The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Autophosphorylation reversibly regulates the Ca2+/calmodulin-dependence of Ca2+/calmodulin-dependent protein kinase II.
Open accessAbstract
Ca2+/calmodulin-dependent protein kinase II contains two subunits, alpha (Mr 50,000) and beta (Mr 60,000/58,000), both of which undergo Ca2+/calmodulin-dependent autophosphorylation. In the present study, we have studied the mechanism of this autophosphorylation reaction and its effect on the activity of the enzyme. Both subunits are autophosphorylated through an intramolecular mechanism. Using synapsin I as substrate, Ca2+/calmodulin-dependent protein kinase II, in its unphosphorylated form, was totally dependent on Ca2+ and calmodulin for its activity. Preincubation of the enzyme with Ca2+, calmodulin, and ATP, under conditions where autophosphorylation of both subunits occurred, converted the enzyme to one that was only partially dependent on Ca2+ and calmodulin for its activity. No change in the total activity, measured in the presence of Ca2+ and calmodulin, was observed. The nonhydrolyzable ATP analog adenosine 5'-[beta, gamma-imido] triphosphate did not substitute for ATP in the preincubation. Moreover, dephosphorylation of autophosphorylated Ca2+/calmodulin-dependent protein kinase II with protein phosphatase 2A resulted in an enzyme that was again totally dependent on Ca2+ and calmodulin for its activity. We propose that autophosphorylation and dephosphorylation reversibly regulate the Ca2+ and calmodulin requirement of Ca2+/calmodulin-dependent protein kinase II.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“it was not until the discovery of a Ca2+/calmodulin-dependent protein kinase, now referred to as CaMKII (9, 10), which became independent of Ca2+ (autonomous) after autophosphorylation (11–15)”
From Synaptic memory and CaMKII (2023) · cites this paper as [13]
In the citing paper
“Fourth, CaMKII has the intriguing property that once activated by Ca2+ the enzymatic activity toward substrates remains after Ca2+ removal (11–15).”
From Synaptic memory and CaMKII (2023) · cites this paper as [13]
In the citing paper
“A further complication for either of these possibilities is that it appears that the subunit being phosphorylated apparently would need to have Ca2+/CaM bound, i.e., it does not significantly occur on inactive subunits (13, 15, 82, 83, 406).”
From Synaptic memory and CaMKII (2023) · cites this paper as [13]
Citations
Cites
A simplification of the protein assay method of Lowry et al. which is more generally applicable
Peterson, G. L. (1977) · Analytical Biochemistry · doi:10.1016/0003-2697(77)90043-4 · Cited by 8,531
Calmodulin Plays a Pivotal Role in Cellular Regulation
Cheung, W. Y. (1980) · Science · doi:10.1126/science.6243188 · Cited by 2,434
Miller, S. (1986) · Cell · doi:10.1016/0092-8674(86)90008-5 · Cited by 864
Llinas, R. H., McGuinness, T. L., Leonard, C. S., Sugimori, M., & Greengard, P. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.9.3035 · Cited by 641
Self-citationNaira, A. C., Hemmings, H. C., & Greengard, P. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.004435 · Cited by 551
Self-citationPhosphorylation activates the insulin receptor tyrosine protein kinase.
Rosen, O. M., Herrera, R., Olowe, Y., Petruzzelli, L., & Cobb, M. H. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.11.3237 · Cited by 545
Bennett, M. K., Erondu, N. E., & Kennedy, M. B. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44239-6 · Cited by 481
Ueda, T., & Greengard, P. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40170-0 · Cited by 407
Self-citationGoldenring, J. R., Gonzalez, B. I., McGuire, J. S., & DeLorenzo, R. J. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44223-2 · Cited by 339
Miller, S. G., & Kennedy, M. B. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39454-1 · Cited by 304
Flagged first, then by citations
Cited by
Sorted by citations
Items 101–200 of 292
Applications of quantitative measurements for assessing glutamate neurotoxicity.
