Physiological Substrates of cAMP-Dependent Protein Kinase

Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B

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Specificity and mechanism of action of some commonly used protein kinase inhibitors

DAVIES, S. P., REDDY, H., CAIVANO, M., & COHEN, P. (2000) · Biochemical Journal · doi:10.1042/bj3510095 · Cited by 3,132

THE STRUCTURE AND REGULATION OF PROTEIN PHOSPHATASES

Cohen, P. (1989) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.58.070189.002321 · Cited by 2,524

Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine 133

Gonzalez, G. A., & Montminy, M. R. (1989) · Cell · doi:10.1016/0092-8674(89)90013-5 · Cited by 2,464

Phosphorylation-Dephosphorylation of Enzymes

Krebs, E. G., & Beavo, J. A. (1979) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.48.070179.004423 · Cited by 2,205

CREB: A Stimulus-Induced Transcription Factor Activated by A Diverse Array of Extracellular Signals

Shaywitz, A. J., & Greenberg, M. E. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.821 · Cited by 2,134

From Ionic Currents to Molecular Mechanisms

Catterall, W. A. (2000) · Neuron · doi:10.1016/s0896-6273(00)81133-2 · Cited by 2,118

Phosphorylated CREB binds specifically to the nuclear protein CBP

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PKA Phosphorylation Dissociates FKBP12.6 from the Calcium Release Channel (Ryanodine Receptor)

Marx, S. O., Reiken, S., Hisamatsu, Y., Jayaraman, T., Burkhoff, D., Rosemblit, N., & Marks, A. R. (2000) · Cell · doi:10.1016/s0092-8674(00)80847-8 · Cited by 1,978

Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP

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Interleukin-3-Induced Phosphorylation of BAD Through the Protein Kinase Akt

Peso, L. D., González-Garcı́a, M., Page, C., Herrera, R., & Nuñez, G. (1997) · Science · doi:10.1126/science.278.5338.687 · Cited by 1,797

14-3-3 Proteins: Structure, Function, and Regulation

Fu, H., Subramanian, R. R., & Masters, S. C. (2000) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.40.1.617 · Cited by 1,579

Inhibition of forskolin-induced neurite outgrowth and protein phosphorylation by a newly synthesized selective inhibitor of cyclic AMP-dependent protein kinase, N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H-89), of PC12D pheochromocytoma cells.

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Nuclear protein CBP is a coactivator for the transcription factor CREB

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A Family of cAMP-Binding Proteins That Directly Activate Rap1

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Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases

Kennelly, P. J., & Krebs, E. G. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98436-x · Cited by 1,339

Switching of the coupling of the β2-adrenergic receptor to different G proteins by protein kinase A

Daaka, Y., Luttrell, L. M., & Lefkowitz, R. J. (1997) · Nature · doi:10.1038/36362 · Cited by 1,270

Turning off the signal: desensitization of β‐adrenergic receptor function

Hausdorff, W. P., Caron, M. G., & Lefkowitz, R. J. (1990) · The FASEB Journal · doi:10.1096/fasebj.4.11.2165947 · Cited by 1,249

Phosphorylation of NF-κB p65 by PKA Stimulates Transcriptional Activity by Promoting a Novel Bivalent Interaction with the Coactivator CBP/p300

Zhong, H., Voll, R. E., & Ghosh, S. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80066-0 · Cited by 1,210

A cyclic nucleotide-gated conductance in olfactory receptor cilia

Nakamura, T., & Gold, G. H. (1987) · Nature · doi:10.1038/325442a0 · Cited by 1,146

cAMP-DEPENDENT PROTEIN KINASE: FRAMEWORK FOR A DIVERSE FAMILY OF REGULATORY ENZYMES

Taylor, S. S., Buechler, J. A., & Yonemoto, W. (1990) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.59.070190.004543 · Cited by 1,144

