Evidence map›Paper›PMID 7050667›Full record

ArticleMolecular and cellular biology1982

Synthesis of specific identified, phosphorylated, heat shock, and heat stroke proteins through the cell cycle of Saccharomyces cerevisiae.

J R Ludwig, J J Foy, S G Elliott, C S McLaughlin

Abstract read
In one paragraph

Article in Molecular and cellular biology, 1982. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

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  16. Identification of a labile protein involved in the G1-to-S transition in Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 1984
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  17. 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

4 authors.

J R Ludwig
J J Foy
S G Elliott
C S McLaughlin

Funding

NCI NIH HHS CA-06504NCI NIH HHS CA-10628
6 · The paper itself

Abstract

The methods of centrifugal elutriation, two-dimensional gel electrophoresis, and dual isotopic labeling were applied to the study and identification of a number of purified yeast proteins. The location of polypeptide spots corresponding to specific proteins was determined on two-dimensional gels. A dual-label method was used to determine the rates of synthesis through the cell cycle of the identified proteins as well as to confirm the results of previous studies from our laboratory on unidentified proteins. The identified proteins, and the more generally defined phosphorylated, heat shock, and heat stroke proteins were found to follow the general pattern of exponential increase in rate of synthesis through the cell cycle. In addition, colorimetric enzyme activity assays were used to examine the catabolic enzyme alpha-glucosidase (EC 3.2.1.20). Both the activity and synthesis of alpha-glucosidase were found to be nonperiodic with respect to the cell cycle. These data contrast with earlier reports of periodicity, which employed induction and selection synchrony to study enzyme expression through the yeast cell cycle.

Indexed as

Cell CycleProtein BiosynthesisProteinsalpha-GlucosidasesCell SeparationElectrophoresis, Polyacrylamide GelFungal ProteinsHeat-Shock ProteinsPhosphoproteinsSaccharomyces cerevisiaealpha-GlucosidasesFungal ProteinsHeat-Shock Proteinsheat stroke proteinsPhosphoproteinsProteins

Identifiers

PMID7050667
PMCPMC369764

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.