Evidence map›Paper›PMID 42613518›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

Degradation System: Sialidase.

Kazuhiro Shiozaki, Koji Yamamoto, Taeko Miyagi

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2026. 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
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.

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

3 authors.

Kazuhiro ShiozakiFaculty of Fisheries and The United Graduate School of Agricultural Science, Kagoshima University, Kagoshima, Japan.
Koji YamamotoFaculty of Health and Medical Care, Saitama Medical University, Saitama, Japan.
Taeko MiyagiCancer Chemotherapy, Miyagi Cancer Center Research Institute, Miyagi, Japan. miyagi-ta@nifty.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sialidases are crucial enzymes responsible for the desialylation of gangliosides. In vertebrates, four sialidases-Neu1, Neu2, Neu3, and Neu4-exhibit distinct reactivity profiles toward gangliosides. This study aims to elucidate the physiological roles of ganglioside degradation mediated by these four sialidases, while also providing a comprehensive analysis of the methodologies employed to study their activity. By understanding the specific functions and analytical approaches associated with each sialidase, we can gain insight into their contributions to various physiological phenomena.

Indexed as

GangliosidesNeuraminidaseAnimalsHumansN-Acetylneuraminic AcidSubstrate SpecificityGangliosidesN-Acetylneuraminic AcidNeuraminidaseGangliosidesN-acetylneuraminic acidSialic acidSialidase

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.