Evidence map›Paper›PMID 29158258›Full record

ArticleThe Journal of biological chemistry2018

A photo-cross-linking approach to monitor folding and assembly of newly synthesized proteins in a living cell.

Ryoji Miyazaki, Naomi Myougo, Hiroyuki Mori, Yoshinori Akiyama

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
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

7 citing papers in PubMed.

  1. Genetically encoded crosslinkers to address protein-protein interactions.Protein science : a publication of the Protein Society · 2023
    Review
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  3. Article
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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

4 authors.

Ryoji MiyazakiFrom the Institute for Frontier Life and Medical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8507, Japan.
Naomi MyougoFrom the Institute for Frontier Life and Medical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8507, Japan.
Hiroyuki MoriFrom the Institute for Frontier Life and Medical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8507, Japan.
Yoshinori AkiyamaFrom the Institute for Frontier Life and Medical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8507, Japan yakiyama@infront.kyoto-u.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many proteins form multimeric complexes that play crucial roles in various cellular processes. Studying how proteins are correctly folded and assembled into such complexes in a living cell is important for understanding the physiological roles and the qualitative and quantitative regulation of the complex. However, few methods are suitable for analyzing these rapidly occurring processes. Site-directed

Indexed as

Amino AcidsBenzophenonesEscherichia coliEscherichia coli ProteinsPhenylalanineProtein BindingProtein Interaction MappingProteins4-benzoylphenylalanineAmino AcidsBenzophenonesEscherichia coli ProteinsPhenylalanineProteinsamber suppressionEscherichia coli (E. coli)p-benzoyl-L-phenylalanine (pBPA)protein assemblyprotein dynamicprotein–protein interactionprotein synthesisunnatural amino acid

Identifiers

PMID29158258
PMCPMC5767871

What OpenQuestion holds

Textmetadata
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.