Evidence map›Paper›PMID 9927690›Full record

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

Identification of a cell protein (FIP-3) as a modulator of NF-kappaB activity and as a target of an adenovirus inhibitor of tumor necrosis factor alpha-induced apoptosis.

Y Li, J Kang, J Friedman, L Tarassishin, J Ye, A Kovalenko, D Wallach, M S Horwitz

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 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
9.8field-weighted citation impact, top 1% 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

57 citing papers in PubMed, 181 citations in OpenAlex.

  1. Review
  2. Article
  3. Role of IκB kinase β in regulating the remodeling of the CARMA1-Bcl10-MALT1 complex.Biochemical and biophysical research communications · 2018
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Adenovirus E3 protein modulates leukocyte functions.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. The zinc finger domain of IKKγ (NEMO) protein in health and disease.Journal of cellular and molecular medicine · 2010
    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

8 authors at 1 institution in 1 country.

Y LiDepartment of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
J Kang
J Friedman
L Tarassishin
J Ye
A Kovalenko
D Wallach
M S Horwitz
Albert Einstein College of Medicine · US

Funding

WORD PROCESSORP30CA013330 · NCI · YESHIVA UNIVERSITY · PI THOMAS E ROHAN · 1985 to 2026
$111.2M
MOLECULAR PATHOGENESIS OF INFECTIOUS DISEASEST32AI007506 · NIAID · YESHIVA UNIVERSITY · PI CASADEVALL, ARTURO · 1997 to 2012
$3.7M
INTERACTION OF PROTEINS WITH AD INHIBITOR OF TNF-ALPHAR01CA072963 · NCI · YESHIVA UNIVERSITY · PI HORWITZ, MARSHALL S · 1997 to 2001
$617k
VIRAL ONCOLOGY AND TUMOR BIOLOGYT32CA009060 · NCI · YESHIVA UNIVERSITY · PI LENZ, JACK R. · 1985 to 2001
$569k
NCI NIH HHS 5T32CA 09060NCI NIH HHS CA13330NCI NIH HHS P30 CA013330NCI NIH HHS R01 CA72963NCI NIH HHS T32 CA009060NIAID NIH HHS T32 AI007506
6 · The paper itself

Abstract

FIP-3 (14.7K interacting protein) was discovered during a search for cell proteins that could interact with an adenovirus protein (Ad E3-14.7K) that had been shown to prevent tumor necrosis factor (TNF)-alpha-induced cytolysis. FIP-3, which contains leucine zippers and a zinc finger domain, inhibits both basal and induced transcriptional activity of NF-kappaB and causes a late-appearing apoptosis with unique morphologic manifestations. Ad E3-14.7K can partially reverse apoptotic death induced by FIP-3. FIP-3 also was shown to bind to other cell proteins, RIP and NIK, which previously had been described as essential components of TNF-alpha-induced NF-kappaB activation. In addition, FIP-3 inhibited activation of NF-kappaB induced by TNF-alpha, the TNFR-1 receptor, RIP, NIK, and IKKbeta, as well as basal levels of endogenous NF-kappaB in 293 cells. Because the activation of NF-kappaB has been shown to inhibit apoptosis, FIP-3 appears both to activate a cell-death pathway and to inhibit an NF-kappaB-dependent survival mechanism.

Indexed as

AdenoviridaeAdenovirus E3 ProteinsAmino Acid SequenceApoptosisCarrier ProteinsCell LineCell SurvivalGlutathione TransferaseHumansI-kappa B KinaseLeucine ZippersMolecular Sequence DataMolecular WeightNF-kappa BNF-kappaB-Inducing KinaseProtein KinasesAdenovirus E3 ProteinsCarrier ProteinsCHUK protein, humanGlutathione TransferaseI-kappa B KinaseIKBKB protein, humanIKBKE protein, humanNF-kappa BNF-kappaB-Inducing KinaseProtein KinasesProteinsProtein Serine-Threonine KinasesReceptor-Interacting Protein Serine-Threonine KinasesRecombinant Fusion ProteinsRecombinant ProteinsRIPK1 protein, humanTumor Necrosis Factor-alpha

Identifiers

PMID9927690
PMCPMC15347
OpenAlexW2033098442

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.