Evidence map›Paper›PMID 20946854›Full record

ArticleMethods in enzymology2010

Genetic and biochemical analysis of the SLN1 pathway in Saccharomyces cerevisiae.

Jan S Fassler, Ann H West

Open access · greenAbstract read
In one paragraph

Article in Methods in enzymology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Transcriptome Analysis of Dimorphic Fungus Sporothrix schenckii Exposed to Temperature Stress.International microbiology : the official journal of the Spanish Society for Microbiology · 2021
    Article
  3. Article
  4. Article
  5. The yeasts phosphorelay systems: a comparative view.World journal of microbiology & biotechnology · 2017
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. 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 at 2 institutions in 1 country.

Jan S FasslerDepartment of Biology, University of Iowa, Iowa City, Iowa, USA.
Ann H West
University of Iowa · USUniversity of Oklahoma · US

Funding

HISTIDINE TO ASPARTATE PHOSPHORYL TRANSFER IN YEASTR01GM059311 · NIGMS · UNIVERSITY OF OKLAHOMA NORMAN · PI WEST, ANN H · 1999 to 2008
$1.8M
SIGNAL TRANSDUCTION BY A YEAST TWO COMPONENT REGULATORR01GM056719 · NIGMS · UNIVERSITY OF IOWA · PI FASSLER, JAN S. · 1998 to 2005
$1.7M
Regulation of eukaryotic histidine kinasesR01GM068746 · NIGMS · UNIVERSITY OF IOWA · PI DESCHENES, ROBERT J · 2003 to 2006
$1.1M
NIGMS NIH HHS GM068746NIGMS NIH HHS GM56719NIGMS NIH HHS GM59311NIGMS NIH HHS R01 GM056719NIGMS NIH HHS R01 GM059311NIGMS NIH HHS R01 GM068746
6 · The paper itself

Abstract

The histidine kinase-based signal transduction pathway was first uncovered in bacteria and is a prominent form of regulation in prokaryotes. However, this type of signal transduction is not unique to prokaryotes; over the last decade two-component signal transduction pathways have been identified and characterized in diverse eukaryotes, from unicellular yeasts to multicellular land plants. A number of small but important differences have been noted in the architecture and function of eukaryotic pathways. Because of the powerful genetic approaches and facile molecular analysis associated with the yeast system, the SLN1 osmotic response pathway in Saccharomyces cerevisiae is particularly useful as a eukaryotic pathway model. This chapter provides an overview of genetic and biochemical methods that have been important in elucidating the stimulus-response events that underlie this pathway and in understanding the details of a eukaryotic His-Asp phosphorelay.

Indexed as

Intracellular Signaling Peptides and ProteinsPhosphorylationProtein KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionIntracellular Signaling Peptides and ProteinsProtein KinasesSaccharomyces cerevisiae ProteinsSLN1 protein, S cerevisiae

Identifiers

PMID20946854
PMCPMC2957310
OpenAlexW1530627041

What OpenQuestion holds

Textmetadata
LicenceTDM
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.