Finkbeiner, S. M., & Stevens, C. F. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.4071 · Cited by 80
Calcium‐dependent serine phosphorylation of synaptophysin
Rubenstein, J. L., Greengard, P., & Czernik, A. J. (1993) · Synapse · doi:10.1002/syn.890130207 · Cited by 79
Self-citationCoppini, R., Ferrantini, C., Mugelli, A., Poggesi, C., & Cerbai, E. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01391 · Cited by 78
Inhibition of Ca2+/calmodulin-dependent protein kinase II by arachidonic acid and its metabolites.
Piomelli, D., Wang, J. K., Sihra, T. S., Nairn, A. C., Czernik, A. J., & Greengard, P. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.21.8550 · Cited by 78
Self-citationHudmon, A., Aronowski, J., Kolb, S. J., & Waxham, M. N. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.15.8800 · Cited by 76
Kwiatkowski, A. P., & King, M. M. (1989) · Biochemistry · doi:10.1021/bi00439a010 · Cited by 76
Mullasseril, P., Döṣemeci, A., Lisman, J. E., & Griffith, L. C. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04744.x · Cited by 75
Bradshaw, J. M., Hudmon, A., & Schulman, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202154200 · Cited by 78
A novel Ca2+-dependent protein kinase from Paramecium tetraurelia.
Gundersen, R. E., & Nelson, D. L. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61236-0 · Cited by 72
Regulation and role of brain calcium/calmodulin-dependent protein kinase II.
Colbran, R. (1992) · Neurochemistry International · doi:10.1016/0197-0186(92)90080-b · Cited by 83
Shani, G., Henis‐Korenblit, S., Jona, G., Gileadi, O., Eisenstein, M., Ziv, T., Admon, A., & Kimchi, A. (2001) · The EMBO Journal · doi:10.1093/emboj/20.5.1099 · Cited by 71
Stabilization of Calmodulin-dependent Protein Kinase II through the Autoinhibitory Domain (*)
Ishida, A., & Fujisawa, H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.5.2163 · Cited by 77
Shioda, N., Beppu, H., Fukuda, T., Li, E., Kitajima, I., & Fukunaga, K. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.4816-10.2011 · Cited by 69
Calmodulin and STIM proteins: Two major calcium sensors in the cytoplasm and endoplasmic reticulum
Marshall, C. B., Nishikawa, T., Osawa, M., Stathopulos, P. B., & Ikura, M. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.01.106 · Cited by 64
Yamamoto, S., Tanaka, E., & Higashi, H. (1997) · Journal of Neurophysiology · doi:10.1152/jn.1997.77.1.386 · Cited by 67
The role of autophosphorylation in activation of the type II calmodulin-dependent protein kinase.
Kwiatkowski, A. P., Shell, D. J., & King, M. M. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68667-3 · Cited by 67
A Biochemical Blueprint for Long-Term MemoryPreprint
Roberson, E. D., & Sweatt, J. D. (1999) · Learning & Memory · doi:10.1101/lm.6.4.381 · Cited by 67
Localization of synapsin I at the frog neuromuscular junction
Valtorta, F., Villa, A., Jahn, R., Camilli, P. V. D., Greengard, P., & Ceccarelli, B. (1988) · Neuroscience · doi:10.1016/0306-4522(88)90353-3 · Cited by 66
Self-citationRegulation of type-II calmodulin kinase: functional implications.
