Evidence map›Paper›PMID 33665382›Full record

ArticleBiochemistry and biophysics reports2021

Macromolecular crowding effects on the kinetics of opposing reactions catalyzed by alcohol dehydrogenase.

Xander E Wilcox, Charmaine B Chung, Kristin M Slade

Open access · goldAbstract read
In one paragraph

Article in Biochemistry and biophysics reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

11 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Aggregation of Phosphates Enhances Enzyme Activity in Aqueous Solution.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Biomedical Applications of Nanozymes: An Enzymology Perspective.Angewandte Chemie (International ed. in English) · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Parameter Reliability and Understanding Enzyme Function.Molecules (Basel, Switzerland) · 2022
    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

3 authors at 2 institutions in 1 country.

Xander E WilcoxDepartment of Chemistry, University of California at Davis, CA, 95616, USA.
Charmaine B ChungDepartment of Chemistry, Hobart and William Smith Colleges, 300 Pulteney St, Geneva, NY, 14456, USA.
Kristin M SladeDepartment of Chemistry, Hobart and William Smith Colleges, 300 Pulteney St, Geneva, NY, 14456, USA.
Hobart and William Smith Colleges · USUniversity of California, Davis · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In order to better understand how the complex, densely packed, heterogeneous milieu of a cell influences enzyme kinetics, we exposed opposing reactions catalyzed by yeast alcohol dehydrogenase (YADH) to both synthetic and protein crowders ranging from 10 to 550 kDa. The results reveal that the effects from macromolecular crowding depend on the direction of the reaction. The presence of the synthetic polymers, Ficoll and dextran, decrease V

Indexed as

Alcohol dehydrogenaseDepletion layerdex, dextran (number afterward represents the molecular weight of the polymer in kDa)DextrankDa, kilodaltonsKD, dissociation constantKm, is Michaelis constantMacromolecular crowdingMichaelis-mentenPEG, polyethylene glycolPVP, polyvinylpyrrolidoneSteady state kineticsVmax, maximal rate under Michaelis-Menten kinetics

Identifiers

PMID33665382
PMCPMC7905371
OpenAlexW3132467223

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.