[3] Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations

Pearson, R. B., & Kemp, B. E. (1991) · Methods in Enzymology · doi:10.1016/0076-6879(91)00127-i · Cited by 1,035

Structure, Function, and Control of Phosphoinositide-Specific Phospholipase C

Rebecchi, M. J., & Pentyala, S. N. (2000) · Physiological Reviews · doi:10.1152/physrev.2000.80.4.1291 · Cited by 997

Regulation and modulation of calcium channels in cardiac, skeletal, and smooth muscle cells

McDonald, T. F., Pelzer, S., Trautwein, W., & Pelzer, D. J. (1994) · Physiological Reviews · doi:10.1152/physrev.1994.74.2.365 · Cited by 995

Glycosylation of Nucleocytoplasmic Proteins: Signal Transduction and O-GlcNAc

Wells, L., Vosseller, K., & Hart, G. W. (2001) · Science · doi:10.1126/science.1058714 · Cited by 954

Inhibition of the EGF-Activated MAP Kinase Signaling Pathway by Adenosine 3′,5′-Monophosphate

Wu, J., Dent, P., Jelinek, T., Wolfman, A., Weber, M. J., & Sturgill, T. W. (1993) · Science · doi:10.1126/science.7694366 · Cited by 919

On target with a new mechanism for the regulation of protein phosphorylation

Hubbard, M. J., & Cohen, P. (1993) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(93)90109-z · Cited by 903

A Cell's Sense of Direction

Parent, C. A., & Devreotes, P. N. (1999) · Science · doi:10.1126/science.284.5415.765 · Cited by 890

Direct activation of cardiac pacemaker channels by intracellular cyclic AMP

DiFrancesco, D., & Tortora, P. (1991) · Nature · doi:10.1038/351145a0 · Cited by 850

Cellular and Molecular Biology of the Aquaporin Water Channels

Borgnia, M., Nielsen, S., Engel, A., & Agre, P. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.425 · Cited by 846

TRANSCRIPTIONAL REGULATION BY cAMP AND ITS RECEPTOR PROTEIN

Kolb, A., Busby, S., Buc, H., Garges, S., & Adhya, S. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.003533 · Cited by 846

Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase.

Kemp, B. E., Graves, D. J., Benjamini, E., & Krebs, E. G. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40137-2 · Cited by 835

Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A

Fang, X., Yu, S. X., Lu, Y., Bast, R. C., Woodgett, J. R., & Mills, G. B. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.220413597 · Cited by 830

The Transcriptional Activity of NF-κB Is Regulated by the IκB-Associated PKAc Subunit through a Cyclic AMP–Independent Mechanism

Zhong, H., SuYang, H., Erdjument-Bromage, H., Tempst, P., & Ghosh, S. (1997) · Cell · doi:10.1016/s0092-8674(00)80222-6 · Cited by 827

Regulation of CREB Phosphorylation in the Suprachiasmatic Nucleus by Light and a Circadian Clock

Ginty, D. D., Kornhauser, J. M., Thompson, M. A., Bading, H., Mayo, K. E., Takahashi, J. S., & Greenberg, M. E. (1993) · Science · doi:10.1126/science.8097062 · Cited by 823

Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit

Roche, K. W., O'Brien, R. J., Mammen, A. L., Bernhardt, J., & Huganir, R. L. (1996) · Neuron · doi:10.1016/s0896-6273(00)80144-0 · Cited by 812

Transcription activation by catabolite activator protein (CAP)

Busby, S., & Ebright, R. H. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3161 · Cited by 800

Mechanisms of sodium pump regulation

Therien, A. G., & Blostein, R. (2000) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2000.279.3.c541 · Cited by 765

Steroidogenic factor 1: a key determinant of endocrine development and function

Parker, K. L., & Schimmer, B. P. (1997) · Endocrine Reviews · doi:10.1210/edrv.18.3.0301 · Cited by 764

