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Regulatory Subunit of Protein Kinase A: Structure of Deletion Mutant with cAMP Binding Domains

Science (American Association for the Advancement of Science), 1995-08, Vol.269 (5225), p.807-813

1995

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Probing the cyclic nucleotide binding sites of cAMP-dependent protein kinases I and II with analogs of adenosine 3',5'-cyclic phosphorothioates

The Journal of biological chemistry, 1990-06, Vol.265 (18), p.10484-10491

1990

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Spatiotemporal Dynamics of Guanosine 3′,5′-Cyclic Monophosphate Revealed by a Genetically Encoded, Fluorescent Indicator

Proceedings of the National Academy of Sciences - PNAS, 2001-02, Vol.98 (5), p.2437-2442

2001

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Determination of Cyclic Nucleotide-Dependent Protein Kinase Substrate Specificity by the Use of Peptide Libraries on Cellulose Paper

Biochemistry (Easton), 1995-08, Vol.34 (33), p.10569-10577

1995

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Active Site Mutations Define the Pathway for the Cooperative Activation of cAMP-Dependent Protein Kinase

Biochemistry (Easton), 1996-03, Vol.35 (9), p.2934-2942

1996

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Crosstalk between Domains in the Regulatory Subunit of cAMP-Dependent Protein Kinase: Influence of Amino Terminus on cAMP Binding and Holoenzyme Formation

Biochemistry (Easton), 1994-06, Vol.33 (23), p.7485-7494

1994

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Isoleucine 368 is involved in low-affinity binding of N6-modified cAMP analogues to site B of the regulatory subunit of cAMP-dependent protein kinase I

Biochemical journal, 1996-05, Vol.316 ( Pt 1) (Pt 1), p.337-343

1996

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Identification of the amino acid sequences responsible for high affinity activation of cGMP kinase Ialpha

The Journal of biological chemistry, 1997-04, Vol.272 (16), p.10522

1997

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Ala335 is essential for high‐affinity cAMP‐binding of both sites A and B of cAMP‐dependent protein kinase type I

FEBS letters, 1995-04, Vol.362 (3), p.291-294

1995

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Crystal Structure of cGMP-Dependent Protein Kinase Reveals Novel Site of Interchain Communication

Structure (London), 2011-09, Vol.19 (9), p.1317-1327

2011

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The switch helix: A putative combinatorial relay for interprotomer communication in cGMP-dependent protein kinase

Biochimica et biophysica acta, 2013-07, Vol.1834 (7), p.1346-1351

2013

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An N-terminally truncated form of cyclic GMP–dependent protein kinase Iα (PKG Iα) is monomeric and autoinhibited and provides a model for activation

The Journal of biological chemistry, 2018-05, Vol.293 (21), p.7916-7929

2018

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Regulatory Subunit of Protein Kinase A: Structure of Deletion Mutant with cAMP Binding Domains

Probing the cyclic nucleotide binding sites of cAMP-dependent protein kinases I and II with analogs of adenosine 3',5'-cyclic phosphorothioates

Spatiotemporal Dynamics of Guanosine 3′,5′-Cyclic Monophosphate Revealed by a Genetically Encoded, Fluorescent Indicator

Determination of Cyclic Nucleotide-Dependent Protein Kinase Substrate Specificity by the Use of Peptide Libraries on Cellulose Paper

Active Site Mutations Define the Pathway for the Cooperative Activation of cAMP-Dependent Protein Kinase

Crosstalk between Domains in the Regulatory Subunit of cAMP-Dependent Protein Kinase: Influence of Amino Terminus on cAMP Binding and Holoenzyme Formation

Isoleucine 368 is involved in low-affinity binding of N6-modified cAMP analogues to site B of the regulatory subunit of cAMP-dependent protein kinase I

Identification of the amino acid sequences responsible for high affinity activation of cGMP kinase Ialpha

Ala335 is essential for high‐affinity cAMP‐binding of both sites A and B of cAMP‐dependent protein kinase type I

Crystal Structure of cGMP-Dependent Protein Kinase Reveals Novel Site of Interchain Communication

The switch helix: A putative combinatorial relay for interprotomer communication in cGMP-dependent protein kinase

An N-terminally truncated form of cyclic GMP–dependent protein kinase Iα (PKG Iα) is monomeric and autoinhibited and provides a model for activation

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