Evidence map›Paper›PMID 10518533›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Interactions of G(h)/transglutaminase with phospholipase Cdelta1 and with GTP.

S N Murthy, J W Lomasney, E C Mak, L Lorand

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

29 citing papers in PubMed, 91 citations in OpenAlex.

  1. Review
  2. Negative self-regulation of transient receptor potential canonical 4 by the specific interaction with phospholipase C-δ1.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2023
    Article
  3. The Impact ofInternational journal of molecular sciences · 2023
    Article
  4. Article
  5. Article
  6. Review
  7. Activity-regulating structural changes and autoantibody epitopes in transglutaminase 2 assessed by hydrogen/deuterium exchange.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  8. Review
  9. The Concise Guide to PHARMACOLOGY 2013/14: enzymes.British journal of pharmacology · 2013
    Article
  10. Article
  11. Article
  12. Genetic architecture of susceptibility to PCB126-induced developmental cardiotoxicity in zebrafish.Toxicological sciences : an official journal of the Society of Toxicology · 2011
    Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Identification of two GTP-independent alternatively spliced forms of tissue transglutaminase in human leukocytes, vascular smooth muscle, and endothelial cells.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2007
    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

4 authors at 1 institution in 1 country.

S N MurthyDepartment of Cell and Molecular Biology, Northwestern University Medical School, Chicago, IL 60611-3008, USA.
J W Lomasney
E C Mak
L Lorand
Northwestern University · US

Funding

Molecular Basis for Protein-Phospholipid InteractionR01HL055591 · NHLBI · NORTHWESTERN UNIVERSITY · PI LOMASNEY, JON W · 2002 to 2005
$1.2M
MOLECULAR BASIS FOR PROTEIN/PHOSPHOLIPID INTERACTIONR29HL055591 · NHLBI · NORTHWESTERN UNIVERSITY · PI LOMASNEY, JON W · 1996 to 2000
$49k
CROSSLINKS IN DIABETIC AND SENILE CATARACTSR01EY003942 · NEI · NORTHWESTERN UNIVERSITY · PI LORAND, LASZLO · 1985 to 1998
–
NEI NIH HHS EY-03942NHLBI NIH HHS HL-02212NHLBI NIH HHS HL-55591NHLBI NIH HHS R01 HL055591NHLBI NIH HHS R29 HL055591
6 · The paper itself

Abstract

The inositol phosphate hydrolyzing activity of human phospholipase Cdelta1 (PLCdelta1) is markedly inhibited when the enzyme is coexpressed with the human heart G(h)/transglutaminase (TG) in human embryonic kidney cells. Because the cotransfection does not affect the amount of PLCdelta1 in the cells, the depression of phospholipase activity probably is a result of a direct interaction between the two proteins. An ELISA procedure was employed to document the associations of purified TG preparations from a variety of tissues (human red cells, rabbit lens, guinea pig liver) with PLCdelta1. Nucleotides (GTP > GDP > ATP > GMP = ADP, in order of decreasing efficiency) interfered with the formation of the PLCdelta1:TG complex. A conformational change in the TG partner, occurring with nucleotide binding, is thought to be responsible for dissociating the two proteins. The structural rearrangement produces a remarkable shift in the anodic mobility of TG in electrophoresis: TG(slow) + GTP -->/<-- [TG:GTP](fast). Altogether, our findings indicate that GTP controls PLCdelta1 activity by releasing this protein from an inhibitory association with G(h)/transglutaminase.

Indexed as

AnimalsChickensEnzyme-Linked Immunosorbent AssayErythrocytesGTP-Binding ProteinsGuanosine TriphosphateGuinea PigsHumansIsoenzymesLens, CrystallineLiverMiceModels, BiologicalPeriodic AcidPhospholipase C deltaRabbitsGTP-Binding ProteinsGuanosine TriphosphateIsoenzymesPeriodic AcidPhospholipase C deltaPLCD1 protein, humanPlcd1 protein, mouseTransglutaminasesType C Phospholipases

Identifiers

PMID10518533
PMCPMC18369
OpenAlexW2113177481

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.