ArticleEMBO reports2006
L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle.
Article in EMBO reports, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 9 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
9 citing papers in PubMed, 22 citations in OpenAlex.
- The fungal myosin I is essential for Fusarium toxisome formation.PLoS pathogens · 2018Article
- Saccharomyces cerevisiae ribosomal protein L26 is not essential for ribosome assembly and function.Molecular and cellular biology · 2012Article
- Evolutionary gain of function for the ER membrane protein Sec62 from yeast to humans.Molecular biology of the cell · 2010Article
- Nuclear alpha NAC influences bone matrix mineralization and osteoblast maturation in vivo.Molecular and cellular biology · 2010Article
- Characterisation of the nascent polypeptide-associated complex in fission yeast.Molecular biology reports · 2007Article
- L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle.EMBO reports · 2007Article
- Ribosomal protein L33 is required for ribosome biogenesis, subunit joining, and repression of GCN4 translation.Molecular and cellular biology · 2007Article
- Distinct yet linked: chaperone networks in the eukaryotic cytosol.Genome biology · 2006Review
- Ccr4-Not complex: the control freak of eukaryotic cells.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
- Retraction · 2007-11-01Falsification/Fabrication of Data · Investigation by Company/Institution ·
- Retracted
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nascent chain-associated complex (NAC) is a dimeric protein complex of archaea and eukarya that interacts with ribosomes and translating polypeptide chains. We show that, in yeast, NAC and the signal-recognition particle (SRP) share the universally conserved ribosomal protein L25 as a docking site, which is in close proximity to the ribosomal exit tunnel. The amino-terminal segment of beta-NAC was found to be required for L25 binding. Purified NAC can prevent protein aggregation in vitro and thus shows certain properties of a molecular chaperone. Interestingly, the alpha-subunit of NAC interacts with the 54 kDa subunit of SRP. Consistent with a regulatory role of NAC in protein translocation into the endoplasmic reticulum (ER), we find that deletion of NAC results in an induction of the ER stress-response pathway. These results identify L25 as a conserved interaction platform for specific cytosolic factors that guide nascent polypeptides to their proper cellular destination.
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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.