Bronstein, J., Farber, D., & Wasterlain, C. (1993) · Brain research. Brain research reviews · doi:10.1016/0165-0173(93)90011-n · Cited by 72
Developmental Regulation of Potassium Channels and the Impact on Neuronal Differentiation
Ribera, A. B., & Spitzer, N. C. (1992) · Springer eBooks · doi:10.1007/978-1-4615-3328-3_1 · Cited by 65
Yao, J. (2006) · Journal of Clinical Investigation · doi:10.1172/jci27918 · Cited by 63
Kennedy, M. B., Bennett, M. K., Bulleit, R. F., Erondu, N., Jennings, V., Miller, S. G., Molloy, S. S., Patton, B. L., & Schenker, L. J. (1990) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1990.055.01.013 · Cited by 63
Sahyoun, N. E., McDonald, O. B., Farrell, F. X., & Lapetina, E. G. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.7.2643 · Cited by 60
Waxham, M. N., Aronowski, J. A., Westgate, S. A., & Kelly, P. T. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.4.1273 · Cited by 60
CaMKII Measures the Passage of Time to Coordinate Behavior and Motivational State
Thornquist, S. C., Langer, K., Zhang, S. X., Rogulja, D., & Crickmore, M. A. (2019) · Neuron · doi:10.1016/j.neuron.2019.10.018 · Cited by 56
Hirata, Y., Takahashi, M., Kudoh, Y., Kano, K., Kawana, H., Makide, K., Shinoda, Y., Yabuki, Y., Fukunaga, K., Aoki, J., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.771519 · Cited by 60
Flexible linkers in CaMKII control the balance between activating and inhibitory autophosphorylation
Bhattacharyya, M., Lee, Y. K., Muratcioglu, S., Qiu, B., Nyayapati, P., Schulman, H., Groves, J. T., & Kuriyan, J. (2020) · eLife · doi:10.7554/elife.53670 · Cited by 58
Potassium ion stimulation triggers protein translation in synaptoneurosomal polyribosomes
Weiler, I. J., & Greenough, W. T. (1991) · Molecular and Cellular Neuroscience · doi:10.1016/1044-7431(91)90060-2 · Cited by 58
Activation of multifunctional Ca2+/calmodulin-dependent protein kinase in GH3 cells
Jefferson, A. B., Travis, S. M., & Schulman, H. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52320-6 · Cited by 58
Ishida, A., Shigeri, Y., Taniguchi, T., & Kameshita, I. (2003) · Pharmacology and Therapeutics · doi:10.1016/j.pharmthera.2003.09.003 · Cited by 52
Ohta, Y., Ohba, T., Fukunaga, K., & Miyamoto, E. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37992-4 · Cited by 57
Calcium/Calmodulin–Dependent Protein Kinase II in Cerebrovascular Diseases
Zhang, X., Connelly, J. A., Levitan, E. S., Sun, D., & Wang, Q. J. (2021) · Translational Stroke Research · doi:10.1007/s12975-021-00901-9 · Cited by 55
Weber, P. C., Lukas, T. J., Craig, T. A., Wilson, E., King, M. M., Kwiatkowski, A. P., & Watterson, D. M. (1989) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340060107 · Cited by 55
Conformational changes underlying calcium/calmodulin‐dependent protein kinase II activation
Hoffman, L., Stein, R. A., Colbran, R. J., & Mchaourab, H. S. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.40 · Cited by 54
Ashpole, N. M., Chawla, A., Martin, M. P., Brustovetsky, T., Brustovetsky, N., & Hudmon, A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.466235 · Cited by 52
Cramer, N., & Galdzicki, Z. (2012) · Neural Plasticity · doi:10.1155/2012/101542 · Cited by 60
Neuronal L-Type Calcium Channel Signaling to the Nucleus Requires a Novel CaMKIIα-Shank3 Interaction
Perfitt, T. L., Wang, X., Dickerson, M. T., Stephenson, J. R., Nakagawa, T., Jacobson, D. A., & Colbran, R. J. (2020) · The Journal of Neuroscience · doi:10.1523/jneurosci.0893-19.2020 · Cited by 54
Mechanism of the Generation of Autonomous Activity of Ca2+/Calmodulin-dependent Protein Kinase IV
Tokumitsu, H., Hatano, N., Inuzuka, H., Yokokura, S., Nozaki, N., & Kobayashi, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406534200 · Cited by 54
Miller, C. A., & Sweatt, J. D. (2006) · Learning & Memory · doi:10.1101/lm.304606 · Cited by 53
