Evidence map›Paper›PMID 38954197›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2024

Assaying Lysosomal Enzyme Activity in Dictyostelium discoideum.

William D Kim, Adam F DiGiacinto, Robert J Huber

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

3 authors.

William D KimEnvironmental and Life Sciences Graduate Program, Trent University, Peterborough, ON, Canada.
Adam F DiGiacintoDepartment of Biology, Trent University, Peterborough, ON, Canada.
Robert J HuberEnvironmental and Life Sciences Graduate Program, Trent University, Peterborough, ON, Canada. roberthuber@trentu.ca.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysosomes are membrane-enclosed organelles that digest intracellular material. They contain more than 50 different enzymes that can degrade a variety of macromolecules including nucleic acids, proteins, polysaccharides, and lipids. In addition to functioning within lysosomes, lysosomal enzymes are also secreted. Alterations in the levels and activities of lysosomal enzymes dysregulates lysosomes, which can lead to the intralysosomal accumulation of biological material and the development of lysosomal storage diseases (LSDs) in humans. Dictyostelium discoideum has a long history of being used to study the trafficking and functions of lysosomal enzymes. More recently, it has been used as a model system to study several LSDs. In this chapter, we outline the methods for assessing the activity of several lysosomal enzymes in D. discoideum (α-galactosidase, β-galactosidase, α-glucosidase, β-glucosidase, β-N-acetylglucosaminidase, α-mannosidase, cathepsin B, cathepsin D, cathepsin F, palmitoyl protein thioesterase 1, and tripeptidyl peptidase 1).

Indexed as

DictyosteliumLysosomesbeta-GalactosidaseEnzyme AssaysHumansLysosomal Storage DiseasesThiolester HydrolasesTripeptidyl-Peptidase 1beta-GalactosidaseThiolester HydrolasesTPP1 protein, humanTripeptidyl-Peptidase 1CathepsinDictyostelium discoideumEnzymeHydrolaseLysosomeModel systemThioesterase

Identifiers

PMID38954197

What OpenQuestion holds

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Registered trials

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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.