Evidence map›Paper›PMID 11408486›Full record

ArticleThe Journal of biological chemistry2001

Gln3p nuclear localization and interaction with Ure2p in Saccharomyces cerevisiae.

A A Kulkarni, A T Abul-Hamd, R Rai, H El Berry, T G Cooper

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

45 citing papers in PubMed, 81 citations in OpenAlex.

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  8. Role of Proline in Pathogen and Host Interactions.Antioxidants & redox signaling · 2019
    Review
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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

5 authors at 1 institution in 1 country.

A A KulkarniDepartment of Molecular Sciences, University of Tennessee, Memphis, Tennessee 38163, USA.
A T Abul-Hamd
R Rai
H El Berry
T G Cooper
University of Tennessee Health Science Center · US

Funding

SYNTHESIS AND ASSEMBLY OF EUKARYOTIC MEMBRANESR01GM035642 · NIGMS · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI COOPER, TERRANCE G. · 1985 to 2015
$4.3M
NIGMS NIH HHS GM-35642NIGMS NIH HHS R01 GM035642
6 · The paper itself

Abstract

Gln3p is one of two well characterized GATA family transcriptional activation factors whose function is regulated by the nitrogen supply of the cell. When nitrogen is limiting, Gln3p and Gat1p are concentrated in the nucleus where they bind GATA sequences upstream of nitrogen catabolite repression (NCR)-sensitive genes and activate their transcription. Conversely, in excess nitrogen, these GATA sequences are unoccupied by Gln3p and Gat1p because these transcription activators are excluded from the nucleus. Ure2p binds to Gln3p and Gat1p and is required for NCR-sensitive transcription to be repressed and for nuclear exclusion of these transcription factors. Here we show the following. (i) Gln3p residues 344-365 are required for nuclear localization. (ii) Replacing Ser-344, Ser-347, and Ser-355 with alanines has minimal effects on GFP-Gln3p localization. However, replacing Gln3p Ser-344, Ser-347, and Ser-355 with aspartates results in significant loss of its ability to be concentrated in the nucleus. (iii) N and C termini of the Gln3p region required for it to complex with Ure2p and be excluded from the nucleus are between residues 1-103 and 301-365, respectively. (iv) N and C termini of the Ure2p region required for it to interact with Gln3p are situated between residues 101-151 and 330-346, respectively. (v) Loss of Ure2p residues participating in either dimer or prion formation diminishes its ability to carry out NCR-sensitive regulation of Gln3p activity.

Indexed as

PrionsRepressor ProteinsSaccharomyces cerevisiae ProteinsTranscription FactorsAmino Acid SequenceBase SequenceCell NucleusDNA-Binding ProteinsDNA PrimersFungal ProteinsGlutathione PeroxidaseGreen Fluorescent ProteinsLuminescent ProteinsMolecular Sequence DataProtein BindingRecombinant Fusion ProteinsDNA-Binding ProteinsDNA PrimersFungal ProteinsGLN3 protein, S cerevisiaeGlutathione PeroxidaseGreen Fluorescent ProteinsLuminescent ProteinsPrionsRecombinant Fusion ProteinsRepressor ProteinsSaccharomyces cerevisiae ProteinsSerineTranscription FactorsURE2 protein, S cerevisiae

Identifiers

PMID11408486
PMCPMC4384441
OpenAlexW1964921534

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.