Evidence map›Paper›PMID 31642774›Full record

ReviewCurrent protein & peptide science2020

Using Yeast to Define the Regulatory Role of Protein Lysine Methylation.

Yogita Jethmalani, Erin M Green

Abstract readReview
In one paragraph

Review in Current protein & peptide science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. A novel role of DOT1L in kidney diseases.Molecular biology reports · 2023
    Review
  5. 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

2 authors.

Yogita JethmalaniDepartment of Biological Sciences, University of Maryland Baltimore County, Baltimore, MD, United States.
Erin M GreenDepartment of Biological Sciences, University of Maryland Baltimore County, Baltimore, MD, United States.

Funding

Lysine methylation at chromatin and cellular responses to stressR01GM124342 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI GREEN, ERIN · 2017 to 2021
$1.5M
The SMYD lysine methyltransferase Set6 in signaling and proteostasisR21AG064507 · NIA · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI GREEN, ERIN · 2019 to 2020
$400k
NIA NIH HHS R21 AG064507NIGMS NIH HHS R01 GM124342
6 · The paper itself

Abstract

The post-translational modifications (PTM) of proteins are crucial for cells to survive under diverse environmental conditions and to respond to stimuli. PTMs are known to govern a broad array of cellular processes including signal transduction and chromatin regulation. The PTM lysine methylation has been extensively studied within the context of chromatin and the epigenetic regulation of the genome. However, it has also emerged as a critical regulator of non-histone proteins important for signal transduction pathways. While the number of known non-histone protein methylation events is increasing, the molecular functions of many of these modifications are not yet known. Proteomic studies of the model system Saccharomyces cerevisiae suggest lysine methylation may regulate a diversity of pathways including transcription, RNA processing, translation, and signal transduction cascades. However, there has still been relatively little investigation of lysine methylation as a broad cellular regulator beyond chromatin and transcription. Here, we outline our current state of understanding of non-histone protein methylation in yeast and propose ways in which the yeast system can be leveraged to develop a much more complete picture of molecular mechanisms through which lysine methylation regulates cellular functions.

Indexed as

Gene Expression Regulation, FungalProtein Processing, Post-TranslationalChromatinHistone-Lysine N-MethyltransferaseHistonesLysineMethylationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionChromatinHistone-Lysine N-MethyltransferaseHistonesLysineSaccharomyces cerevisiae ProteinsmethylationPost-translational modificationsignalingtranscriptiontranslationyeast

Identifiers

PMID31642774
PMCPMC7176527

What OpenQuestion holds

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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.