Evidence map›Paper›PMID 11867433›Full record

ArticleBiophysical journal2002

Molecular mechanisms of calcium and magnesium binding to parvalbumin.

M Susan Cates, Miguel L Teodoro, George N Phillips

Abstract read
In one paragraph

Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
–field-weighted citation impact
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

31 citing papers in PubMed.

  1. Article
  2. CaProtein science : a publication of the Protein Society · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Social Experience during Adolescence Shapes Maturation of Parvalbumin-Positive Interneurons in the Left Orbitofrontal Cortex.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
    Article
  8. Article
  9. Deciphering albumin-directed drug delivery by imaging.Advanced drug delivery reviews · 2022
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Many-body effect determines the selectivity for CaProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Article
  17. Article
  18. Article
  19. The Involvement of MgOxidative medicine and cellular longevity · 2017
    Review
  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.

M Susan CatesDepartment of Biochemistry and Cell Biology, Rice University, Houston, Texas 77005, USA.
Miguel L Teodoro
George N Phillips

Funding

TRAINING PROGRAM IN COMPUTATIONAL BIOLOGY AND MEDICINET15LM007093 · NLM · RICE UNIVERSITY · PI Lydia E. Kavraki · 1992 to 2026
$20.8M
NLM NIH HHS LM07093NLM NIH HHS T15 LM007093
6 · The paper itself

Abstract

Molecular dynamics simulations have been used to investigate the relationship between the coordinating residues of the EF-hand calcium binding loop of parvalbumin and the overall plasticity and flexibility of the protein. The first simulation modeled the transition from Ca(2+) to Mg(2+) coordination by varying the van der Waals parameters for the bound metal ions. The glutamate at position 12 could be accurately and reversibly seen to be a source of selective bidentate ligation of Ca(2+) in the simulations. A second simulation correlated well with the experimental observation that an E101D substitution at EF loop position 12 results in a dramatically less tightly bound monodentate Ca(2+) coordination by aspartate. A final set of simulations investigated Ca(2+) binding in the E101D mutant loop in the presence of applied external forces designed to impose bidentate coordination. The results of these simulations illustrate that the aspartate is capable of attaining a suitable orientation for bidentate coordination, thus implying that it is the inherent rigidity of the loop that prevents bidentate coordination in the parvalbumin E101D mutant.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCalciumComputer SimulationEsocidaeGlutamic AcidIonsMagnesiumModels, MolecularMolecular Sequence DataMutationNitrogenParvalbuminsProtein BindingProtein Structure, TertiaryCalciumGlutamic AcidIonsMagnesiumNitrogenParvalbuminsSerine

Identifiers

PMID11867433
PMCPMC1301919

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.