Evidence map›Paper›PMID 34064874›Full record

ArticleMolecules (Basel, Switzerland)2021

Ca

Yuya Tanikawa, Shingo Kanemura, Dai Ito, Yuxi Lin, Motonori Matsusaki, Kimiko Kuroki, Hiroshi Yamaguchi, Katsumi Maenaka, Young-Ho Lee, Kenji Inaba and 1 more

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed, 1 pooled it
0.8field-weighted citation impact, top 34% 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

8 citing papers in PubMed, 1 synthesis or guideline pooled it, 10 citations in OpenAlex.

  1. Gene expression regulation by CaCellular & molecular biology letters · 2026
    Pooled it
  2. Review
  3. Review
  4. CaNature cell biology · 2025
    Article
  5. CaCommunications chemistry · 2025
    Article
  6. Review
  7. Article
  8. Article
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

11 authors at 6 institutions in 2 countries.

Yuya TanikawaSchool of Science and Technology, Kwansei Gakuin University, 2-1 Gakuen, Sanda 669-1337, Japan.
Shingo KanemuraSchool of Science and Technology, Kwansei Gakuin University, 2-1 Gakuen, Sanda 669-1337, Japan.ORCID 0000-0002-7012-8179
Dai ItoDepartment of Brain and Cognitive Science, Daegu Gyeongbuk Institute of Science and Technology, 333 Techno Jungang Daero, Daegu 42988, Korea.
Yuxi LinResearch Center for Bioconvergence Analysis, Korea Basic Science Institute, 162 Yeongudanji-ro, Ochang, Cheongju 28119, Korea.
Motonori MatsusakiFrontier Research Institute for Interdisciplinary Sciences, Tohoku University, 6-3 Aramakiaza Aoba, Aoba-ku, Sendai 980-8578, Japan.ORCID 0000-0002-7296-033X
Kimiko KurokiLaboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Nishi 6, Kita 12, Kita-ku, Sapporo 060-0812, Japan.
Hiroshi YamaguchiSchool of Science and Technology, Kwansei Gakuin University, 2-1 Gakuen, Sanda 669-1337, Japan.
Katsumi MaenakaLaboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Nishi 6, Kita 12, Kita-ku, Sapporo 060-0812, Japan.ORCID 0000-0002-5459-521X
Young-Ho LeeResearch Center for Bioconvergence Analysis, Korea Basic Science Institute, 162 Yeongudanji-ro, Ochang, Cheongju 28119, Korea.
Kenji InabaInstitute of Multidisciplinary Research for Advanced Materials, Tohoku University, 2-1-1 Katahira, Aoba-ku, Sendai 980-8577, Japan.ORCID 0000-0001-8229-0467
Masaki OkumuraFrontier Research Institute for Interdisciplinary Sciences, Tohoku University, 6-3 Aramakiaza Aoba, Aoba-ku, Sendai 980-8578, Japan.ORCID 0000-0001-8130-2470
Tohoku University · JPHokkaido University · JPKwansei Gakuin University · JPChungnam National University · KRDaegu Gyeongbuk Institute of Science and Technology · KRKorea Basic Science Institute · KR

Funding

Japan Agency for Medical Research and Development JP20am0101093Japan Society for the Promotion of Science 18H03978Japan Society for the Promotion of Science 19H04799Japan Society for the Promotion of Science 19K06520Japan Society for the Promotion of Science 20H04688Japan Society for the Promotion of Science 20KK0156Japan Society for the Promotion of Science 21H04758Japan Society for the Promotion of Science JP19J00893Japan Society for the Promotion of Science JP19K16092Japan Society for the Promotion of Science JP20K15969National Research Foundation of Korea NRF-2019R1A2C1004954
6 · The paper itself

Abstract

ERp57, a member of the protein disulfide isomerase family, is a ubiquitous disulfide catalyst that functions in the oxidative folding of various clients in the mammalian endoplasmic reticulum (ER). In concert with ER lectin-like chaperones calnexin and calreticulin (CNX/CRT), ERp57 functions in virtually all folding stages from co-translation to post-translation, and thus plays a critical role in maintaining protein homeostasis, with direct implication for pathology. Here, we present mechanisms by which Ca

Indexed as

CalciumCalnexinDisulfidesHumansModels, BiologicalOxidation-ReductionProtein AggregatesProtein BindingProtein Disulfide-IsomerasesProtein FoldingThermodynamicsCalciumCalnexinDisulfidesPDIA3 protein, humanProtein AggregatesProtein Disulfide-IsomerasesCa2+calnexinchaperoneendoplasmic reticulumERp57human leukocyte antigenoxidative folding

Identifiers

PMID34064874
PMCPMC8151781
OpenAlexW3161047060

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.