Search Results - "Kunze, Ruth"
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Mutational Analysis of the Nsa2 N-Terminus Reveals Its Essential Role in Ribosomal 60S Subunit Assembly
Published in International journal of molecular sciences (30-11-2020)“…The ribosome assembly factor Nsa2 is part of the Rea1-Rsa4-Nsa2 interconnected relay on nuclear pre-60S particles that is essential for 60S ribosome…”
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Correction: Mpp10 represents a platform for the interaction of multiple factors within the 90S pre-ribosome
Published in PloS one (12-06-2020)“…[This corrects the article DOI: 10.1371/journal.pone.0183272.]…”
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Mpp10 represents a platform for the interaction of multiple factors within the 90S pre-ribosome
Published in PloS one (16-08-2017)“…In eukaryotes, ribosome assembly is a highly complex process that involves more than 200 assembly factors that ensure the folding, modification and processing…”
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Probing the nucleoporin FG repeat network defines structural and functional features of the nuclear pore complex
Published in The Journal of cell biology (17-10-2011)“…Unraveling the organization of the FG repeat meshwork that forms the active transport channel of the nuclear pore complex (NPC) is key to understanding the…”
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Modular self-assembly of a Y-shaped multiprotein complex from seven nucleoporins
Published in The EMBO journal (01-02-2002)“…Now that it is likely that all yeast nucleoporins are known, one of the ultimate goals is the in vitro assembly of the entire nuclear pore complex from its ∼30…”
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Reconstitution of Nup157 and Nup145N into the Nup84 Complex[boxs]
Published in The Journal of biological chemistry (06-05-2005)“…About 30 different nucleoporins (Nups) constitute the nuclear pore complex. We have affinity-purified 28 of these nuclear pore proteins and identified new…”
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Linker Nups connect the nuclear pore complex inner ring with the outer ring and transport channel
Published in Nature structural & molecular biology (01-10-2015)“…An in vitro –reconstitution approach reveals the interactions between nuclear pore complex modules. Short motifs within linker nucleoporins connect the…”
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The Efg1–Bud22 dimer associates with the U14 snoRNP contacting the 5′ rRNA domain of an early 90S pre-ribosomal particle
Published in Nucleic acids research (11-01-2024)“…Abstract The DEAD-box helicase Dbp4 plays an essential role during the early assembly of the 40S ribosome, which is only poorly understood to date. By applying…”
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Thermophile 90S Pre-ribosome Structures Reveal the Reverse Order of Co-transcriptional 18S rRNA Subdomain Integration
Published in Molecular cell (19-09-2019)“…Eukaryotic ribosome biogenesis involves RNA folding and processing that depend on assembly factors and small nucleolar RNAs (snoRNAs). The 90S (SSU-processome)…”
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Insight into Structure and Assembly of the Nuclear Pore Complex by Utilizing the Genome of a Eukaryotic Thermophile
Published in Cell (22-07-2011)“…Despite decades of research, the structure and assembly of the nuclear pore complex (NPC), which is composed of ∼30 nucleoporins (Nups), remain elusive. Here,…”
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Coordinated Ribosomal L4 Protein Assembly into the Pre-Ribosome Is Regulated by Its Eukaryote-Specific Extension
Published in Molecular cell (04-06-2015)“…Eukaryotic ribosome biogenesis requires nuclear import and hierarchical incorporation of ∼80 ribosomal proteins (RPs) into the ribosomal RNA core. In contrast…”
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Structural Basis of the Nic96 Subcomplex Organization in the Nuclear Pore Channel
Published in Molecular cell (18-01-2008)“…Nic96 is a conserved nucleoporin that recruits the Nsp1-Nup49-Nup57 complex, a module with Phe-Gly (FG) repeats, to the central transport channel of the…”
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Monitoring Spatiotemporal Biogenesis of Macromolecular Assemblies by Pulse-Chase Epitope Labeling
Published in Molecular cell (14-09-2012)“…Many cellular proteins perform their roles within macromolecular assemblies. Hence, an understanding of how these multiprotein complexes form is a fundamental…”
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Coordinated Ribosomal L4 Protein Assembly into the Pre-Ribosome Is Regulated by Its Eukaryote-Specific Extension
Published in Molecular cell (01-06-2015)Get full text
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Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex
Published in Nature cell biology (01-07-2007)“…Nucleocytoplasmic transport occurs through nuclear pore complexes (NPCs) embedded in the nuclear envelope. Here, we discovered an unexpected role for yeast…”
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