(Q27730228)

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Comparison of the solution structures of microcystin-LR and motuporin

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Comparison of the solution structures of microcystin-LR and motuporin (English)

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author name string

J R Bagu

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1

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F D Sönnichsen

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2

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D Williams

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3

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R J Andersen

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4

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B D Sykes

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5

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C F Holmes

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6

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February 1995

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Nature structural biology

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volume

2

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114-6

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2

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https://scigraph.springernature.com/pub.10.1038/nsb0295-114

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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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21 January 2018

Structure-Function Relationships of Microcystins, Liver Tumor Promoters, in Interaction with Protein Phosphatase

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21 January 2018

Inhibitors of protein kinases and phosphatases

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21 January 2018

Structural modifications imparting reduced toxicity in microcystins from Microcystis spp.

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21 January 2018

The toxins of cyanobacteria

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31 March 2020

Inhibition of protein phosphatases by microcystins and nodularin associated with hepatotoxicity

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31 March 2020

Hepatocyte deformation induced by cyanobacterial toxins reflects inhibition of protein phosphatases

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https://api.crossref.org/works/10.1038%2FNSB0295-114

retrieved

31 March 2020

Hyperphosphorylation of cytokeratins 8 and 18 by microcystin-LR, a new liver tumor promoter, in primary cultured rat hepatocytes

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https://api.crossref.org/works/10.1038%2FNSB0295-114

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31 March 2020

Nodularin, microcystin, and the configuration of Adda

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31 March 2020

Identification and characterization of hydrophobic microcystins in Canadian freshwater cyanobacteria

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31 March 2020

Motuporin, A Potent Protein Phosphatase Inhibitor Isolated from the Papua New Guinea Sponge Theonella swinhoei Gray

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31 March 2020

NMR studies of [U-13C]cyclosporin A bound to cyclophilin: bound conformation and portions of cyclosporin involved in binding

(Q27730228)

Comparison of the solution structures of microcystin-LR and motuporin

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