Churn, S. B., Taft, W. C., Billingsley, M. S., Sankaran, B., & DeLorenzo, R. J. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb08431.x · Cited by 53
Engholm‐Keller, K., Waardenberg, A. J., Müller, J. A., Wark, J. R., Fernando, R. N., Arthur, J. W., Robinson, P. J., Dietrich, D., Schoch, S., & Graham, M. E. (2019) · PLoS Biology · doi:10.1371/journal.pbio.3000170 · Cited by 51
Intracellular signals that mediate thymic negative selection
Vasquez, N. J., Kane, L., & Hedrick, S. Μ. (1994) · Immunity · doi:10.1016/1074-7613(94)90008-6 · Cited by 52
Ikeda, A., Okuno, S., & Fujisawa, H. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98996-9 · Cited by 51
Yamagata, Y., Jovanovic, J. N., Czernik, A. J., Greengard, P., & Obata, K. (2002) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2001.00753.x · Cited by 49
Self-citationLickteig, R. L., Shenolikar, S., Denner, L. A., & Kelly, P. T. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37414-3 · Cited by 48
Enzymatic Gating of Voltage‐Activated Calcium Channels
Armstrong, D. L., Rossier, M. F., Shcherbatko, A., & White, R. E. (1991) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1991.tb36478.x · Cited by 47
DeRemer, M., Saeli, R. J., Brautigan, D. L., & Edelman, A. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42235-1 · Cited by 47
Yamagata, Y. (2003) · Journal of Pharmacological Sciences · doi:10.1254/jphs.93.22 · Cited by 46
Autophosphorylation-Dependent Activation of a Calcium-Dependent Protein Kinase from Groundnut1
Chaudhuri, S., Seal, A., & DasGupta, M. (1999) · PLANT PHYSIOLOGY · doi:10.1104/pp.120.3.859 · Cited by 46
Yoshimura, Y., & Yamauchi, T. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.42.26354 · Cited by 46
Frangakis, M. V., Ohmstede, C. A., & Sahyoun, N. E. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99164-7 · Cited by 46
Two Developmentally Regulated Isoenzymes of Calmodulin‐Stimulated Protein Kinase II in Rat Forebrain
Rostas, J. A. P., Seccombe, M. A., & Weinberger, R. P. (1988) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1988.tb03003.x · Cited by 46
LeVine, H., & Sahyoun, N. E. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb13442.x · Cited by 46
Maier, L. S. (2005) · Brazilian Journal of Medical and Biological Research · doi:10.1590/s0100-879x2005000900002 · Cited by 45
Menegon, A., Verderio, C., Leoni, C., Benfenati, F., Czernik, A. J., Greengard, P., Matteoli, M., & Valtorta, F. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-16-07016.2002 · Cited by 44
Self-citationCellular and molecular pathways controlling muscle size in response to exercise
Attwaters, M., & Hughes, S. M. (2021) · FEBS Journal · doi:10.1111/febs.15820 · Cited by 47
Seeger, C., Talibov, V., & Danielson, U. H. (2017) · Journal of Molecular Recognition · doi:10.1002/jmr.2621 · Cited by 44
Magupalli, V. G., Mochida, S., Yan, J., Jiang, X. J., Westenbroek, R. E., Nairn, A. C., Scheuer, T., & Catterall, W. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.369058 · Cited by 43
Self-citationShen, K., & Meyer, T. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70010096.x · Cited by 43
Yamagata, Y., Czernik, A. J., & Greengard, P. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98628-x · Cited by 43
Self-citationZhao, Y., Franklin, R. M., & Kappes, B. (1994) · Molecular and Biochemical Parasitology · doi:10.1016/0166-6851(94)90159-7 · Cited by 42
Kasahara, J., Fukunaga, K., & Miyamoto, E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.13.9061 · Cited by 42
Kindling induced changes in calmodulin kinase II immunoreactivity
Bronstein, J. M., Farber, D. B., Micevych, P. E., Lasher, R. S., & Wasterlain, C. G. (1990) · Brain Research · doi:10.1016/0006-8993(90)90490-3 · Cited by 42
Saccharomyces cerevisiae protein kinase dependent on Ca2+ and calmodulin
Miyakawa, T., Oka, Y., Tsuchiya, E., & Fukui, S. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.3.1417-1422.1989 · Cited by 42
