Evidence map›Paper›PMID 24235144›Full record

ArticleThe Journal of biological chemistry2013

Ca2+-independent binding of anionic phospholipids by phospholipase C δ1 EF-hand domain.

Jingfei Cai, Su Guo, Jon W Lomasney, Mary F Roberts

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

8 citing papers in PubMed, 16 citations in OpenAlex.

  1. Rice phospholipase C4 enhances CaPlant communications · 2026
    Article
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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

4 authors at 2 institutions in 1 country.

Jingfei CaiFrom the Department of Chemistry, Boston College, Chestnut Hill, Massachusetts 02467 and.
Su Guo
Jon W Lomasney
Mary F Roberts
Boston College · USNorthwestern University · US

Funding

ACTIVATION OF PI-SPECIFIC PHOSPHOLIPASE C ENZYMESR01GM060418 · NIGMS · BOSTON COLLEGE · PI ROBERTS, MARY FEDARKO · 2000 to 2013
$3.1M
NIGMS NIH HHS R01 GM060418NIGMS NIH HHS R01 GM60418
6 · The paper itself

Abstract

Recombinant EF-hand domain of phospholipase C δ1 has a moderate affinity for anionic phospholipids in the absence of Ca(2+) that is driven by interactions of cationic and hydrophobic residues in the first EF-hand sequence. This region of PLC δ1 is missing in the crystal structure. The relative orientation of recombinant EF with respect to the bilayer, established with NMR methods, shows that the N-terminal helix of EF-1 is close to the membrane interface. Specific mutations of EF-1 residues in full-length PLC δ1 reduce enzyme activity but not because of disturbing partitioning of the protein onto vesicles. The reduction in enzymatic activity coupled with vesicle binding studies are consistent with a role for this domain in aiding substrate binding in the active site once the protein is transiently anchored at its target membrane.

Indexed as

AnimalsCalciumCatalytic DomainLipid BilayersMutationNuclear Magnetic Resonance, BiomolecularPhospholipase C deltaPhospholipidsProtein BindingProtein Structure, SecondaryRatsRecombinant ProteinsCalciumLipid BilayersPhospholipase C deltaPhospholipidsPlcd1 protein, ratRecombinant ProteinsEnzymesGlycerophospholipidMembrane EnzymesNMRPhospholipase CPhospholipid VesicleSite-directed Mutagenesis

Identifiers

PMID24235144
PMCPMC3873580
OpenAlexW2029857787

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.