Evidence map›Paper›PMID 18628952›Full record

ArticlePloS one2008

Protein solubility and folding enhancement by interaction with RNA.

Seong Il Choi, Kyoung Sim Han, Chul Woo Kim, Ki-Sun Ryu, Byung Hee Kim, Kyun-Hwan Kim, Seo-Il Kim, Tae Hyun Kang, Hang-Cheol Shin, Keo-Heun Lim and 3 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
1.4field-weighted citation impact, top 20% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

46 citing papers in PubMed, 69 citations in OpenAlex.

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  14. Mechanisms of TDP-43 Proteinopathy Onset and Propagation.International journal of molecular sciences · 2021
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 3 institutions in 1 country.

Seong Il ChoiInstitute of Life Science and Biotechnology, Yonsei University, Seodaemun-Gu, Seoul, Korea.
Kyoung Sim Han
Chul Woo Kim
Ki-Sun Ryu
Byung Hee Kim
Kyun-Hwan Kim
Seo-Il Kim
Tae Hyun Kang
Hang-Cheol Shin
Keo-Heun Lim
Hyo Kyung Kim
Jeong-Min Hyun
Baik L Seong
Yonsei University · KRKonkuk University · KRSoongsil University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

While basic mechanisms of several major molecular chaperones are well understood, this machinery has been known to be involved in folding of only limited number of proteins inside the cells. Here, we report a chaperone type of protein folding facilitated by interaction with RNA. When an RNA-binding module is placed at the N-terminus of aggregation-prone target proteins, this module, upon binding with RNA, further promotes the solubility of passenger proteins, potentially leading to enhancement of proper protein folding. Studies on in vitro refolding in the presence of RNA, coexpression of RNA molecules in vivo and the mutants with impaired RNA binding ability suggests that RNA can exert chaperoning effect on their bound proteins. The results suggest that RNA binding could affect the overall kinetic network of protein folding pathway in favor of productive folding over off-pathway aggregation. In addition, the RNA binding-mediated solubility enhancement is extremely robust for increasing soluble yield of passenger proteins and could be usefully implemented for high-throughput protein expression for functional and structural genomic research initiatives. The RNA-mediated chaperone type presented here would give new insights into de novo folding in vivo.

Indexed as

CytosolDNAEnhancer Elements, GeneticHumansModels, GeneticMolecular ChaperonesMutagenesis, Site-DirectedNucleic Acid ConformationProtein BindingProtein DenaturationProtein FoldingProteinsProtein Structure, TertiaryRNASolubilityDNAMolecular ChaperonesProteinsRNA

Identifiers

PMID18628952
PMCPMC2444022
OpenAlexW2079466113

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.