Evidence map›Paper›PMID 34732571›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

The bacterial tyrosine kinase system CpsBCD governs the length of capsule polymers.

Rei Nakamoto, Jeric Mun Chung Kwan, Jasmine Fei Li Chin, Hui Ting Ong, Josue Flores-Kim, Caroline Midonet, Michael S VanNieuwenhze, Xue Li Guan, Lok-To Sham

Open access · greenAbstract readVideo-Audio Media
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Intra-serotype variation ofMicrobiology spectrum · 2025
    Article
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  12. Influence of glycan structure on the colonization ofProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Structural basis for the recognition of the bacterial tyrosine kinase Wzc by its cognate tyrosine phosphatase Wzb.Proceedings of the National Academy of Sciences of the United States of America · 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

9 authors at 4 institutions in 2 countries.

Rei NakamotoInfectious Diseases Translational Research Programme, Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117545.ORCID 0000-0001-7807-6548
Jeric Mun Chung KwanLee Kong Chian School of Medicine, Nanyang Technological University, Singapore 308232.
Jasmine Fei Li ChinMechanobiology Institute, National University of Singapore 117411, Singapore.
Hui Ting OngMechanobiology Institute, National University of Singapore 117411, Singapore.
Josue Flores-KimDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115.ORCID 0000-0001-8282-6647
Caroline MidonetDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115.ORCID 0000-0002-3200-0297
Michael S VanNieuwenhzeDepartment of Molecular and Cellular Biochemistry, Indiana University, Bloomington, IN 47405.ORCID 0000-0001-6093-5949
Xue Li GuanLee Kong Chian School of Medicine, Nanyang Technological University, Singapore 308232.
Lok-To ShamInfectious Diseases Translational Research Programme, Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117545; lsham@nus.edu.sg.ORCID 0000-0001-9047-0310
National University of Singapore · SGHarvard University · USNanyang Technological University · SGIndiana University Bloomington · US

Funding

Supplement to Chemical Biology Studies of the Dynamics and Inhibition of Peptidoglycan BiosynthesisR35GM136365 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI VANNIEUWENHZE, MICHAEL S · 2020 to 2024
$2.0M
NIGMS NIH HHS R35 GM136365
6 · The paper itself

Abstract

Many pathogenic bacteria are encased in a layer of capsular polysaccharide (CPS). This layer is important for virulence by masking surface antigens, preventing opsonophagocytosis, and avoiding mucus entrapment. The bacterial tyrosine kinase (BY-kinase) regulates capsule synthesis and helps bacterial pathogens to survive different host niches. BY-kinases autophosphorylate at the C-terminal tyrosine residues upon external stimuli, but the role of phosphorylation is still unclear. Here, we report that the BY-kinase CpsCD is required for growth in

Indexed as

Bacterial CapsulesBacterial ProteinsGalactosyltransferasesPolysaccharides, BacterialProtein-Tyrosine KinasesStreptococcus pneumoniaeBacterial ProteinsCpsD protein, bacteriaCpsD protein, Streptococcus pneumoniaeGalactosyltransferasesPolysaccharides, BacterialProtein-Tyrosine Kinasesbacterial tyrosine kinasecapsular polysaccharideStreptococcus pneumoniae

Identifiers

PMID34732571
PMCPMC8609450
OpenAlexW3208398889

What OpenQuestion holds

Textmetadata
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.