Evidence map›Paper›PMID 10611312›Full record

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

Interaction of the Ras-related protein associated with diabetes rad and the putative tumor metastasis suppressor NM23 provides a novel mechanism of GTPase regulation.

J Zhu, Y H Tseng, J D Kantor, C J Rhodes, B R Zetter, J S Moyers, C R Kahn

Open access · bronzeAbstract 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 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

52 citing papers in PubMed, 116 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Modulation of small GTPase activity by NME proteins.Laboratory investigation; a journal of technical methods and pathology · 2018
    Review
  8. The NDPK/NME superfamily: state of the art.Laboratory investigation; a journal of technical methods and pathology · 2018
    Article
  9. Oncogenic Epstein-Barr virus recruits Nm23-H1 to regulate chromatin modifiers.Laboratory investigation; a journal of technical methods and pathology · 2018
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Regulation of the metastasis suppressor Nm23-H1 by tumor viruses.Naunyn-Schmiedeberg's archives of pharmacology · 2015
    Review
  15. Janus-faces of NME-oncoprotein interactions.Naunyn-Schmiedeberg's archives of pharmacology · 2015
    Review
  16. Article
  17. Article
  18. Review
  19. Review
  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

7 authors at 2 institutions in 1 country.

J ZhuResearch Division, Joslin Diabetes Center, Department of Medicine, Harvard Medical School, One Joslin Place, Boston, MA 02215, USA.
Y H Tseng
J D Kantor
C J Rhodes
B R Zetter
J S Moyers
C R Kahn
Harvard University · USJoslin Diabetes Center · US

Funding

SPECIAL ASSAY COREP30DK036836 · NIDDK · JOSLIN DIABETES CENTER · PI ROHIT N. KULKARNI · 1986 to 2026
$50.5M
TRAINING IN DIABETES AND METABOLISMT32DK007260 · NIDDK · JOSLIN DIABETES CENTER · PI LAURIE J GOODYEAR · 1986 to 2026
$13.6M
GENE EXPRESSION IN DIABETES BY SUBTRACTIVE CLONINGR01DK045935 · NIDDK · JOSLIN DIABETES CENTER · PI KAHN, C RONALD · 1993 to 2003
$2.8M
Modulators of Prostate Cancer MetastasisR01CA037393 · NCI · CHILDREN'S HOSPITAL BOSTON · PI ZETTER, BRUCE R · 1985 to 2015
$2.6M
METABOLIC CONTROL OF INSULIN EXOCYTOSISR01DK047919 · NIDDK · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI RHODES, CHRISTOPHER J · 1994 to 2005
$1.7M
CHARACTERIZING RAD, A DIABETES RELATED RAS LIKE PROTEINF32DK009193 · NIDDK · JOSLIN DIABETES CENTER · PI ZHU, JIANHUA · 1994 to 1997
–
NCI NIH HHS R01 CA037393NCI NIH HHS R01 CA 37393NIDDK NIH HHS DK 45935NIDDK NIH HHS F32 DK009193NIDDK NIH HHS P30 DK036836NIDDK NIH HHS R01 DK045935NIDDK NIH HHS R01 DK047919NIDDK NIH HHS R01 DK 47919NIDDK NIH HHS T32 DK007260
6 · The paper itself

Abstract

Rad is the prototypic member of a new class of Ras-related GTPases. Purification of the GTPase-activating protein (GAP) for Rad revealed nm23, a putative tumor metastasis suppressor and a development gene in Drosophila. Antibodies against nm23 depleted Rad-GAP activity from human skeletal muscle cytosol, and bacterially expressed nm23 reconstituted the activity. The GAP activity of nm23 was specific for Rad, was absent with the S105N putative dominant negative mutant of Rad, and was reduced with mutations of nm23. In the presence of ATP, GDP.Rad was also reconverted to GTP.Rad by the nucleoside diphosphate (NDP) kinase activity of nm23. Simultaneously, Rad regulated nm23 by enhancing its NDP kinase activity and decreasing its autophosphorylation. Melanoma cells transfected with wild-type Rad, but not the S105N-Rad, showed enhanced DNA synthesis in response to serum; this effect was lost with coexpression of nm23. Thus, the interaction of nm23 and Rad provides a potential novel mechanism for bidirectional, bimolecular regulation in which nm23 stimulates both GTP hydrolysis and GTP loading of Rad whereas Rad regulates activity of nm23. This interaction may play important roles in the effects of Rad on glucose metabolism and the effects of nm23 on tumor metastasis and developmental regulation.

Indexed as

AnimalsDiabetes MellitusDNAEnzyme ActivationGenes, Tumor SuppressorGlucoseGTP PhosphohydrolasesGuanosine TriphosphateHumansImmediate-Early ProteinsModels, BiologicalMonomeric GTP-Binding ProteinsNeoplasm MetastasisNM23 Nucleoside Diphosphate KinasesNucleoside-Diphosphate KinaseProtein BindingDNAGEM protein, humanGlucoseGTP PhosphohydrolasesGuanosine TriphosphateImmediate-Early ProteinsMonomeric GTP-Binding ProteinsNM23 Nucleoside Diphosphate KinasesNME1 protein, humanNme1 protein, mouseNucleoside-Diphosphate Kinaseras ProteinsRRAD protein, humanRrad protein, mouseRrad protein, ratTranscription Factors

Identifiers

PMID10611312
PMCPMC24747
OpenAlexW2118036359

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.