Evidence map›Paper›PMID 42441850›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2026

Role of Pbr1, a putative oxidoreductase, in the ER quality control and folding of yeast Fks1 glucan synthase.

Keisuke Obara, Hiroki Okada, Guihong Tan, Shinsuke Ohnuki, Godai Suzuki, Haruka Ohtake, Karen Kubo, Farzan Ghanegolmohammadi, Shunsuke Ishizaka, Yoko Yashiroda and 13 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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

23 authors.

Keisuke Obara *Department of Biological Science, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan.ORCID 0000-0002-2441-0907
Hiroki Okada *Department of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa 277-8562, Japan.
Guihong Tan *Terrence Donnelly Centre for Cellular and Biomolecular Research and Department of Molecular Genetics, University of Toronto, Toronto, ON M5S 3E1, Canada.
Shinsuke OhnukiDepartment of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa 277-8562, Japan.
Godai SuzukiDepartment of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa 277-8562, Japan.
Haruka OhtakeDepartment of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa 277-8562, Japan.
Karen KuboDepartment of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa 277-8562, Japan.
Farzan GhanegolmohammadiDepartment of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa 277-8562, Japan.
Shunsuke IshizakaDepartment of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa 277-8562, Japan.
Yoko YashirodaMolecular Ligand Target Research Team, RIKEN Center for Sustainable Resource Science, Wako 351-0198, Japan.
Aoi OkitaDepartment of Biological Science, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan.
Emi Mishiro-SatoMolecular Structure Center, World Premier International Research Center Initiative-Institute of Transformative Bio-Molecules, Nagoya University, Nagoya 464-8602, Japan.ORCID 0000-0001-5528-4440
Kuninori SuzukiDepartment of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa 277-8562, Japan.ORCID 0000-0003-1239-1179
Yasushi TamuraFaculty of Science, Yamagata University, Yamagata 990-8560, Japan.
Rei AshineInstitute for Integrated Cell-Material Sciences, Kyoto University, Kyoto 606-8501, Japan.
Yoshiki IkedaInstitute for Integrated Cell-Material Sciences, Kyoto University, Kyoto 606-8501, Japan.
Takumi KamuraDepartment of Biological Science, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan.ORCID 0000-0001-8541-447X
Jolanda van LeeuwenCenter for Integrative Genomics, Quartier UNIL-Sorge Bâtiment Génopode, Lausanne CH-1015, Switzerland.
Brenda AndrewsTerrence Donnelly Centre for Cellular and Biomolecular Research and Department of Molecular Genetics, University of Toronto, Toronto, ON M5S 3E1, Canada.ORCID 0000-0001-6427-6493
Erfei BiDepartment of Cell and Developmental Biology, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA 19104-6058.ORCID 0000-0002-2998-3608
Nobuo N NodaInstitute for Genetic Medicine, Hokkaido University, Sapporo 060-0815, Japan.ORCID 0000-0002-6940-8069
Charles BooneTerrence Donnelly Centre for Cellular and Biomolecular Research and Department of Molecular Genetics, University of Toronto, Toronto, ON M5S 3E1, Canada.ORCID 0000-0002-3542-6760
Yoshikazu OhyaDepartment of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa 277-8562, Japan.

Funding

Cytokinesis and the Septin CytoskeletonR35GM153501 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Erfei Bi · 2024 to 2026
$2.1M
HHS | NIH (NIH) R01HG00583HHS | NIH (NIH) R35GM153501MEXT | Japan Society for the Promotion of Science (JSPS) JP19H03205MEXT | Japan Society for the Promotion of Science (JSPS) JP19K06561MEXT | Japan Society for the Promotion of Science (JSPS) JP22H02216MEXT | Japan Society for the Promotion of Science (JSPS) JP22K06141MEXT | Japan Society for the Promotion of Science (JSPS) JP23K27126MEXT | Japan Society for the Promotion of Science (JSPS) JPJS00420240017MEXT | JSPS | Japan Society for the Promotion of Science JP25H01320MEXT | JSPS | Japan Society for the Promotion of Science JP25H01321NIGMS NIH HHS R35 GM153501
6 · The paper itself

Abstract

The biogenesis of multipass membrane proteins challenges the endoplasmic reticulum (ER) quality control, particularly when transmembrane segments contain polar or charged residues required for function. Fks1, the catalytic subunit of yeast β-(1,3)-glucan synthase, exemplifies this challenge because its large multipass transmembrane architecture must support glucan synthesis at the plasma membrane while also undergoing efficient biogenesis in the ER. Here, we investigate the cellular role of

Indexed as

Endoplasmic ReticulumGlucosyltransferasesOxidoreductasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCell WallEchinocandinsMembrane ProteinsProtein FoldingEchinocandinsFKS1 protein, S cerevisiaeGlucosyltransferasesMembrane ProteinsOxidoreductasesSaccharomyces cerevisiae ProteinsER quality controlglucan synthaseyeast

Identifiers

PMID42441850
PMCPMC13389381

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.