Evidence map›Paper›PMID 38975783›Full record

ArticlemBio2024

Functional redundancy of ubiquitin-like sulfur-carrier proteins facilitates flexible, efficient sulfur utilization in the primordial archaeon

Ryota Hidese, Takayuki Ohira, Satsuki Sakakibara, Tsutomu Suzuki, Naoki Shigi, Shinsuke Fujiwara

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in mBio, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Ryota Hidese *Graduate School of Science, Technology and Innovation, Kobe University, Kobe, Japan.ORCID 0000-0001-9857-6099
Takayuki Ohira *Department of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, Tokyo, Japan.ORCID 0000-0002-1487-1312
Satsuki SakakibaraDepartment of Bioscience, Graduate School of Science and Technology, Kwansei-Gakuin University, Sanda, Hyogo, Japan.
Tsutomu SuzukiDepartment of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, Tokyo, Japan.ORCID 0000-0002-9731-1731
Naoki ShigiComputational Bio Big-Data Open Innovation Laboratory, National Institute of Advanced Industrial Science and Technology (AIST), Tokyo, Japan.ORCID 0000-0003-4452-8264
Shinsuke FujiwaraDepartment of Bioscience, Graduate School of Science and Technology, Kwansei-Gakuin University, Sanda, Hyogo, Japan.ORCID 0000-0003-4863-3301

Funding

MEXT | Japan Science and Technology Agency (JST) JPMJER2002MEXT | Japan Society for the Promotion of Science (JSPS) 20H02901MEXT | Japan Society for the Promotion of Science (JSPS) 21H02436, 21K19243, 24H01341Takeda Science Foundation (TSF)
6 · The paper itself

Abstract

Ubiquitin-like proteins (Ubls) in eukaryotes and bacteria mediate sulfur transfer for the biosynthesis of sulfur-containing biomolecules and form conjugates with specific protein targets to regulate their functions. Here, we investigated the functions and physiological importance of Ubls in a hyperthermophilic archaeon by constructing a series of deletion mutants. We found that the Ubls (TK1065, TK1093, and TK2118) in

Indexed as

Archaeal ProteinsSulfurThermococcusRNA, TransferUbiquitinsArchaeal ProteinsRNA, TransferSulfurUbiquitinselemental sulfurmolybdopterinthermophilic archaeatRNA thionucleosidetungstopterinubiquitin-like protein

Identifiers

PMID38975783
PMCPMC11323500

What OpenQuestion holds

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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.