Evidence map›Paper›PMID 17128963›Full record

ArticleBiochemistry2006

Calmodulin, conformational states, and calcium signaling. A single-molecule perspective.

Carey K Johnson

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.9field-weighted citation impact, top 6% 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

27 citing papers in PubMed, 67 citations in OpenAlex.

  1. Review
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  11. Switchable Nitroproteome States ofFrontiers in microbiology · 2019
    Article
  12. Soluble calcium-binding proteins (SCBPs) of the earthworm Lumbricus terrestris: possible role as relaxation factors in muscle.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Impact of methionine oxidation on calmodulin structural dynamics.Biochemical and biophysical research communications · 2015
    Article
  18. Article
  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

1 author at 1 institution in 1 country.

Carey K JohnsonDepartment of Chemistry, 1251 Wescoe Drive, University of Kansas, Lawrence, Kansas 66045-7582, USA. ckjohnson@ku.edu
University of Kansas · US

Funding

TRAINING GRANT IN DYNAMIC ASPECTS OF CHEMICAL BIOLOGYT32GM008545 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI LAMB, AUDREY L · 1994 to 2019
$4.9M
SINGLE-MOLECULE DYNAMICS OF TARGET BINDING BY CALMODULINR01GM058715 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI JOHNSON, CAREY K · 2000 to 2003
$890k
OAKWOOD COLLEGE MARC HONORS PROGRAMT34GM008259 · NIGMS · OAKWOOD COLLEGE · PI GWEBU, EPHRAIM TOBELA · 1988 to 1998
–
NIGMS NIH HHS R01 GM058715NIGMS NIH HHS R01 GM58715NIGMS NIH HHS T32 GM008545NIGMS NIH HHS T34 GM008259
6 · The paper itself

Abstract

Single-molecule fluorescence measurements can provide a new perspective on the conformations, dynamics, and interactions of proteins. Recent examples are described illustrating the application of single-molecule fluorescence spectroscopy to calcium signaling proteins with an emphasis on the new information available in single-molecule fluorescence burst measurements, resonance energy transfer, and polarization modulation methods. Calcium signaling pathways are crucial in many cellular processes. The calcium binding protein calmodulin (CaM) serves as a molecular switch to regulate a network of calcium signaling pathways. Single-molecule spectroscopic methods can yield insights into conformations and dynamics of CaM and CaM-regulated proteins. Examples include studies of the conformations and dynamics of CaM, binding of target peptides, and interaction with the plasma-membrane Ca2+ pump. Single-molecule resonance energy transfer measurements revealed conformational substates of CaM, and single-molecule polarization modulation spectroscopy was used to probe interactions between CaM and the plasma-membrane Ca2+-ATPase.

Indexed as

Calcium SignalingCalciumCalcium-Transporting ATPasesCalmodulinMolecular ConformationSubstrate SpecificityCalciumCalcium-Transporting ATPasesCalmodulin

Identifiers

PMID17128963
PMCPMC2533622
OpenAlexW2066679361

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.