Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The Crystal Structure of the Ubiquitin-like Domain of Ribosome Assembly Factor Ytm1 and Characterization of Its Interaction with the AAA-ATPase Midasin.

The Journal of biological chemistry - 8 Jan 2016

Romes Erin M, Sobhany Mack, Stanley Robin E

Abstract excerpt

The synthesis of eukaryotic ribosomes is a complex, energetically demanding process requiring the aid of numerous non-ribosomal factors, such as the PeBoW complex. The mammalian PeBoW complex, composed of Pes1, Bop1, and WDR12, is essential for the processing of the 32S preribosomal RNA. Previous work in Saccharomyces cerevisiae has shown that release of the homologous proteins in this complex (Nop7, Erb1, and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to ATPases Associated with Diverse Cellular Activities
Share to Cell Nucleolus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glutamic Acid

Share to Metals

Share to Ribosomes

Share to RNA Polymerase I

Share to Ubiquitin

Source

Open in PubMed Open full text

Identifiers

PMID: 26601951
DOI: 10.1074/jbc.M115.693259
PMCID: PMC4705406

Genes

MDN1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Crystal Structure of the Ubiquitin-like Domain of Ribosome Assembly Factor Ytm1 and Characterization of Its Interaction with the AAA-ATPase Midasin.PMID 26601951Read ↗

Concerted removal of the Erb1-Ytm1 complex in ribosome biogenesis relies on an elaborate interface.Semantic proximity Read ↗

The structure of Erb1-Ytm1 complex reveals the functional importance of a high-affinity binding between two β-propellers during the assembly of large ribosomal subunits in eukaryotes.Semantic proximity Read ↗

Mammalian WDR12 is a novel member of the Pes1-Bop1 complex and is required for ribosome biogenesis and cell proliferation.Semantic proximity Read ↗

Ytm1, Nop7, and Erb1 form a complex necessary for maturation of yeast 66S preribosomes.Semantic proximity Read ↗

Rei1 and Reh1 facilitate the loading of eL24Semantic proximity Read ↗

MetAP-like Ebp1 occupies the human ribosomal tunnel exit and recruits flexible rRNA expansion segmentsSemantic proximity Read ↗

Exploration of the proxiOME of large subunit ribosomal proteins reveals Acl1 and Bcl1 as cooperating dedicated chaperones of Rpl1Semantic proximity Read ↗

Interactions among Ytm1, Erb1, and Nop7 required for assembly of the Nop7-subcomplex in yeast preribosomes.Semantic proximity Read ↗

The deca-GX3 proteins Yae1-Lto1 function as adaptors recruiting the ABC protein Rli1 for iron-sulfur cluster insertionSemantic proximity Read ↗

Structure of the Human Atg13-Atg101 HORMA Heterodimer: an Interaction Hub within the ULK1 Complex.Semantic proximity Read ↗

Rrb1p, a yeast nuclear WD-repeat protein involved in the regulation of ribosome biosynthesis.Semantic proximity Read ↗

Expression and genomic analysis of midasin, a novel and highly conserved AAA protein distantly related to dyneinSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.