Evidence map›Paper›PMID 23650586›Full record

ArticleFEBS open bio2012

Tyrosine phosphorylation plays a role in increasing maspin protein levels and its cytoplasmic accumulation.

Mariana Tamazato Longhi, Nathalie Cella

Open access · goldAbstract read
In one paragraph

Article in FEBS open bio, 2012. 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
0.5field-weighted citation impact, top 36% 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, 20 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

2 authors at 1 institution in 1 country.

Mariana Tamazato LonghiDepartamento de Biologia Celular e Desenvolvimento, Instituto de Ciências Biomédicas, Av. Prof. Lineu Prestes, 1524, Universidade de São Paulo, São Paulo 05508-900, SP, Brazil ; Departamento de Bioquímica, Instituto de Química, Av. Prof. Lineu Prestes, 748, Universidade de São Paulo, São Paulo 05508-900, SP, Brazil.
Nathalie Cella
Universidade de São Paulo · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Maspin is a tumor suppressor with many biological activities, multiple ligands and different subcellular localizations. Its underlying molecular mechanism remains elusive. We hypothesized that phosphorylation might regulate maspin localization and function. Using two-dimensional gel electrophoresis with different focusing power followed by Western blot we identified four different maspin forms with the same molecular weight (42 kDa), but different isoelectric points. Three of these forms were sensitive to acidic phosphatase treatment, suggesting that they are phosphorylated. Sodium peroxidovanadate treatment, a protein-tyrosine phosphatase inhibitor, resulted in a rapid increase in maspin protein levels and cytoplasmic accumulation. These data show that there are three different maspin tyrosine phosphoforms. Inhibition of tyrosine phosphatases increased maspin protein levels and leads to its cytoplasmic accumulation.

Indexed as

2D-SDS-PAGE, two-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresisCytoplasmic accumulationDTT, dithiothreitolGAPDH, glyceraldehyde 3-phosphate dehydrogenaseIEF, isoelectric focalizationMaspinPTM, post-translational modificationserpin, serine protease inhibitorTumor suppressorTyrosine phosphorylation

Identifiers

PMID23650586
PMCPMC3642124
OpenAlexW2030478160

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.