Evidence map›Paper›PMID 8970164›Full record

ArticleMolecular biology of the cell1996

Structure of pp32, an acidic nuclear protein which inhibits oncogene-induced formation of transformed foci.

T H Chen, J R Brody, F E Romantsev, J G Yu, A E Kayler, E Voneiff, F P Kuhajda, G R Pasternack

Abstract read
In one paragraph

Article in Molecular biology of the cell, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 82 citations in OpenAlex.

  1. International journal of molecular sciences · 2022
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  6. Cracking the ANP32 whips: important functions, unequal requirement, and hints at disease implications.BioEssays : news and reviews in molecular, cellular and developmental biology · 2014
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  12. PHAPI/pp32 suppresses tumorigenesis by stimulating apoptosis.The Journal of biological chemistry · 2009
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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.

T H ChenDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
J R Brody
F E Romantsev
J G Yu
A E Kayler
E Voneiff
F P Kuhajda
G R Pasternack
Johns Hopkins University · US

Funding

CELLULAR &MOLECULAR MECH OF INFLAMMATORY REACTIONST32AI007247 · NIAID · JOHNS HOPKINS UNIVERSITY · PI Joel L Pomerantz · 1985 to 2026
$10.2M
NOVEL NUCLEAR PROTEINS IN NORMAL AND CANCER CELLSR01CA054404 · NCI · JOHNS HOPKINS UNIVERSITY · PI PASTERNACK, GARY R. · 1992 to 1999
–
NCI NIH HHS R01 CA 54404NIAID NIH HHS T32 AI 07247
6 · The paper itself

Abstract

pp32 is a nuclear protein found highly expressed in normal tissues in those cells capable of self-renewal and in neoplastic cells. We report the cloning of cDNAs encoding human and murine pp32. The clones encode a 28.6-kDa protein; approximately two-thirds of the N-terminal predicts an amphipathic alpha helix containing two possible nuclear localization signals and a potential leucine zipper motif. The C-terminal third is exceptionally acidic, comprised of approximately 70% aspartic and glutamic acid residues; the predicted pI of human pp32 is 3.81. Human and murine pp32 cDNAs are 88% identical; the predicted proteins are 89% identical and 95% similar. Although the structure of pp32 is suggestive of a transcription factor, pp32 did not significantly modulate transcription of a reporter construct when fused to the Gal4 DNA-binding domain. In contrast, in cotransfection experiments, pp32 inhibited the ability of a broad assortment of oncogene pairs to transform rat embryo fibroblasts, including ras + myc, ras + jun, ras + E1a, ras + mutant p53, and E6 + E7. In related experiments, pp32 inhibited the ability of Rat 1a-myc cells to grow in soft agar, whereas it failed to affect ras-induced focus formation in NIH3T3 cells. These results suggest that pp32 may play a key role in self-renewing cell populations where it may act in the nucleus to limit their sensitivity to transformation.

Indexed as

Gene Expression RegulationGenes, mycGenes, ras3T3 CellsAmino Acid SequenceAnimalsBase SequenceCell LineDNA, ComplementaryGene ExpressionHumansMiceMolecular Sequence DataNuclear ProteinsOncogenesPhosphoproteinsDNA, ComplementaryNuclear ProteinsPhosphoproteinsRNA, Messenger

Identifiers

PMID8970164
PMCPMC276049
OpenAlexW2168145310

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.