Evidence map›Paper›PMID 23610410›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Structures of complexes comprised of Fischerella transcription factor HetR with Anabaena DNA targets.

Youngchang Kim, Zi Ye, Grazyna Joachimiak, Patrick Videau, Jasmine Young, Kathryn Hurd, Sean M Callahan, Piotr Gornicki, Jindong Zhao, Robert Haselkorn and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

  1. Coordination of NProceedings of the National Academy of Sciences of the United States of America · 2026
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  10. Functional Overlap ofJournal of bacteriology · 2018
    Article
  11. 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
  12. 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
  13. Article
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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

11 authors at 5 institutions in 2 countries.

Youngchang KimMidwest Center for Structural Genomics and Structural Biology Center, Biosciences, Argonne National Laboratory, Argonne, IL 60439, USA.
Zi Ye
Grazyna Joachimiak
Patrick Videau
Jasmine Young
Kathryn Hurd
Sean M Callahan
Piotr Gornicki
Jindong Zhao
Robert Haselkorn
Andrzej Joachimiak
University of Hawaii System · USJoint Center for Structural Genomics · USArgonne National Laboratory · USChinese Academy of Sciences · CNInstitute of Hydrobiology · CN

Funding

Midwest Center for Structural GenomicsU54GM094585 · NIGMS · UNIVERSITY OF CHICAGO · PI MINOR, WLADEK · 2010 to 2014
$33.7M
NIGMS NIH HHS GM094585NIGMS NIH HHS U54 GM094585
6 · The paper itself

Abstract

HetR is an essential regulator of heterocyst development in cyanobacteria. Many mutations in HetR render Anabaena incapable of nitrogen fixation. The protein binds to a DNA palindrome upstream of hetP and other genes. We have determined the crystal structures of HetR complexed with palindromic DNA targets, 21, 23, and 29 bp at 2.50-, 3.00-, and 3.25-Å resolution, respectively. The highest-resolution structure shows fine details of specific protein-DNA interactions. The lower-resolution structures with longer DNA duplexes have similar interaction patterns and show how the flap domains interact with DNA in a sequence nonspecific fashion. Fifteen of 15 protein-DNA contacts predicted on the basis of the structure were confirmed by single amino acid mutations that abolished binding in vitro and complementation in vivo. A striking feature of the structure is the association of glutamate 71 from each subunit of the HetR dimer with three successive cytosines in each arm of the palindromic target, a feature that is conserved among all known heterocyst-forming cyanobacteria sequenced to date.

Indexed as

Amino AcidsAnabaenaBacterial ProteinsCrystallography, X-RayCyanobacteriaCytosineDNA, BacterialGenetic Complementation TestGlutamic AcidInverted Repeat SequencesModels, MolecularMolecular ConformationMutagenesisMutationNitrogenProtein BindingAmino AcidsBacterial ProteinsCytosineDNA, BacterialGlutamic AcidHetR protein, BacteriaNitrogenTranscription Factorsheterocyst differentiationmutagenesisX-ray crystallography

Identifiers

PMID23610410
PMCPMC3651475
OpenAlexW1977959149

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.