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Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants.

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TLDR
The cyclic heptapeptide, microcystin‐LR, inhibits protein phosphatases 1 (PP1) and 2A (PP2A) with K i, values below 0.1 nM, and this results are strikingly similar to those obtained with the tumour promoter okadaic acid.
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This article is published in FEBS Letters.The article was published on 1990-05-21 and is currently open access. It has received 1555 citations till now. The article focuses on the topics: Okadaic acid & Protein tyrosine phosphatase.

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Reference BookDOI

Toxic cyanobacteria in water: a guide to their public health consequences, monitoring and management.

TL;DR: The state of knowledge regarding the principal considerations in the design of programmes and studies for monitoring water resources and supplies and describes the approaches and procedures used as mentioned in this paper, and the information needed for protecting drinking water sources and recreational water bodies from the health hazards caused by cyanobacteria and their toxins.
Journal ArticleDOI

Calcineurin : form and function

TL;DR: This review provides a comprehensive examination of the biological roles of calcineurin and reviews aspects related to its structure and catalytic mechanism.
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Serine/Threonine Phosphatases: Mechanism through Structure

Yigong Shi
- 30 Oct 2009 - 
TL;DR: Biochemical and structural investigations that advance the mechanistic understanding of the three major classes of PSPs are discussed, with a focus on PP2A.
Journal ArticleDOI

The Effects of Harmful Algal Blooms on Aquatic Organisms

TL;DR: The Effects of Harmful Algal Blooms on Aquatic Organisms: Vol. 10, No. 2, pp. 113-390 as mentioned in this paper was the first publication of this article.
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Journal ArticleDOI

The structure and regulation of protein phosphatases

TL;DR: Four major serine/threonine-specific protein phosphatase catalytic subunits are present in the cytoplasm of animal cells and have broad and overlapping specificities in vitro, and account for virtually all measurable activity in tissue extracts toward a variety of phosphoproteins that regulate metabolism, muscle contractility, and other processes.
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Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics

TL;DR: Kinetic studies showed that okadaic acid acts as a non-competitive or mixed inhibitor on the okadaIC acid-sensitive enzymes.
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Okadaic acid: a new probe for the study of cellular regulation.

TL;DR: The tumour promoter okadaic acid is a potent and specific inhibitor of protein phosphatases 1 and 2A and is extremely useful for identifying biological processes that are controlled through the reversible phosphorylation of proteins.
Journal ArticleDOI

Protein phosphatases come of age.

TL;DR: This Minireview will concentrate on recent progress that has demonstrated key roles for these enzymes in tumor suppression and in cell division and identified novel phosphatase catalytic subunits.
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An improved procedure for identifying and quantitating protein phosphatases in mammalian tissues

TL;DR: An improved procedure for the identification and quantitation of type 1, type 2A and type 2C protein phosphatases in tissue extracts is developed.
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