Activation of a Calcium-Calmodulin-dependent Protein Kinase I Cascade in PC12 Cells
Aletta, J. M., Selbert, M. A., Nairn, A. C., & Edelman, A. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20930 · Cited by 41
Self-citationRood, R. P., Emmer, E., Wesolek, J. H., McCullen, J., Husain, Z., Cohen, M. E., Braithwaite, R. S., Murer, H., Sharp, G. W. G., & Donowitz, M. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113665 · Cited by 41
Protein Kinase C and its Role in Cell Growth
Woodgett, J. R., Hunter, T. R., & Gould, K. L. (1987) · Springer eBooks · doi:10.1007/978-1-4613-1915-3_6 · Cited by 41
Okamoto, H., & Ichikawa, K. (2000) · Biological Cybernetics · doi:10.1007/pl00007960 · Cited by 41
Wang, D., Surratt, C. K., & Sadée, W. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750763.x · Cited by 40
A Retinal Calmodulin‐Dependent Kinase: Calcium/ Calmodulin‐Stimulated and ‐Inhibited States
Bronstein, J. M., Wasterlain, C. G., & Farber, D. B. (1988) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1988.tb03028.x · Cited by 40
Nygârd, O., Nilsson, A., Carlberg, U., Nilsson, L., & Amons, R. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55316-3 · Cited by 40
Cerebellar GABA B receptors modulate function of GABA A receptors
Hahner, L., McQuilkin, S. J., & Harris, R. A. (1991) · The FASEB Journal · doi:10.1096/fasebj.5.10.1648524 · Cited by 39
Saitoh, Y., Yamamoto, H., Fukunaga, K., Matsukado, Y., & Miyamoto, E. (1987) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1987.tb10022.x · Cited by 39
α‐Synuclein involvement in hippocampal synaptic plasticity: role of NO, cGMP, cGK and CaMKII
Liu, S., Fà, M., Ninan, I., Trinchese, F., Dauer, W. T., & Arancio, O. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05569.x · Cited by 38
Rich, D. P., Colbran, R. J., Schworer, C. M., & Soderling, T. R. (1989) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1989.tb11777.x · Cited by 37
Churn, S. B., Yaghmai, A. A., Povlishock, J. T., Rafiq, A., & DeLorenzo, R. J. (1992) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.1992.109 · Cited by 37
Control Sites of Ribosomal S6 Kinase B and Persistent Activation through Tumor Necrosis Factor
Tomás-Zuber, M., Mary, J., & Lesslauer, W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002586200 · Cited by 34
Kwiatkowski, A. P., Huang, C., & King, M. M. (1990) · Biochemistry · doi:10.1021/bi00453a019 · Cited by 34
Phosphorylation and dephosphorylation of protein in regulating cellular function
Kurosawa, M. (1994) · Journal of Pharmacological and Toxicological Methods · doi:10.1016/1056-8719(94)90075-2 · Cited by 33
Calmodulin-Regulated Protein Kinases
Lukas, T. J., Mirzoeva, S., & Watterson, D. M. (1998) · Elsevier eBooks · doi:10.1016/b978-0-08-092636-0.50007-4 · Cited by 33
Autoactivation of calmodulin-dependent protein kinase II by autophosphorylation.
Katoh, T., & Fujisawa, H. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)49951-6 · Cited by 32
Lapadula, E. S., Lapadula, D. M., & Abou-Donia, M. B. (1992) · Neurochemistry International · doi:10.1016/0197-0186(92)90174-p · Cited by 31
Wang, X., Takata, T., Bai, X., Ou, F., Yokono, K., & Sakurai, T. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-101869 · Cited by 29
Li, H., & Aluko, R. E. (2005) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2005.05.007 · Cited by 29
Benfenati, F., Onofri, F., Czernik, A. J., & Valtorta, F. (1996) · Molecular Brain Research · doi:10.1016/0169-328x(96)00053-8 · Cited by 29
Role of calcium/calmodulin-dependent kinase 2 in neurodevelopmental disorders
Onori, M. P., & van Woerden, G. M. (2021) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2021.03.014 · Cited by 30
Hagiwara, T., Ohsako, S., & Yamauchi, T. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55312-6 · Cited by 28
Effects of some metal‐ATP complexes on Na(+)‐Ca2+ exchange in internally dialysed squid axons.
