ArticleBiometals : an international journal on the role of metal ions in biology, biochemistry, and medicine2017
The interactions of metal cations and oxyanions with protein tyrosine phosphatase 1B.
Article in Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers, 1 of them a synthesis that pooled it.
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Who cites it
9 citing papers in PubMed, 1 synthesis or guideline pooled it, 24 citations in OpenAlex.
- The preventive and carcinogenic effect of metals on cancer: a systematic review.BMC public health · 2024Pooled it
- Sodium tungstate promotes vascularization to support beta cell replacement in diabetes.EMBO molecular medicine · 2026Article
- PTPN2 copper-sensing relays copper level fluctuations into EGFR/CREB activation and associated CTR1 transcriptional repression.Nature communications · 2024Article
- Does the Micronutrient Molybdenum Have a Role in Gestational Complications and Placental Health?Nutrients · 2023Review
- Heavy metal ions exchange driven protein phosphorylation cascade functions in genomic instability in spermatocytes and male infertility.Nucleic acids research · 2023Article
- Heavy Metals in the Environment and Thyroid Cancer.Cancers · 2021Review
- Regulatory Role of Zinc in Immune Cell Signaling.Molecules and cells · 2021Review
- Increased Thyroid Cancer Incidence in Volcanic Areas: A Role of Increased Heavy Metals in the Environment?International journal of molecular sciences · 2020Review
- Article
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Protein tyrosine phosphatases are not considered to be metalloenzymes. Yet, they are inhibited by zinc cations and metal and non-metal oxyanions that are chemical analogues of phosphate, e.g. vanadate. Metal inhibition is generally not recognized as these enzymes are purified, supplied, and assayed with buffers containing chelating and reducing agents. We screened a series of cations and anions for their capacity to inhibit protein tyrosine phosphatase 1B and discuss the ensuing general issues with inhibition constants reported in the scientific literature. In contrast to zinc, which binds to the phosphocysteine intermediate in the closed conformation of protein tyrosine phosphatase 1B when the catalytic aspartate has moved into the active site, other divalent cations such as cadmium and copper may also bind to the enzyme in the open conformation. Inhibition by both anions and cations, conditions such as pH, the presence of metal ligands such as glutathione, and the existence of multiple conformational states of protein tyrosine phosphatases in the reaction cycle establish a complex pattern of inhibition of these important regulatory enzymes with implications for the physiology, pharmacology and toxicology of metal ions.
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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.