Evidence map›Paper›PMID 19546223›Full record

ArticleThe Journal of biological chemistry2009

Ca2+-dependent conformational changes in a C-terminal cytosolic domain of polycystin-2.

Frank Schumann, Helen Hoffmeister, Reto Bader, Maren Schmidt, Ralph Witzgall, Hans Robert Kalbitzer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. X-ray crystallography of TRP channels.Channels (Austin, Tex.) · 2018
    Review
  6. Function and regulation of TRPP2 ion channel revealed by a gain-of-function mutant.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  7. Article
  8. Review
  9. A high-resolution structure of the EF-hand domain of human polycystin-2.Protein science : a publication of the Protein Society · 2014
    Article
  10. Structural biology of TRP channels.Handbook of experimental pharmacology · 2014
    Review
  11. Article
  12. Ion channels in renal disease.Chemical reviews · 2012
    Review
  13. Article
  14. Article
  15. Article
  16. Structural biology of TRP channels.Advances in experimental medicine and biology · 2011
    Article
  17. Polycystin-1, 2, and STIM1 interact with IP(3)R to modulate ER Ca release through the PI3K/Akt pathway.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2011
    Article
  18. Article
  19. 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

6 authors at 2 institutions in 2 countries.

Frank SchumannInstitute of Biophysics and Physical Biochemistry, University of Regensburg, Regensburg, Germany.
Helen Hoffmeister
Reto Bader
Maren Schmidt
Ralph Witzgall
Hans Robert Kalbitzer
Czech Academy of Sciences, Institute of Biophysics · CZUniversity of Regensburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The PKD1 and PKD2 genes are the genes that are mutated in patients suffering from autosomal dominant polycystic kidney disease. The human PKD2 gene codes for a 968-amino acid long membrane protein called polycystin-2 that represents a cation channel whose activity can be regulated by Ca(2+) ions. By CD, fluorescence, and NMR spectroscopy, we have studied a 117-amino acid-long fragment of the cytoplasmic domain of polycystin-2, polycystin-2-(680-796) that was proposed to contain a Ca(2+)-binding site. NMR structure determination reveals the existence of two Ca(2+)-binding sites in polycystin-2-(680-796) arranged in a typical and an atypical EF-hand motif. In the absence of Ca(2+) the protein forms a dimer that is dissociated by Ca(2+) binding. This dissociation may be related to the Ca(2+) inactivation observed earlier. The calcium affinity of the protein was determined by fluorescence and NMR spectroscopy. At 293 K, the K(D) values for the high and low affinity sites are 55 mum and 179 mum, respectively.

Indexed as

Protein MultimerizationAmino Acid MotifsBinding SitesCalciumCircular DichroismHumansMutationNuclear Magnetic Resonance, BiomolecularPolycystic Kidney, Autosomal DominantProtein BindingProtein Structure, TertiarySpectrometry, FluorescenceTRPP Cation ChannelsCalciumTRPP Cation Channels

Identifiers

PMID19546223
PMCPMC2782030
OpenAlexW2168457399

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.