Evidence map›Paper›PMID 21628585›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Structure of transcription factor HetR required for heterocyst differentiation in cyanobacteria.

Youngchang Kim, Grazyna Joachimiak, Zi Ye, T Andrew Binkowski, Rongguang Zhang, Piotr Gornicki, Sean M Callahan, Wolfgang R Hess, Robert Haselkorn, Andrzej Joachimiak

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. 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
2.4field-weighted citation impact, top 11% 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, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. The Pkn22 Kinase ofFrontiers in microbiology · 2019
    Article
  9. Functional Overlap ofJournal of bacteriology · 2018
    Article
  10. An amidase is required for proper intercellular communication in the filamentous cyanobacteriumProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Formation and maintenance of nitrogen-fixing cell patterns in filamentous cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  12. Article
  13. Shape matters: lifecycle of cooperative patches promotes cooperation in bulky populations.Evolution; international journal of organic evolution · 2015
    Article
  14. Article
  15. Article
  16. Article
  17. Structures of complexes comprised of Fischerella transcription factor HetR with Anabaena DNA targets.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  18. Article
  19. Restricted cellular differentiation in cyanobacterial filaments.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  20. 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

10 authors at 5 institutions in 3 countries.

Youngchang KimMidwest Center for Structural Genomics and Structural Biology Center, Biosciences, Argonne National Laboratory, 9700 South Cass Avenue, Building 202, Argonne, IL 60439, USA.
Grazyna Joachimiak
Zi Ye
T Andrew Binkowski
Rongguang Zhang
Piotr Gornicki
Sean M Callahan
Wolfgang R Hess
Robert Haselkorn
Andrzej Joachimiak
Joint Center for Structural Genomics · USUniversity of Chicago · USArgonne National Laboratory · USUniversity of Freiburg · DEUniversity of Hawaii System · US

Funding

Midwest Center for Structural GenomicsU54GM094585 · NIGMS · UNIVERSITY OF CHICAGO · PI MINOR, WLADEK · 2010 to 2014
$33.7M
NIGMS NIH HHS GM09485NIGMS NIH HHS U54 GM094585
6 · The paper itself

Abstract

HetR is an essential regulator of heterocyst development in cyanobacteria. HetR binds to a DNA palindrome upstream of the hetP gene. We report the crystal structure of HetR from Fischerella at 3.0 Å. The protein is a dimer comprised of a central DNA-binding unit containing the N-terminal regions of the two subunits organized with two helix-turn-helix motifs; two globular flaps extending in opposite directions; and a hood over the central core formed from the C-terminal subdomains. The flaps and hood have no structural precedent in the protein database, therefore representing new folds. The structural assignments are supported by site-directed mutagenesis and DNA-binding studies. We suggest that HetR serves as a scaffold for assembly of transcription components critical for heterocyst development.

Indexed as

Protein Structure, QuaternaryProtein Structure, TertiaryBacterial ProteinsCrystallography, X-RayCyanobacteriaDNA, BacterialGene Expression Regulation, BacterialModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein BindingTranscription FactorsBacterial ProteinsDNA, BacterialHetR protein, BacteriaTranscription Factors

Identifiers

PMID21628585
PMCPMC3121805
OpenAlexW2004455624

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.