Evidence map›Paper›PMID 38652697›Full record

ReviewThe Plant cell2024

The structural basis for light harvesting in organisms producing phycobiliproteins.

Donald A Bryant, Christopher J Gisriel

Open access · greenAbstract readReview
In one paragraph

Review in The Plant cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
8.2field-weighted citation impact, top 2% 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

23 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Structural proteomics reveals the functional docking interface of ferredoxin-NADPThe Plant journal : for cell and molecular biology · 2026
    Article
  7. Structural insight of a photosystem I-CpcL-phycobilisome supercomplex from a cyanobacteriumProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Antioxidants (Basel, Switzerland) · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Molecular glue for phycobilisome attachment to photosystem II inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  20. Identification and role ofFrontiers in plant science · 2025
    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

2 authors at 2 institutions in 1 country.

Donald A BryantDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA.ORCID 0000-0003-2782-5988
Christopher J GisrielDepartment of Chemistry, Yale University, New Haven, CT 06520, USA.ORCID 0000-0002-8011-0052
Pennsylvania State University · USYale University · US

Funding

Photosystem II as a model protein for understanding metalloenzyme active site assemblyK99GM140174 · NIGMS · YALE UNIVERSITY · PI GISRIEL, CHRISTOPHER · 2021 to 2022
$192k
National Science Foundation MCB-1613022NIGMS NIH HHS K99 GM140174NIH HHS K99GM140174
6 · The paper itself

Abstract

Cyanobacteria, red algae, and cryptophytes produce 2 classes of proteins for light harvesting: water-soluble phycobiliproteins (PBP) and membrane-intrinsic proteins that bind chlorophylls (Chls) and carotenoids. In cyanobacteria, red algae, and glaucophytes, phycobilisomes (PBS) are complexes of brightly colored PBP and linker (assembly) proteins. To date, 6 structural classes of PBS have been described: hemiellipsoidal, block-shaped, hemidiscoidal, bundle-shaped, paddle-shaped, and far-red-light bicylindrical. Two additional antenna complexes containing single types of PBP have also been described. Since 2017, structures have been reported for examples of all of these complexes except bundle-shaped PBS by cryogenic electron microscopy. PBS range in size from about 4.6 to 18 mDa and can include ∼900 polypeptides and bind >2000 chromophores. Cyanobacteria additionally produce membrane-associated proteins of the PsbC/CP43 superfamily of Chl a/b/d-binding proteins, including the iron-stress protein IsiA and other paralogous Chl-binding proteins (CBP) that can form antenna complexes with Photosystem I (PSI) and/or Photosystem II (PSII). Red and cryptophyte algae also produce CBP associated with PSI but which belong to the Chl a/b-binding protein superfamily and which are unrelated to the CBP of cyanobacteria. This review describes recent progress in structure determination for PBS and the Chl proteins of cyanobacteria, red algae, and cryptophytan algae.

Indexed as

CyanobacteriaPhycobiliproteinsRhodophytaCryptophytaLight-Harvesting Protein ComplexesPhycobilisomesLight-Harvesting Protein ComplexesPhycobiliproteinsPhycobilisomes

Identifiers

PMID38652697
PMCPMC11449063
OpenAlexW4395029901

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.