Evidence map›Paper›PMID 20946842›Full record

ArticleMethods in enzymology2010

Kinetic studies of the yeast His-Asp phosphorelay signaling pathway.

Alla O Kaserer, Babak Andi, Paul F Cook, 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 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.0field-weighted citation impact, top 21% 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

5 citing papers in PubMed, 10 citations in OpenAlex.

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  5. Review
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.

Alla O KasererDepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma, USA.
Babak Andi
Paul F Cook
Ann H West
University 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
NIGMS NIH HHS GM59311NIGMS NIH HHS R01 GM059311
6 · The paper itself

Abstract

For both prokaryotic and eukaryotic His-Asp phosphorelay signaling pathways, the rates of protein phosphorylation and dephosphorylation determine the stimulus-to-response time frame. Thus, kinetic studies of phosphoryl group transfer between signaling partners are important for gaining a full understanding of how the system is regulated. In many cases, the phosphotransfer reactions are too fast for rates to be determined by manual experimentation. Rapid quench flow techniques thus provide a powerful method for studying rapid reactions that occur in the millisecond time frame. In this chapter, we describe experimental design and procedures for kinetic characterization of the yeast SLN1-YPD1-SSK1 osmoregulatory phosphorelay system using a rapid quench flow kinetic instrument.

Indexed as

Intracellular Signaling Peptides and ProteinsKineticsProtein KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionIntracellular Signaling Peptides and ProteinsProtein KinasesSaccharomyces cerevisiae ProteinsSLN1 protein, S cerevisiaeSSK1 protein, S cerevisiaeYPD1 protein, S cerevisiae

Identifiers

PMID20946842
PMCPMC2957298
OpenAlexW1910316983

What OpenQuestion holds

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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.