Evidence map›Paper›PMID 17524618›Full record

ReviewCellular signalling2007

Stimulation of phospholipase Cbeta by membrane interactions, interdomain movement, and G protein binding--how many ways can you activate an enzyme?

Guillaume Drin, Suzanne Scarlata

Abstract readReview
In one paragraph

Review in Cellular signalling, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Article
  2. Review
  3. Phospholipase Signaling in Breast Cancer.Advances in experimental medicine and biology · 2021
    Review
  4. Review
  5. Article
  6. Article
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  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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.

Guillaume DrinInstitut de Pharmacologie Moléculaire et Cellulaire, CNRS et Université de Nice-Sophia Antipolis, 06560 Valbonne, France.
Suzanne Scarlata

Funding

ACTIVATION OF PHOSPHOLIPASE C BETA BY G PROTEINSR01GM053132 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI SCARLATA, SUZANNE F · 1995 to 2014
$3.5M
NIGMS NIH HHS GM 053132NIGMS NIH HHS R01 GM053132
6 · The paper itself

Abstract

Signaling proteins are usually composed of one or more conserved structural domains. These domains are usually regulatory in nature by binding to specific activators or effectors, or species that regulate cellular location, etc. Inositol-specific mammalian phospholipase C (PLC) enzymes are multidomain proteins whose activities are controlled by regulators, such as G proteins, as well as membrane interactions. One of these domains has been found to bind membranes, regulators, and activate the catalytic region. The recently solved structure of a major region of PLC-beta2 together with the structure of PLC-delta1 and a wealth of biochemical studies poises the system towards an understanding of the mechanism through which their regulations occurs.

Indexed as

Amino Acid SequenceAnimalsCell MembraneEnzyme ActivationGTP-Binding ProteinsHumansIsoenzymesMolecular Sequence DataPhospholipase C betaPhospholipase C deltaProtein BindingProtein Structure, TertiaryType C PhospholipasesGTP-Binding ProteinsIsoenzymesPhospholipase C betaPhospholipase C deltaPLCB2 protein, humanPLCD1 protein, humanType C Phospholipases

Identifiers

PMID17524618
PMCPMC1963342

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.