Evidence map›Paper›PMID 22116355›Full record

ReviewCellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology2011

STAS domain structure and function.

Alok K Sharma, Alan C Rigby, Seth L Alper

Open access · bronzeAbstract readReview
In one paragraph

Review in Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

47 citing papers in PubMed, 101 citations in OpenAlex.

  1. Review
  2. Article
  3. Microorganisms · 2025
    Review
  4. Article
  5. Lighting the way: how theJournal of bacteriology · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Chemotaxis Coupling Protein CheWInfection and immunity · 2023
    Article
  10. Effect of NaCl stress on exoproteome profiles ofFrontiers in microbiology · 2023
    Article
  11. Selection of Diagnostically Significant Regions of theInternational journal of molecular sciences · 2022
    Article
  12. Review
  13. Mutation Screening and Functional Study ofJournal of clinical research in pediatric endocrinology · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. STAS Domain Only Proteins in Bacterial Gene Regulation.Frontiers in cellular and infection microbiology · 2021
    Review
  19. 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

3 authors at 2 institutions in 1 country.

Alok K SharmaMolecular and Vascular Medicine Division, Beth Israel Deaconess Medical Center, Department of Medicine, Harvard Medical School, Boston, MA 02215, USA. aksharma@bidmc.harvard.edu
Alan C Rigby
Seth L Alper
Harvard University Press · USBeth Israel Deaconess Medical Center · US

Funding

STRUCTURE-FUNCTION RELATIONSHIPS IN THE ALIMENTARY TRACTP30DK034854 · NIDDK · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI JONATHAN C KAGAN · 1986 to 2026
$32.4M
MOLECULAR PHYSIOLOGY OF BAND 3 LIKE PROTEINS OF KIDNEYR37DK043495 · NIDDK · BETH ISRAEL DEACONESS MEDICAL CENTER · PI ALPER, SETH LEO · 1998 to 2007
$3.0M
MOLECULAR PHYSIOLOGY OF BAND 3-LIKE PROTEINS OF KIDNEYR01DK043495 · NIDDK · BETH ISRAEL DEACONESS MEDICAL CENTER · PI ALPER, SETH LEO · 1991 to 1997
–
NIDDK NIH HHS DK34854NIDDK NIH HHS DK43495NIDDK NIH HHS P30 DK034854NIDDK NIH HHS R37 DK043495
6 · The paper itself

Abstract

Pendrin shares with nearly all SLC26/SulP anion transporters a carboxy-terminal cytoplasmic segment organized around a Sulfate Transporter and Anti-Sigma factor antagonist (STAS) domain. STAS domains of divergent amino acid sequence exhibit a conserved fold of 4 β strands interspersed among 5 α helices. The first STAS domain proteins studied were single-domain anti-sigma factor antagonists (anti-anti-σ). These anti-anti-σ indirectly stimulate bacterial RNA polymerase by inactivating inhibitory anti-σ kinases, liberating σ factors to direct specific transcription of target genes or operons. Some STAS domains are nucleotide-binding phosphoproteins or nucleotidases. Others are interaction/transduction modules within multidomain sensors of light, oxygen and other gasotransmitters, cyclic nucleotides, inositol phosphates, and G proteins. Additional multidomain STAS protein sequences suggest functions in sensing, metabolism, or transport of nutrients such as sugars, amino acids, lipids, anions, vitamins, or hydrocarbons. Still other multidomain STAS polypeptides include histidine and serine/threonine kinase domains and ligand-activated transcription factor domains. SulP/SLC26 STAS domains and adjacent sequences interact with other transporters, cytoskeletal scaffolds, and with enzymes metabolizing transported anion substrates, forming putative metabolons. STAS domains are central to membrane targeting of many SulP/SLC26 anion transporters, and STAS domain mutations are associated with at least three human recessive diseases. This review summarizes STAS domain structure and function.

Indexed as

BacteriaDNA-Directed RNA PolymerasesHumansMembrane Transport ProteinsModels, MolecularProtein Structure, SecondaryProtein Structure, TertiarySulfate TransportersDNA-Directed RNA PolymerasesMembrane Transport ProteinsSLC26A4 protein, humanSulfate Transporters

Identifiers

PMID22116355
PMCPMC3709189
OpenAlexW2010043198

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.