Evidence map›Paper›PMID 21210280›Full record

ArticleEuropean journal of applied physiology2011

Strong ion reserve: a viewpoint on acid base equilibria and buffering.

Michalis Agrafiotis

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in European journal of applied physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Frontiers in medicine · 2025
    Article
  2. Article
  3. Review
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

1 author.

Michalis AgrafiotisSecond Department of Intensive Care Medicine, "Georgios Papanikolaou" General Hospital of Thessaloniki, 57010, Exochi, Greece. m.agrafiotis@gmail.com

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Evidence suggests that strong ions can exist reversibly bound to proteins in a pH-dependent manner and that they can be recruited into the biological solution, modulating its strong ion difference in a process that opposes the acid base disturbances imposed on the system. These recruitable strong ions represent the solution's 'strong ion reserve'. The physiologic [corrected] role of these protein-bound strong ions [corrected] in the buffering of acid base disorders is discussed.

Indexed as

Acid-Base EquilibriumBuffersChemistry, AnalyticHumansHydrogen-Ion ConcentrationIonsModels, TheoreticalOsmolar ConcentrationProteinsResearchSolutionsBuffersIonsProteinsSolutions

Identifiers

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.