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ProteomicsCross-Linking Mass Spectrometry (CXMS) of human pre-60S ribosomal particles
Cross-Linking Mass Spectrometry (CXMS) analysis of human pre-60S ribosomal particles.
ORGANISM(S): Homo Sapiens 
PXD019025 |
ProteomicsProteomics analysis of human pre-40S ribosomal particles
Proteomics analysis of late human pre-40S particles purified using a catalytically-inactive RIO1 as bait. Analysis of RIO1(kd)-StHA pre-40S particles composition upon RPS26 depletion with siRNA.
ORGANISM(S): Homo sapiens (Human) 
2021-05-12 | PXD019270 | Pride
Ribosomal particles 
ProteomicsProteomics analysis of Tsr1-purified yeast pre-40S particles
Proteomics analysis of pre-40S ribosomal particles.
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2020-03-09 | PXD016577 | Pride
Tsr1 Ribosome Pre-40s particles 
ProteomicsStructure of the AAA-ATPase Drg1 during extraction of Rlp24 from pre-60S particles
The AAA-ATPase Drg1 is a key factor in eukaryotic ribosome biogenesis that initiates cytoplasmic maturation of the large ribosomal subunit. Drg1 releases the shuttling maturation factor Rlp24 from pre-60S particles shortly after nuclear export, a strict requirement for downstream maturation. The mol...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-10-14 | PXD032098 | Pride
Large ribosomal subunit Ribosome biogenesis Aaa-atpases Substrate recognition Substrate translocation mechanism Single particle cryo-em 
ProteomicsBottom-up and top-down LC-MS/MS of ribosomal purifications
Ribosomal purifications of spinach 70S ribosome and human 40S and 60S ribosomal subunits were analyzed with bottom-up LC-MS/MS to identify proteins comprising purified complexes as well as co-purified proteins. In order to assess and quantify proteoforms of ribosomal proteins in ribosomal purificati...
ORGANISM(S): Spinacia oleracea Homo sapiens (Human) Escherichia coli 
2018-06-26 | PXD008881 | Pride
Ribosome Top-down Bottom-up 
UnknownSequential protein association with nascent 60S ribosomal particles.
Not available
S-EPMC164837 | biostudies-literature
ProteomicsExploration of the proxiOME of large subunit ribosomal proteins reveals Acl1 and Bcl1 as cooperating dedicated chaperones of Rpl1
In eukaryotes, most newly synthesized ribosomal proteins (r-proteins) need to rapidly and safely get into the nucleus to reach their assembly site on pre-ribosomal particles. However, only for few r-proteins tailored support mechanisms involving so-called dedicated chaperones could so far be reveale...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2026-04-14 | PXD070550 | Pride
Acl1  bcl1  ul1  dedicated chaperone  ribosomal protein  ribosome biogenesis  nuclear import  importin  karyopherin  yeast  turboid  proximity labelling  proxiome. 
UnknownYeast ribosomal protein L7 and its homologue Rlp7 are simultaneously present at distinct sites on pre-60S ribosomal particles.
Not available
S-EPMC3814368 | biostudies-literature
ProteomicsA comprehensive view on r- protein binding and rRNA domain structuring during early ribosome formation
Formation of the eukaryotic ribosomal subunits follows a strict regime to assemble ribosomal proteins (r-protein) with ribosomal RNAs (rRNA) while removing internal (ITS) and external (ETS) transcribed rRNA spacers. During early stages of large subunit (LSU) formation, ITS2 together with six assembl...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2026-02-02 | PXD058994 | Pride
Ribosome biogenesis Single particle cryo-em Lsu assembly Ssu processome Rrna domain folding Ribosomal protein assembly 
UnknownStructural snapshot of cytoplasmic pre-60S ribosomal particles bound by Nmd3, Lsg1, Tif6 and Reh1.
Not available
S-EPMC5555584 | biostudies-literature
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