Beyond the Dopamine Receptor

Greengard, P., Allen, P. B., & Nairn, A. C. (1999) · Neuron · doi:10.1016/s0896-6273(00)80798-9 · Cited by 746

Epithelial sodium channel regulated by aldosterone-induced protein sgk

Chen, S.-Y., Bhargava, A., Mastroberardino, L., Meijer, O. C., Wang, J., Buse, P., Firestone, G. L., Verrey, F., & Pearce, D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2514 · Cited by 734

Phosphorylation of Histone H3 Is Required for Proper Chromosome Condensation and Segregation

Wei, Y., Yu, L., Bowen, J., Gorovsky, M. A., & Allis, C. D. (1999) · Cell · doi:10.1016/s0092-8674(00)80718-7 · Cited by 718

Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation.

Luo, W., Grupp, I. L., Harrer, J., Ponniah, S., Grupp, G., Duffy, J. J., Doetschman, T., & Kranias, E. G. (1994) · Circulation Research · doi:10.1161/01.res.75.3.401 · Cited by 706

Serine/Threonine Protein Kinases and Apoptosis

Cross, T. G., Scheel-Toellner, D., Henriquez, N. V., Deacon, E., Salmon, M., & Lord, J. M. (2000) · Experimental Cell Research · doi:10.1006/excr.2000.4836 · Cited by 690

Studies on the Mechanism of Hormone Action

Sutherland, E. W. (1972) · Science · doi:10.1126/science.177.4047.401 · Cited by 687

Intricate Regulation of Tyrosine Hydroxylase Activity and Gene Expression

Kumer, S. C., & Vrana, K. E. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67020443.x · Cited by 679

Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel

Cheng, S. H., Rich, D. P., Marshall, J., Gregory, R. J., Welsh, M. J., & Smith, A. E. (1991) · Cell · doi:10.1016/0092-8674(91)90446-6 · Cited by 663

Use of an oriented peptide library to determine the optimal substrates of protein kinases

Songyang, Z., Blechner, S., Hoagland, N., Hoekstra, M. F., Piwnica-Worms, H., & Cantley, L. C. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00221-9 · Cited by 652

Phosphorylation and Inactivation of BAD by Mitochondria-Anchored Protein Kinase A

Harada, H., Becknell, B., Wilm, M., Mann, M., Huang, L. J.-S., Taylor, S. S., Scott, J. D., & Korsmeyer, S. J. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80469-4 · Cited by 645

DARPP-32, a dopamine-regulated neuronal phosphoprotein, is a potent inhibitor of protein phosphatase-1

Hemmings, H. C., Greengard, P., Tung, H. Y. L., & Cohen, P. (1984) · Nature · doi:10.1038/310503a0 · Cited by 614

Phospholamban: Protein Structure, Mechanism of Action, and Role in Cardiac Function

SIMMERMAN, H. K. B., & JONES, L. R. (1998) · Physiological Reviews · doi:10.1152/physrev.1998.78.4.921 · Cited by 574

Dedicated Myosin Light Chain Kinases with Diverse Cellular Functions

Kamm, K. E., & Stull, J. T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r000028200 · Cited by 572

The GAF domain: an evolutionary link between diverse phototransducing proteins

Aravind, L., & Ponting, C. P. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01148-1 · Cited by 570

Cyclic nucleotide phosphodiesterases: Relating structure and function

Francis, S. H., Turko, I. V., & Corbin, J. D. (2000) · Progress in Nucleic Acid Research and Molecular Biology · doi:10.1016/s0079-6603(00)65001-8 · Cited by 564

Molecular Mechanisms Regulating Hormone-Sensitive Lipase and Lipolysis

Holm, C., Østerlund, T., Laurell, H., & Contreras, J. A. (2000) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.20.1.365 · Cited by 564

Protein kinase A phosphorylation of RhoA mediates the morphological and functional effects of cyclic AMP in cytotoxic lymphocytes

Lang, P., Gesbert, F., Delespine‐Carmagnat, M., Stancou, R., Pouchelet, M., & Bertoglio, J. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00383.x · Cited by 558

