Evidence map›Paper›PMID 33616868›Full record

ArticleHuman cell2021

Identification of characteristic proteins at late-stage erythroid differentiation in vitro.

Koji Funato, Takaaki Abe, Ryo Kurita, Yoshihisa Watanabe, Yukio Nakamura, Shigeki Miyata, Yusuke Furukawa, Masahiro Satake

Abstract read
PubMed Publisher
In one paragraph

Article in Human cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Redox Modulation of Erythropoiesis by Selenoproteins.Biological trace element research · 2026
    Review
  2. Article
  3. Review
  4. Altered Capacity for HAntioxidants (Basel, Switzerland) · 2022
    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

8 authors.

Koji FunatoDepartment of Research and Development, Central Blood Institute, Blood Service Headquarters, Japanese Red Cross Society, Tatsumi 2-1-67, Koto-ku, Tokyo , 135-8521, Japan.
Takaaki AbeDepartment of Research and Development, Central Blood Institute, Blood Service Headquarters, Japanese Red Cross Society, Tatsumi 2-1-67, Koto-ku, Tokyo , 135-8521, Japan.
Ryo KuritaDepartment of Research and Development, Central Blood Institute, Blood Service Headquarters, Japanese Red Cross Society, Tatsumi 2-1-67, Koto-ku, Tokyo , 135-8521, Japan. r-kurita@jrc.or.jp.
Yoshihisa WatanabeDepartment of Research and Development, Central Blood Institute, Blood Service Headquarters, Japanese Red Cross Society, Tatsumi 2-1-67, Koto-ku, Tokyo , 135-8521, Japan.
Yukio NakamuraCell Engineering Division, RIKEN BioResource Center, Ibaraki, Japan.
Shigeki MiyataDepartment of Research and Development, Central Blood Institute, Blood Service Headquarters, Japanese Red Cross Society, Tatsumi 2-1-67, Koto-ku, Tokyo , 135-8521, Japan.
Yusuke FurukawaDivision of Stem Cell Regulation, Center for Molecular Medicine, Jichi Medical University, Tochigi, Japan.
Masahiro SatakeDepartment of Research and Development, Central Blood Institute, Blood Service Headquarters, Japanese Red Cross Society, Tatsumi 2-1-67, Koto-ku, Tokyo , 135-8521, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The production of red blood cells in vitro, which is useful for basic or clinical research, has been improved. Further optimization of culture protocols may facilitate erythroid differentiation from hematopoietic stem cells to red blood cells. However, the details of erythropoiesis, particularly regarding the behaviors of differentiation-related proteins, remain unclear. Here, we performed erythroid differentiation using two independent bone marrow- or cord blood-derived CD34+ cell sources and identified proteins showing reproducible differential expression in all groups. Notably, most of the proteins expressed at the early stage were downregulated during erythroid differentiation. However, seven proteins showed upregulated expression in both bone marrow cells and cord blood cells. These proteins included alpha-synuclein and selenium-binding protein 1, the roles of which have not been clarified in erythropoiesis. There is a possibility that these factors contribute to erythroid differentiation as they maintained a high expression level. These findings provide a foundation for further mechanistic studies on erythropoiesis.

Indexed as

Erythrocytesalpha-SynucleinBone Marrow CellsCell DifferentiationCells, CulturedErythropoiesisFetal BloodGene ExpressionHematopoietic Stem CellsHumansSelenium-Binding ProteinsUp-Regulationalpha-SynucleinSELENBP1 protein, humanSelenium-Binding ProteinsCD34+ cellDifferentiation-related factorErythropoiesisMass spectrometryProtein identification

Identifiers

PMID33616868

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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.