“…Stress granules are non-membrane bound RNA-protein granules essential for survival during acute cellular stress. TIA-1 is a key protein in the formation of…”
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Crystal Structures of Flax Rust Avirulence Proteins AvrL567-A and -D Reveal Details of the Structural Basis for Flax Disease Resistance Specificity
Published in The Plant cell (01-09-2007)“…The gene-for-gene mechanism of plant disease resistance involves direct or indirect recognition of pathogen avirulence (Avr) proteins by plant resistance (R)…”
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zinc fingers of the SR-like protein ZRANB2 are single-stranded RNA-binding domains that recognize 5' splice site-like sequences
Published in Proceedings of the National Academy of Sciences - PNAS (07-04-2009)“…The alternative splicing of mRNA is a critical process in higher eukaryotes that generates substantial proteomic diversity. Many of the proteins that are…”
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TDP-43 and FUS–structural insights into RNA recognition and self-association
Published in Current opinion in structural biology (01-12-2019)“…•Common and unique features influence RNA interaction and self-association by TDP-43 and FUS.•TDP-43 binds RNA sequence specifically whereas FUS binds both…”
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The Solution Structure of FUS Bound to RNA Reveals a Bipartite Mode of RNA Recognition with Both Sequence and Shape Specificity
Published in Molecular cell (07-02-2019)“…Fused in sarcoma (FUS) is an RNA binding protein involved in regulating many aspects of RNA processing and linked to several neurodegenerative diseases…”
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Zinc Fingers as Protein Recognition Motifs: Structural Basis for the GATA-1/Friend of GATA Interaction
Published in Proceedings of the National Academy of Sciences - PNAS (18-01-2005)“…GATA-1 and friend of GATA (FOG) are zinc-finger transcription factors that physically interact to play essential roles in erythroid and megakaryocytic…”
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Sticky fingers: zinc-fingers as protein-recognition motifs
Published in Trends in biochemical sciences (Amsterdam. Regular ed.) (01-02-2007)“…Zinc-fingers (ZnFs) are extremely abundant in higher eukaryotes. Once considered to function exclusively as sequence-specific DNA-binding motifs, ZnFs are now…”
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Analysis of the Structure and Function of the Transcriptional Coregulator HOP
Published in Biochemistry (Easton) (05-09-2006)“…Homeodomain-only protein (HOP) is an 8-kDa transcriptional corepressor that is essential for the normal development of the mammalian heart. Previous studies…”
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Characterization of a Family of RanBP2-Type Zinc Fingers that Can Recognize Single-Stranded RNA
Published in Journal of molecular biology (25-03-2011)“…The recognition of single-stranded RNA (ssRNA) is an important aspect of gene regulation, and a number of different classes of protein domains that recognize…”
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The NMR signature of gluconoylation: a frequent N-terminal modification of isotope-labeled proteins
Published in Journal of biomolecular NMR (15-02-2019)“…N-terminal gluconoylation is a moderately widespread modification in recombinant proteins expressed in Escherichia coli , in particular in proteins bearing an…”
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TIA-1 RRM23 binding and recognition of target oligonucleotides
Published in Nucleic acids research (05-05-2017)“…TIA-1 (T-cell restricted intracellular antigen-1) is an RNA-binding protein involved in splicing and translational repression. It mainly interacts with RNA via…”
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Designed metal-binding sites in biomolecular and bioinorganic interactions
Published in Current opinion in structural biology (01-08-2008)“…The design of metal-binding functionality in proteins is expanding into many different areas with a wide range of practical and research applications. Here we…”
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Zinc fingers are known as domains for binding DNA and RNA. Do they also mediate protein‐protein interactions?
Published in IUBMB life (01-12-2006)Get full text
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Crystallization of a ZRANB2-RNA complex
Published in Acta crystallographica. Section F, Structural biology and crystallization communications (01-12-2008)“…ZRANB2 is a zinc‐finger protein that has been shown to influence alternative splice‐site selection. The protein comprises a C‐terminal arginine/serine‐rich…”
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Crystallization of a ZRANB2aRNA complex
Published in Acta crystallographica. Section F, Structural biology and crystallization communications (01-12-2008)“…ZRANB2 is a zinc-finger protein that has been shown to influence alternative splice-site selection. The protein comprises a C-terminal arginine/serine-rich…”
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