Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1 (Q27729832)

5

object named as

A. C. Nairn

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18 July 2024

author name string

J. Goldberg

1

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H. B. Huang

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18 July 2024

Y. G. Kwon

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18 July 2024

J. Kuriyan

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full work available at URL

18 July 2024

language of work or name

English

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publication date

31 August 1995

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http://www.nature.com/articles/376745a0

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https://api.crossref.org/works/10.1038/376745A0

http://www.nature.com/articles/376745a0.pdf

18 July 2024

file format

Portable Document Format

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https://api.crossref.org/works/10.1038/376745A0

18 July 2024

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376

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issue

6543

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page(s)

745-53

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Immunophilin-sensitive protein phosphatase action in cell signaling pathways

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Determination of macromolecular structures from anomalous diffraction of synchrotron radiation

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Conservation analysis and structure prediction of the protein serine/threonine phosphatases. Sequence similarity with diadenosine tetraphosphatase from Escherichia coli suggests homology to the protein phosphatases.

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Predicted secondary and supersecondary structure for the serine-threonine-specific protein phosphatase family

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Structural basis for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism

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Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis

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Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site

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Hydrolysis of phosphate monoesters: a biological problem with multiple chemical solutions

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Inhibitor-2 functions like a chaperone to fold three expressed isoforms of mammalian protein phosphatase-1 into a conformation with the specificity and regulatory properties of the native enzyme.

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Conserved sequence pattern in a wide variety of phosphoesterases

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Phosphatase 2A associated with polyomavirus small-T or middle-T antigen is an okadaic acid-sensitive tyrosyl phosphatase

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Purification of type 1 protein (serine/threonine) phosphatases by microcystin-Sepharose affinity chromatography

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Mutagenesis of the catalytic subunit of rabbit muscle protein phosphatase-1.

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Comparison of the solution structures of microcystin-LR and motuporin

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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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Two isoforms of protein phosphatase 1 may be produced from the same gene

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The nucleotide sequence of the cDNA encoding the human lung protein phosphatase 2A alpha catalytic subunit

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Cloning of human calcineurin A: evidence for two isozymes and identification of a polyproline structural domain

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Discovery of a protein phosphatase activity encoded in the genome of bacteriophage lambda. Probable identity with open reading frame 221.

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Co-crystallization of the catalytic subunit of the serine/threonine specific protein phosphatase 1 from human in complex with microcystin LR.

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