RNA Helicase A Mediates Association of CBP with RNA Polymerase II

Nakajima, T., Uchida, C., Anderson, S. F., Lee, C.-G., Hurwitz, J., Parvin, J. D., & Montminy, M. (1997) · Cell · doi:10.1016/s0092-8674(00)80376-1 · Cited by 540

Synapsins as Regulators of Neurotransmitter Release

Hilfiker, S., Pieribone, V. A., Czernik, A. J., Kao, H.-T., Augustine, G. J., & Greengard, P. (1999) · Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences · doi:10.1098/rstb.1999.0378 · Cited by 537

Modulation of ION Channels by Protein Phosphorylation and Dephosphorylation

Levitan, I. B. (1994) · Annual Review of Physiology · doi:10.1146/annurev.ph.56.030194.001205 · Cited by 523

cAMP-Dependent Regulation of Cardiac L-Type Ca2+ Channels Requires Membrane Targeting of PKA and Phosphorylation of Channel Subunits

Gao, T., Yatani, A., Dell'Acqua, M. L., Sako, H., Green, S. A., Dascal, N., Scott, J. D., & Hosey, M. M. (1997) · Neuron · doi:10.1016/s0896-6273(00)80358-x · Cited by 519

General Anosmia Caused by a Targeted Disruption of the Mouse Olfactory Cyclic Nucleotide–Gated Cation Channel

Brunet, L. J., Gold, G. H., & Ngai, J. (1996) · Neuron · doi:10.1016/s0896-6273(00)80200-7 · Cited by 516

Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity

Witcher, D. R., Kovacs, R. J., Schulman, H., Cefali, D. C., & Jones, L. R. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99140-4 · Cited by 507

Defective smooth muscle regulation in cGMP kinase I-deficient mice

Pfeifer, A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.11.3045 · Cited by 497

Regulation of NMDA Receptors by an Associated Phosphatase-Kinase Signaling Complex

Westphal, R. S., Tavalin, S. J., Lin, J. W., Alto, N. M., Fraser, I. D. C., Langeberg, L. K., Sheng, M., & Scott, J. D. (1999) · Science · doi:10.1126/science.285.5424.93 · Cited by 496

Characterization of Protein Kinase A and Protein Kinase C Phosphorylation of the N-Methyl-D-aspartate Receptor NR1 Subunit Using Phosphorylation Site-specific Antibodies

Tingley, W. G., Ehlers, M. D., Kameyama, K., Doherty, C., Ptak, J. B., Riley, C. T., & Huganir, R. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.8.5157 · Cited by 495

Requirement of Rsk-2 for Epidermal Growth Factor-Activated Phosphorylation of Histone H3

Sassone-Corsi, P., Mizzen, C. A., Cheung, P., Crosio, C., Monaco, L., Jacquot, S., Hanauer, A., & Allis, C. D. (1999) · Science · doi:10.1126/science.285.5429.886 · Cited by 484

cAMP-GEFII is a direct target of cAMP in regulated exocytosis

Ozaki, N., Shibasaki, T., Kashima, Y., Miki, T., Takahashi, K., Ueno, H., Sunaga, Y., Yano, H., Matsuura, Y., Iwanaga, T., et al. (2000) · Nature Cell Biology · doi:10.1038/35041046 · Cited by 481

cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets.

