Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential (Q27748804)

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author name string

L. Prade

1

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A. Girod

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V. Kinzel

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R. Huber

5

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D. Bossemeyer

6

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language of work or name

English

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National Center for Biotechnology Information

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full work available at URL

3 December 2024

publication date

15 December 1997

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http://www.cell.com/article/S0969212697003109/pdf

file format

Portable Document Format

online access status

open access

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3 December 2024

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https://api.elsevier.com/content/article/PII:S0969212697003109?httpAccept=text/plain

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5

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issue

12

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page(s)

1627-37

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28 Use and specificity of staurosporine, UCN-O1, and calphostin C as protein kinase inhibitors

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Staurosporine is a potent inhibitor of p34cdc2 and p34cdc2-like kinases

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Staurosporine, a potent inhibitor of phospholipid/Ca++dependent protein kinase

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Characterization of specific binding sites for [3H]-staurosporine on various protein kinases

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Characterization of receptor tyrosine-specific protein kinases by the use of inhibitors. Staurosporine is a 100-times more potent inhibitor of insulin receptor than IGF-I receptor.

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Staurosporine causes epidermal growth factor to induce differentiation in PC12 cells via receptor up-regulation

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Staurosporine induces a complete program of terminal differentiation in neoplastic mouse keratinocytes via activation of protein kinase C.

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Staurosporine induces programmed cell death in embryonic neurons and activation of the ceramide pathway.

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A derivative of staurosporine (CGP 41 251) shows selectivity for protein kinase C inhibition and in vitro anti-proliferative as well as in vivo anti-tumor activity

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Staurosporine: An Effective Inhibitor for Ca2+/Calmodulin-Dependent Protein Kinase II

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Different susceptibility of protein kinases to staurosporine inhibition. Kinetic studies and molecular bases for the resistance of protein kinase CK2

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Crystal structures of catalytic subunit of cAMP-dependent protein kinase in complex with isoquinolinesulfonyl protein kinase inhibitors H7, H8, and H89. Structural implications for selectivity

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High-resolution crystal structures of human cyclin-dependent kinase 2 with and without ATP: bound waters and natural ligand as guides for inhibitor design

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Structural basis for selectivity of the isoquinoline sulfonamide family of protein kinase inhibitors

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Modelling study of protein kinase inhibitors: binding mode of staurosporine and origin of the selectivity of CGP 52411

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Inhibition mechanisms of staurosporine and H7 to cAMP-dependent protein kinase through docking study

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Cloning of the C alpha catalytic subunit of the bovine cAMP-dependent protein kinase

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Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase

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A binary complex of the catalytic subunit of cAMP-dependent protein kinase and adenosine further defines conformational flexibility

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3 December 2024

Identifiers

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Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017