Evidence map›Paper›PMID 33077848›Full record

ArticleScientific reports2020

Quantifying the distribution of protein oligomerization degree reflects cellular information capacity.

Lena Danielli, Ximing Li, Tamir Tuller, Ramez Daniel

Erratum issuedAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Lena DanielliDepartment of Biomedical Engineering, Technion-Israel Institute of Technology, 3200003, Haifa, Israel.
Ximing LiDepartment of Biomedical Engineering, Technion-Israel Institute of Technology, 3200003, Haifa, Israel.
Tamir TullerDepartment of Biomedical Engineering, Tel Aviv University, 69978, Ramat Aviv, Israel.
Ramez DanielDepartment of Biomedical Engineering, Technion-Israel Institute of Technology, 3200003, Haifa, Israel. ramizda@bm.technion.ac.il.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The generation of information, energy and biomass in living cells involves integrated processes that optimally evolve into complex and robust cellular networks. Protein homo-oligomerization, which is correlated with cooperativity in biology, is one means of scaling the complexity of protein networks. It can play critical roles in determining the sensitivity of genetic regulatory circuits and metabolic pathways. Therefore, understanding the roles of oligomerization may lead to new approaches of probing biological functions. Here, we analyzed the frequency of protein oligomerization degree in the cell proteome of nine different organisms, and then, we asked whether there are design trade-offs between protein oligomerization, information precision and energy costs of protein synthesis. Our results indicate that there is an upper limit for the degree of protein oligomerization, possibly because of the trade-off between cellular resource limitations and the information precision involved in biochemical reaction networks. These findings can explain the principles of cellular architecture design and provide a quantitative tool to scale synthetic biological systems.

Indexed as

AnimalsBiopolymersComputational BiologyHumansProtein Interaction MappingProteinsSynthetic BiologyBiopolymersProteins

Identifiers

PMID33077848
PMCPMC7573690

What OpenQuestion holds

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Registered trials

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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.