Butt, E., Abel, K., Krieger, M., Palm, D., Hoppe, V., Hoppe, J., & Walter, U. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36652-8 · Cited by 468

Identification of Novel Phosphorylation Sites in Hormone-sensitive Lipase That Are Phosphorylated in Response to Isoproterenol and Govern Activation Properties in Vitro

Anthonsen, M. W., Rönnstrand, L., Wernstedt, C., Degerman, E., & Holm, C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.1.215 · Cited by 468

Targeting of PKA to Glutamate Receptors through a MAGUK-AKAP Complex

Colledge, M., Dean, R. A., Scott, G. K., Langeberg, L. K., Huganir, R. L., & Scott, J. D. (2000) · Neuron · doi:10.1016/s0896-6273(00)00013-1 · Cited by 467

An Apical PDZ Protein Anchors the Cystic Fibrosis Transmembrane Conductance Regulator to the Cytoskeleton

Short, D. B., Trotter, K. W., Reczek, D., Kreda, S. M., Bretscher, A., Boucher, R. C., Stutts, M. J., & Milgram, S. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.31.19797 · Cited by 467

Forskolin: a specific stimulator of adenylyl cyclase or a diterpene with multiple sites of action?

Laurenza, A., Sutkowski, E. M., & Seamon, K. B. (1989) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(89)80008-2 · Cited by 456

sgk Is an Aldosterone-induced Kinase in the Renal Collecting Duct

Náray-Fejes-Tóth, A., Canessa, C., Cleaveland, E. S., Aldrich, G., & Fejes-Tóth, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.24.16973 · Cited by 454

Coupling of hormonal stimulation and transcription via the cyclic AMP-responsive factor CREB is rate limited by nuclear entry of protein kinase A.

Hagiwara, M., Brindle, P., Harootunian, A., Armstrong, R., Rivier, J., Vale, W., Tsien, R., & Montminy, M. R. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.8.4852 · Cited by 453

The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase

Thomson, S. (1999) · The EMBO Journal · doi:10.1093/emboj/18.17.4779 · Cited by 450

Control of CFTR Channel Gating by Phosphorylation and Nucleotide Hydrolysis

GADSBY, D. C., & NAIRN, A. C. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.1.s77 · Cited by 443

The Multidrug Resistance Protein 5 Functions as an ATP-dependent Export Pump for Cyclic Nucleotides

Jedlitschky, G., Burchell, B., & Keppler, D. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005463200 · Cited by 442

Phosphorylation of the α-Amino-3-hydroxy-5-methylisoxazole4-propionic Acid Receptor GluR1 Subunit by Calcium/ Calmodulin-dependent Kinase II

Mammen, A. L., Kameyama, K., Roche, K. W., & Huganir, R. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.51.32528 · Cited by 441

Structure and Function of Cyclic Nucleotide-Dependent Protein Kinases

Francis, S. H., & Corbin, J. D. (1994) · Annual Review of Physiology · doi:10.1146/annurev.ph.56.030194.001321 · Cited by 440

Follicle-Stimulating Hormone (FSH) Stimulates Phosphorylation and Activation of Protein Kinase B (PKB/Akt) and Serum and Glucocorticoid-Induced Kinase (Sgk): Evidence for A Kinase-Independent Signaling by FSH in Granulosa Cells

González, I., Falender, A. E., Ochsner, S. A., Firestone, G. L., & Richards, J. S. (2000) · Molecular Endocrinology · doi:10.1210/me.14.8.1283 · Cited by 430

Structure, Localization, and Regulation of cGMP-inhibited Phosphodiesterase (PDE3)

Degerman, E., Belfrage, P., & Manganiello, V. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.11.6823 · Cited by 428

Bidirectional Regulation of DARPP-32 Phosphorylation by Dopamine

Nishi, A., Snyder, G. L., & Greengard, P. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-21-08147.1997 · Cited by 424

14-3-3 proteins: regulation of subcellular localization by molecular interference

MUSLIN, A. (2000) · Cellular Signalling · doi:10.1016/s0898-6568(00)00131-5 · Cited by 417

Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction?

