Evidence map›Paper›PMID 7892222›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

Analysis of the human guanylin gene and the processing and cellular localization of the peptide.

O Hill, M Kuhn, H D Zucht, Y Cetin, H Kulaksiz, K Adermann, G Klock, G Rechkemmer, W G Forssmann, H J Mägert

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. 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
2.2field-weighted citation impact, top 12% 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, 57 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Pendrin, a novel transcriptional target of the uroguanylin system.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2013
    Review
  9. Phosphate sensing.Current opinion in nephrology and hypertension · 2009
    Review
  10. Mechanisms of actions of guanylin peptides in the kidney.Pflugers Archiv : European journal of physiology · 2005
    Review
  11. HCC-2, a human chemokine: gene structure, expression pattern, and biological activity.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  12. Article
  13. Bronchiolar nonciliated secretory (Clara) cells: source of guanylin in the mammalian lung.Proceedings of the National Academy of Sciences of the United States of America · 1995
    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 4 institutions in 2 countries.

O HillLower Saxony Institute for Peptide Research, Hannover, Germany.
M Kuhn
H D Zucht
Y Cetin
H Kulaksiz
K Adermann
G Klock
G Rechkemmer
W G Forssmann
H J Mägert
Research Institute for Philosophy Hannover · DETechnical University of Darmstadt · DEHarvard University · USMedizinische Hochschule Hannover · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The complete cell biological analysis of human guanylin, a recently discovered regulatory peptide, is offered in this investigation: (i) the nucleotide sequence of the gene, (ii) the isolation and characterization of its circulating molecular form, and (iii) its localization in enterochromaffin cells of the gut. As determined by molecular cloning, DNA sequencing, and comparison with the known cDNA sequence, the approximately 2.6-kbp large gene consists of three exons interrupted by two introns. The putative promoter region contains a TTTAAAA sequence motif and several potential binding sites for transcription factors such as AP-1, AP-2, Sp 1, and glucocorticoid receptors. The isolated hormonal form of guanylin is a 94-amino acid peptide with a molecular mass of 10.3 kDa. Western blot analysis of RP-HPLC fractions from blood plasma confirms this molecular form. Thus, guanylin is synthesized by gut enterochromaffin cells as a prohormone of 115 amino acids and is processed to the molecular form of 94 amino acids circulating in the blood.

Indexed as

Gastrointestinal HormonesPeptide BiosynthesisPromoter Regions, GeneticProtein Processing, Post-TranslationalAmino Acid SequenceAnimalsBase SequenceBinding SitesBumetanideChromatography, High Pressure LiquidColonDNA-Binding ProteinsDNA, ComplementaryDNA PrimersHumansIntestinal MucosaBumetanideDNA-Binding ProteinsDNA, ComplementaryDNA PrimersGastrointestinal HormonesguanylinNatriuretic PeptidesPeptidesReceptors, GlucocorticoidRecombinant ProteinsSp1 Transcription FactorTranscription Factor AP-1Transcription Factor AP-2Transcription Factors

Identifiers

PMID7892222
PMCPMC42420
OpenAlexW2069038615

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.