Evidence map›Paper›PMID 26987901›Full record

ArticleThe Journal of biological chemistry2016

NEU3 Sialidase Protein Interactors in the Plasma Membrane and in the Endosomes.

Federica Cirillo, Andrea Ghiroldi, Chiara Fania, Marco Piccoli, Enrica Torretta, Guido Tettamanti, Cecilia Gelfi, Luigi Anastasia

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

13 citing papers in PubMed, 30 citations in OpenAlex.

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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

8 authors at 2 institutions in 1 country.

Federica CirilloFrom the Istituto Di Ricovero e Cura a Carattere Scientifico Policlinico San Donato, 20097 San Donato Milanese, Milan and.
Andrea GhiroldiFrom the Istituto Di Ricovero e Cura a Carattere Scientifico Policlinico San Donato, 20097 San Donato Milanese, Milan and.
Chiara FaniaFrom the Istituto Di Ricovero e Cura a Carattere Scientifico Policlinico San Donato, 20097 San Donato Milanese, Milan and.
Marco PiccoliFrom the Istituto Di Ricovero e Cura a Carattere Scientifico Policlinico San Donato, 20097 San Donato Milanese, Milan and.
Enrica Torrettathe Department of Biomedical Sciences for Health, University of Milan, 20122 Milan, Italy.
Guido TettamantiFrom the Istituto Di Ricovero e Cura a Carattere Scientifico Policlinico San Donato, 20097 San Donato Milanese, Milan and.
Cecilia GelfiFrom the Istituto Di Ricovero e Cura a Carattere Scientifico Policlinico San Donato, 20097 San Donato Milanese, Milan and the Department of Biomedical Sciences for Health, University of Milan, 20122 Milan, Italy.
Luigi AnastasiaFrom the Istituto Di Ricovero e Cura a Carattere Scientifico Policlinico San Donato, 20097 San Donato Milanese, Milan and the Department of Biomedical Sciences for Health, University of Milan, 20122 Milan, Italy luigi.anastasia@unimi.it.
IRCCS Policlinico San Donato · ITUniversity of Milan · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NEU3 sialidase has been shown to be a key player in many physio- and pathological processes, including cell differentiation, cellular response to hypoxic stress, and carcinogenesis. The enzyme, peculiarly localized on the outer leaflet of the plasma membrane, has been shown to be able to remove sialic acid residues from the gangliosides present on adjacent cells, thus creating cell to cell interactions. Nonetheless, herein we report that the enzyme localization is dynamically regulated between the plasma membrane and the endosomes, where a substantial amount of NEU3 is stored with low enzymatic activity. However, under opportune stimuli, NEU3 is shifted from the endosomes to the plasma membrane, where it greatly increases the sialidase activity. Finally, we found that NEU3 possesses also the ability to interact with specific proteins, many of which are different in each cell compartment. They were identified by mass spectrometry, and some selected ones were also confirmed by cross-immunoprecipitation with the enzyme, supporting NEU3 involvement in the cell stress response, protein folding, and intracellular trafficking.

Indexed as

Cell MembraneEndoplasmic Reticulum Chaperone BiPEndosomesHeat-Shock ProteinsHEK293 CellsHeLa CellsHumansNeuraminidaseProtein FoldingProtein TransportRecombinant ProteinsStress, PhysiologicalUp-RegulationEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsNeu3 protein, humanNeuraminidaseRecombinant ProteinsendosomeendosomesgangliosidegangliosidesNEU3protein-protein interactionsialidasesphingolipid

Identifiers

PMID26987901
PMCPMC4865910
OpenAlexW2305359200

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.