The Eleventh Datta Lecture. The structural basis for substrate recognition and control by protein kinases (Q47789294)

5 February 2018

review article

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title

The Eleventh Datta Lecture. The structural basis for substrate recognition and control by protein kinases (English)

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5 February 2018

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5 February 2018

author name string

L N Johnson

series ordinal

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5 February 2018

E D Lowe

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5 February 2018

D J Owen

series ordinal

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5 February 2018

language of work or name

English

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publication date

1 June 1998

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5 February 2018

published in

FEBS Letters

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5 February 2018

volume

430

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5 February 2018

issue

1-2

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5 February 2018

page(s)

1-11

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5 February 2018

The protein kinases of budding yeast: six score and more

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2.2 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor

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Atomic structure of the MAP kinase ERK2 at 2.3 A resolution

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The structure of mitogen-activated protein kinase p38 at 2.1-A resolution

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Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

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Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product

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The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition

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Three-dimensional structure of mammalian casein kinase I: molecular basis for phosphate recognition

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Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog

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Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism

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Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation

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

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Three protein kinase structures define a common motif

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Structure of an enzyme required for aminoglycoside antibiotic resistance reveals homology to eukaryotic protein kinases

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Active and inactive protein kinases: structural basis for regulation

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Domain movements in protein kinases

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A structural basis for substrate specificities of protein Ser/Thr kinases: primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1.

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Inactivation and Activation of Liver Phosphorylase

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Crystal structure of casein kinase-1, a phosphate-directed protein kinase

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29 Use of peptide substrates to study the specificity of phosphorylase kinase phosphorylation

7 January 2021

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Solution structure of the cAMP-dependent protein kinase catalytic subunit and its contraction upon binding the protein kinase inhibitor peptide

7 January 2021

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Chemical mechanism of the adenosine cyclic 3',5'-monophosphate dependent protein kinase from pH studies

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The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification 1

7 January 2021

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inferred from DOI database lookup

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based on heuristic

Identifiers

DOI

10.1016/S0014-5793(98)00606-1

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5 February 2018

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5 February 2018