Evidence map›Paper›PMID 8972186›Full record

ArticleMolecular and cellular biology1997

Suppression of grp78 core promoter element-mediated stress induction by the dbpA and dbpB (YB-1) cold shock domain proteins.

W W Li, Y Hsiung, V Wong, K Galvin, Y Zhou, Y Shi, A S Lee

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.4field-weighted citation impact, top 6% 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

20 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Article
  3. Cold Shock Proteins Mediate GN with Mesangioproliferation.Journal of the American Society of Nephrology : JASN · 2016
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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

7 authors at 1 institution in 1 country.

W W LiDepartment of Biochemistry and Molecular Biology, Norris Cancer Center, University of Southern California School of Medicine, Los Angeles 90033, USA.
Y Hsiung
V Wong
K Galvin
Y Zhou
Y Shi
A S Lee
University of Southern California · US

Funding

STRESS INDUCTION OF THE GLUCOSE REGULATED PROTEINSR01CA027607 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LEE, AMY S · 1985 to 2021
$11.1M
TRANSCRIPTIONAL REPRESSION AND ACTIVATION BY YY1R01GM053874 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI SHI, YANG · 1996 to 2010
$4.6M
COORDINATED GENE EXPRESSION IN MAMMALIAN CELLSR37CA027607 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LEE, AMY S · 1988 to 1995
–
NCI NIH HHS CA27607NIGMS NIH HHS GM53874
6 · The paper itself

Abstract

The highly conserved grp78 core promoter element plays an important role in the induction of grp78 under diverse stress signals. Previous studies have established a functional region in the 3' half of the core (stress-inducible change region [SICR]) which exhibits stress-inducible changes in stressed nuclei. The human transcription factor YY1 is shown to bind the SICR and transactivate the core element under stress conditions. Here we report that expression library screening with the core element has identified two new core binding proteins, YB-1 and dbpA. Both proteins belong to the Y-box family of proteins characterized by an evolutionarily conserved DNA binding motif, the cold shock domain (CSD). In contrast to YY1, which binds only double-stranded SICR, the Y-box/CSD proteins much prefer the lower strand of the SICR. The Y-box proteins can repress the inducibility of the grp78 core element mediated by treatment of cells with A23187, thapsigargin, and tunicamycin. In gel shift assays, YY1 binding to the core element is inhibited by either YB-1 or dbpA. A yeast interaction trap screen using LexA-YY1 as a bait and a HeLa cell cDNA-acid patch fusion library identified YB-1 as a YY1-interacting protein. In cotransfection experiments, the Y-box proteins antagonize the YY1-mediated enhancement of transcription directed by the grp78 core in stressed cells. Thus, the CSD proteins may be part of the stress signal transduction mechanism in the mammalian system.

Indexed as

CCAAT-Enhancer-Binding ProteinsBacterial ProteinsCarrier ProteinsCloning, MolecularCold TemperatureDNA-Binding ProteinsDNA, Single-StrandedEndoplasmic Reticulum Chaperone BiPErythroid-Specific DNA-Binding FactorsHeat-Shock ProteinsHeLa CellsHumansLexA Repressor ProteinMolecular ChaperonesMolecular Sequence DataNFI Transcription FactorsBacterial ProteinsCarrier ProteinsCCAAT-Enhancer-Binding ProteinsDNA-Binding ProteinsDNA, Single-StrandedEndoplasmic Reticulum Chaperone BiPErythroid-Specific DNA-Binding FactorsHeat-Shock ProteinsHSPA5 protein, humanLexA Repressor ProteinMolecular ChaperonesNFI Transcription FactorsNuclear ProteinsRecombinant Fusion ProteinsSerine EndopeptidasesTranscription FactorsY-Box-Binding Protein 1YBX1 protein, humanYBX3 protein, humanYY1 protein, humanYY1 Transcription Factor

Identifiers

PMID8972186
PMCPMC231730
OpenAlexW2128196906

What OpenQuestion holds

Textmetadata
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Registered trials

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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.