Evidence map›Paper›PMID 22001612›Full record

ReviewBiochimica et biophysica acta2012

Measuring the kinetics of calcium binding proteins with flash photolysis.

Guido C Faas, Istvan Mody

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

11 citing papers in PubMed, 30 citations in OpenAlex.

  1. Differential regulation of calcium-activated plant kinases in Arabidopsis thaliana.The Plant journal : for cell and molecular biology · 2025
    Article
  2. Nano-organization of synaptic calcium signaling.Biochemical Society transactions · 2024
    Review
  3. Review
  4. Regulation of renal calbindin expression during cisplatin-induced kidney injury.Journal of biochemical and molecular toxicology · 2022
    Article
  5. A multiscale sliding filament model of lymphatic muscle pumping.Biomechanics and modeling in mechanobiology · 2021
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Visualizing CaMKII and CaM activity: a paradigm of compartmentalized signaling.Journal of molecular medicine (Berlin, Germany) · 2013
    Review
  11. 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

2 authors at 1 institution in 1 country.

Guido C FaasDepartment of Neurology, UCLA David Geffen School of Medicine, NRB 1, Room 575E, 635 Charles Young Drive South, Los Angeles, CA 90095-7335, USA. gfaas@ucla.edu
Istvan Mody
University of California, Los Angeles · US

Funding

Neuronal Calcium Homeostasis and Synaptic FunctionR01NS027528 · NINDS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI MODY, ISTVAN · 1990 to 2006
$1.9M
Extracellular Zinc Buffering and A-beta OligomerizationR21AG037151 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI FAAS, GUIDO · 2011 to 2012
$347k
NIA NIH HHS 1R21AG037151-01A1NIA NIH HHS R21 AG037151NINDS NIH HHS NS027528
6 · The paper itself

Abstract

backgroundCalcium-binding proteins (CBPs) are instrumental in the control of Ca2+ signaling. They are the fastest players within the Ca2+ toolkit responding within microseconds to [Ca2+] changes. The CBPs compete for Ca2+ which plays a direct role in modulating Ca2+ transients and the resulting biochemical message. The kinetic properties of the CBPs have to be known to have a good understanding of Ca2+ signaling. SCOPE OF REVIEW: Most techniques used to measure binding kinetics are too slow to accurately determine the fast kinetics of most CBP. Furthermore, many CBPs bind Ca2+ in a cooperative way, which should be incorporated in the kinetic modeling. Here we will review a new ultra-fast in vitro technique for measuring Ca2+ binding properties of CBPs following flash photolysis of caged Ca2+. Compartmental modeling is used to resolve the kinetics of fast cooperative Ca2+ binding to CBPs. MAJOR

conclusionsCurrently this technique has only been used to quantify the kinetics of three CBPs (calbindin, calretinin and calmodulin), but has already provided remarkable insights into the specific role that these kinetics in Ca2+ signaling. GENERAL SIGNIFICANCE: The potential to gain novel insights into Ca2+ signaling by quantifying kinetics of other CBPs using this technique is very promising. This article is part of a Special Issue entitled Biochemical, biophysical and genetic approaches to intracellular calcium signaling.

Indexed as

Calcium SignalingAcetatesAlgorithmsAnimalsCalcium-Binding ProteinsChelating AgentsEthylenediaminesHumansKineticsModels, BiologicalPhotolysisProtein BindingSpectrometry, FluorescenceAcetatesCalcium-Binding ProteinsChelating AgentsDM-nitrophenEthylenediamines

Identifiers

PMID22001612
PMCPMC3294183
OpenAlexW2080728275

What OpenQuestion holds

Textmetadata
LicenceTDM
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.