Gautel, M., Zuffardi, O., Freiburg, A., & Labeit, S. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07187.x · Cited by 411

Phosphorylation and Activation of a cAMP-specific Phosphodiesterase by the cAMP-dependent Protein Kinase

Sette, C., & Conti, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.28.16526 · Cited by 409

Cloning and Characterization of a Novel Human Phosphodiesterase That Hydrolyzes Both cAMP and cGMP (PDE10A)

Fujishige, K., Kotera, J., Michibata, H., Yuasa, K., Takebayashi, S.-I., Okumura, K., & Omori, K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.26.18438 · Cited by 404

A C-terminal motif found in the β 2 -adrenergic receptor, P2Y1 receptor and cystic fibrosis transmembrane conductance regulator determines binding to the Na + /H + exchanger regulatory factor family of PDZ proteins

Hall, R. A., Ostedgaard, L. S., Premont, R. T., Blitzer, J. T., Rahman, N., Welsh, M. J., & Lefkowitz, R. J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.15.8496 · Cited by 404

Mechanism of Regulation of the Epac Family of cAMP-dependent RapGEFs

de Rooij, J., Rehmann, H., van Triest, M., Cool, R. H., Wittinghofer, A., & Bos, J. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001113200 · Cited by 398

Phosphorylation of troponin I and the inotropic effect of adrenaline in the perfused rabbit heart

SOLARO, R. J., MOIR, A. J. G., & PERRY, S. V. (1976) · Nature · doi:10.1038/262615a0 · Cited by 395

Phosphorylation of steroidogenic acute regulatory protein (StAR) modulates its steroidogenic activity

Arakane, F., King, S. R., Du, Y., Kallen, C. B., Walsh, L. P., Watari, H., Stocco, D. M., & Strauss, J. F. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.51.32656 · Cited by 391

Insulin-Induced Phosphorylation and Activation of Cyclic Nucleotide Phosphodiesterase 3B by the Serine-Threonine Kinase Akt

Kitamura, T., Kitamura, Y., Kuroda, S., Hino, Y., Ando, M., Kotani, K., Konishi, H., Matsuzaki, H., Kikkawa, U., Ogawa, W., et al. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.9.6286 · Cited by 376

Isolation and characterization of a dual-substrate phosphodiesterase gene family: PDE10A

Soderling, S. H., Bayuga, S. J., & Beavo, J. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.12.7071 · Cited by 374

Downregulation of Transient K+Channels in Dendrites of Hippocampal CA1 Pyramidal Neurons by Activation of PKA and PKC

Hoffman, D. A., & Johnston, D. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-10-03521.1998 · Cited by 373

Anchoring of protein kinase A is required for modulation of AMPA/kainate receptors on hippocampal neurons

Rosenmund, C., Carr, D. W., Bergeson, S. E., Nilaver, G., Scott, J. D., & Westbrook, G. L. (1994) · Nature · doi:10.1038/368853a0 · Cited by 371

New Signaling Pathways for Hormones and Cyclic Adenosine 3',5'-Monophosphate Action in Endocrine Cells

Richards, J. S. (2001) · Molecular Endocrinology · doi:10.1210/me.15.2.209 · Cited by 368

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Myosin light chain kinase phosphorylation in tracheal smooth muscle.

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The phosphorylation state of phosducin determines its ability to block transducin subunit interactions and inhibit transducin binding to activated rhodopsin.

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Phosphorylation of the pro-apoptotic protein BAD on serine 155, a novel site, contributes to cell survival

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Dopaminergic Modulation of Sodium Current in Hippocampal Neurons via cAMP-Dependent Phosphorylation of Specific Sites in the Sodium Channel α Subunit

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Untitled work

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Mutations in STRA6 Cause a Broad Spectrum of Malformations Including Anophthalmia, Congenital Heart Defects, Diaphragmatic Hernia, Alveolar Capillary Dysplasia, Lung Hypoplasia, and Mental Retardation

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Activation of PKA leads to mesenchymal-to-epithelial transition and loss of tumor-initiating ability

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The cAMP Pathway as Therapeutic Target in Autoimmune and Inflammatory Diseases

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Rapamycin decreases tau phosphorylation at Ser214 through regulation of cAMP-dependent kinase.

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