Voltage Clamp Fluorometry of P-Type ATPases.

Robert E Dempski

Abstract read

In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

–field-weighted citation impact, top 77% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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

1 author at 1 institution in 1 country.

Robert E DempskiDepartment of Chemistry and Biochemistry, Worcester Polytechnic Institute, 100 Institute Road, Worcester, MA, 01609, USA. rdempski@wpi.edu.

Worcester Polytechnic Institute · US

Funding

The molecular determinants of zinc uptake mediated by hZIP4R01GM105964 · NIGMS · WORCESTER POLYTECHNIC INSTITUTE · PI DEMPSKI, ROBERT EDWARD · 2014 to 2018

$1.4M

NIGMS NIH HHS GM105964NIGMS NIH HHS R01 GM105964

6 · The paper itself

Abstract

Voltage clamp fluorometry has become a powerful tool to compare partial reactions of P-type ATPases such as the Na(+),K(+)-ATPase and H(+),K(+)-ATPase with conformational dynamics of these ion pumps. Here, we describe the methodology to heterologously express membrane proteins in X. laevis oocytes and site-specifically label these proteins with one or more fluorophores. Fluorescence changes are measured simultaneously with current measurements under two-electrode voltage clamp conditions.

Indexed as

AnimalsFluorometryH(+)-K(+)-Exchanging ATPaseOocytesPatch-Clamp TechniquesRNA, MessengerSodium-Potassium-Exchanging ATPaseXenopus laevisH(+)-K(+)-Exchanging ATPaseRNA, MessengerSodium-Potassium-Exchanging ATPaseDistance constraintsDonor photobleachingFluorescence

Identifiers

PMID26695040

DOI10.1007/978-1-4939-3179-8_25

PMCPMC4717471

OpenAlexW2407899171

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.