Evidence map›Paper›PMID 27890939›Full record

ReviewCoordination chemistry reviews2016

The metal face of protein tyrosine phosphatase 1B.

Elisa Bellomo, Kshetrimayum Birla Singh, Alberto Massarotti, Christer Hogstrand, Wolfgang Maret

Open access · hybridAbstract readReview
In one paragraph

Review in Coordination chemistry reviews, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

38 citing papers in PubMed, 88 citations in OpenAlex.

  1. Vanadium salt inhibits osteoclast formation and preserves bone integrity in a rat model of type-1 diabetes associated bone loss.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
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  11. Shikonin and Juglone InhibitBiotech (Basel (Switzerland)) · 2023
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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

5 authors at 2 institutions in 2 countries.

Elisa BellomoMetal Metabolism Group, Division of Diabetes and Nutritional Sciences, Faculty of Life Sciences and Medicine, King's College London, London, UK.
Kshetrimayum Birla SinghMetal Metabolism Group, Division of Diabetes and Nutritional Sciences, Faculty of Life Sciences and Medicine, King's College London, London, UK.
Alberto MassarottiDipartimento di Scienze del Farmaco, Università del Piemonte Orientale "A. Avogadro", Novara, Italy.
Christer HogstrandMetal Metabolism Group, Division of Diabetes and Nutritional Sciences, Faculty of Life Sciences and Medicine, King's College London, London, UK.
Wolfgang MaretMetal Metabolism Group, Division of Diabetes and Nutritional Sciences, Faculty of Life Sciences and Medicine, King's College London, London, UK.
King's College London · GBUniversità degli Studi del Piemonte Orientale “Amedeo Avogadro” · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A new paradigm in metallobiochemistry describes the activation of inactive metalloenzymes by metal ion removal. Protein tyrosine phosphatases (PTPs) do not seem to require a metal ion for enzymatic activity. However, both metal cations and metal anions modulate their enzymatic activity. One binding site is the phosphate binding site at the catalytic cysteine residue. Oxyanions with structural similarity to phosphate, such as vanadate, inhibit the enzyme with nanomolar to micromolar affinities. In addition, zinc ions (Zn

Identifiers

PMID27890939
PMCPMC5115158
OpenAlexW2464993195

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.