Evidence map›Paper›PMID 10597267›Full record

ArticleOncogene1999

Mmip-2, a novel RING finger protein that interacts with mad members of the Myc oncoprotein network.

X Y Yin, K Gupta, W P Han, E S Levitan, E V Prochownik

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

11 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. The Max network gone mad.Molecular and cellular biology · 2001
    Review
  11. 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

5 authors at 3 institutions in 1 country.

X Y YinSection of Hematology/Oncology, Children's Hospital of Pittsburgh, University of Pittsburgh Cancer Institute, PA 15213, USA.
K Gupta
W P Han
E S Levitan
E V Prochownik
Children's Hospital of Pittsburgh · USUPMC Hillman Cancer Center · USUniversity of Pittsburgh Medical Center · US

Funding

Dense-Core Vesicle Circulation, Capture and Synaptic Neuropeptide ReleaseR01NS032385 · NINDS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI EDWIN S LEVITAN · 1995 to 2026
$13.0M
MOLECULAR BIOLOGY OF HEMATOPOIETIC DIFFERENTIATIONR01HL033741 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PROCHOWNIK, EDWARD V · 1985 to 2000
$341k
NHLBI NIH HHS HL33741NINDS NIH HHS NS32385
6 · The paper itself

Abstract

Mad proteins are basic-helix-loop-helix-leucine zipper (bHLH-ZIP)-containing members of the myc oncoprotein network. They interact with the bHLH-ZIP protein max, compete for the same DNA binding sites as myc-max heterodimers and down-regulate myc-responsive genes. Using the bHLH-ZIP domain of mad1 as a yeast two-hybrid 'bait', we identified Mmip-2, a novel RING finger protein that interacts with all mad members, but weakly or not at all with c-myc, max or unrelated bHLH or bZIP proteins. The mad1-Mmip-2 interaction is mediated by the ZIP domain in the former protein and by at least two regions in the latter which do not include the RING finger. Mmip-2 can disrupt max-mad DNA binding and can reverse the suppressive effects of mad proteins on c-myc-responsive target genes and on c-myc + ras-mediated focus formation in fibroblasts. Tagging with spectral variants of green fluorescent protein showed that Mmip-2 and mad proteins reside in separate cytoplasmic and nuclear compartments, respectively. When co-expressed, however, the proteins interact and translocate to the cellular compartment occupied by the more abundant protein. These observations suggest a novel way by which Mmip-2 can modulate the transcriptional activity of myc oncoproteins.

Indexed as

Carrier ProteinsRepressor Proteins3T3 CellsAmino Acid SequenceAnimalsBase SequenceCell Cycle ProteinsCloning, MolecularDNA, ComplementaryFungal ProteinsMiceMolecular Sequence DataNuclear ProteinsPhosphoproteinsPrecipitin TestsProtein BindingCarrier ProteinsCell Cycle ProteinsDNA, ComplementaryFungal ProteinsMAD1L1 protein, humanMad1l1 protein, mouseMAD1 protein, S cerevisiaeNuclear ProteinsPhosphoproteinsProto-Oncogene Proteins c-mycRepressor ProteinsRnf17 protein, mouseSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID10597267
OpenAlexW2332675818

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.