DiPolo, R., & Beaugé, L. (1993) · The Journal of Physiology · doi:10.1113/jphysiol.1993.sp019544 · Cited by 28
Ca2+/Calmodulin-Dependent Protein Kinase II (CaMKII) in the Heart
Maier, L. S. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2888-2_30 · Cited by 27
Functional analysis of Ca2+/calmodulin-dependent protein kinase II expressed in bacteria
Waxham, M. N., Aronowski, J. A., & Kelly, P. T. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83259-8 · Cited by 27
Kohanski, R. A. (1993) · Biochemistry · doi:10.1021/bi00073a007 · Cited by 27
King, M. M. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68848-9 · Cited by 27
Intracellular Regulation of GABAA-Receptor Function
Stelzer, A. (1992) · Springer eBooks · doi:10.1007/978-1-4615-3328-3_4 · Cited by 26
Cimino, M., Benfenati, F., Farabegoli, C., Cattabeni, F., Fuxé, K., Agnati, L. F., & Toffano, G. (1987) · Acta Physiologica Scandinavica · doi:10.1111/j.1748-1716.1987.tb08143.x · Cited by 27
Alterations of CaMKII after hypoxia‐ischemia during brain development
Tang, K., Liu, C., Kuluz, J. W., & Hu, B. R. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02733.x · Cited by 26
Singleton, M. W., Holbert, W. H., Lee, A. T., Bracey, J. M., & Churn, S. B. (2005) · Epilepsia · doi:10.1111/j.1528-1167.2005.19205.x · Cited by 26
Døskeland, A. P., Vintermyr, O. K., Flatmark, T., Cotton, R. G. H., & Døskeland, S. O. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb16913.x · Cited by 26
Saitoh, Y., Yamamoto, H., Ushio, Y., & Miyamoto, E. (1989) · Brain Research · doi:10.1016/0006-8993(89)90862-7 · Cited by 26
Intracellular Calcium and Cell Function
Villereal, M. L., & Palfrey, H. C. (1989) · Annual Review of Nutrition · doi:10.1146/annurev.nu.09.070189.002023 · Cited by 25
Localization of mRNA for protein phosphatase 2A in the brain of adult rats
Abe, H., Shima, H., Sekiguchi, M., Guo, H., Nagao, M., Tamura, S., & Kondo, H. (1994) · Molecular Brain Research · doi:10.1016/0169-328x(94)90041-8 · Cited by 25
Metadata
- Authors
- Lai, Y., Nairn, A. C., & Greengard, P.
- Affiliations
- Rockefeller University (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1986-06
- Volume
- 83
- Issue
- 12
- Pages
- 4253-4257
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC323710
- OpenAlex
- W2011962611
- Cited by
- 292
- References
- 33
- Citations by year
- 2026: 1 · 2025: 5 · 2023: 4 · 2022: 2 · 2021: 4 · 2020: 4 · 2019: 5 · 2018: 1 · 2017: 2 · 2016: 2 · 2015: 2 · 2014: 2 · 2013: 5 · 2012: 6
- FWCI
- 10.93
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- calcium/calmodulin-dependent protein kinase II, autophosphorylation, kinase regulation, synapsin I, protein phosphatase 2A, dephosphorylation, ATP requirement, enzyme activation
- MeSH terms
- Adenosine Triphosphate, Animals, Calcium, Calmodulin, Enzyme Activation, Hot Temperature, Kinetics, Phosphoprotein Phosphatases, Phosphorylation, Protein Kinases, Structure-Activity Relationship, Rats, Protein Phosphatase 2
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review