Evidence map›Paper›PMID 7565699›Full record

ArticleMolecular and cellular biology1995

Structure-function relationships of the yeast cyclin-dependent kinase Pho85.

R C Santos, N C Waters, C L Creasy, L W Bergman

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

13 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  4. Mammalian Cdk5 is a functional homologue of the budding yeast Pho85 cyclin-dependent protein kinase.Proceedings of the National Academy of Sciences of the United States of America · 1999
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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

4 authors at 1 institution in 1 country.

R C SantosDepartment of Microbiology, Medical College of Pennsylvania, Philadelphia, USA.
N C Waters
C L Creasy
L W Bergman
Hahnemann University Hospital · US

Funding

NIGMS NIH HHS GM41620
6 · The paper itself

Abstract

The PHO85 gene of Saccharomyces cerevisiae encodes a cyclin-dependent kinase involved in both transcriptional regulation and cell cycle progression. Although a great deal is known concerning the structure, function, and regulation of the highly homologous Cdc28 protein kinase, little is known concerning these relationships in regard to Pho85. In this study, we constructed a series of Pho85-Cdc28 chimeras to map the region(s) of the Pho85 molecule that is critical for function of Pho85 in repression of acid phosphatase (PHO5) expression. Using a combination of site-directed and ethyl methanesulfonate-induced mutagenesis, we have identified numerous residues critical for either activation of the Pho85 kinase, interaction of Pho85 with the cyclin-like molecule Pho80, or substrate recognition. Finally, analysis of mutations analogous to those previously identified in either Cdc28 or cdc2 of Schizosaccharomyces pombe suggested that the inhibition of Pho85-Pho80 activity in mechanistically different from that seen in the other cyclin-dependent kinases.

Indexed as

Repressor ProteinsSaccharomyces cerevisiae ProteinsAcid PhosphataseAmino Acid SequenceCDC28 Protein Kinase, S cerevisiaeConserved SequenceCyclin-Dependent KinasesCyclinsEnzyme RepressionFungal ProteinsGenetic Complementation TestMolecular Sequence DataMutagenesisRecombinant Fusion ProteinsSaccharomyces cerevisiaeSequence AlignmentAcid PhosphataseCDC28 Protein Kinase, S cerevisiaeCyclin-Dependent KinasesCyclinsFungal ProteinsPHO80 protein, S cerevisiaePHO85 protein, S cerevisiaeRecombinant Fusion ProteinsRepressor ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID7565699
PMCPMC230798
OpenAlexW2145316333

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.