Critical amino acid residues of AIP, a highly specific inhibitory peptide of calmodulin‐dependent protein kinase II
Open accessAbstract
The importance of the individual amino acid residues of AIP (KKALRRQEAVDAL), a highly specific inhibitor of calmodulin‐dependent protein kinase II (CaMKII), was studied. Replacement of Arg 6, Gln 7, or Ala 9 by other amino acid residues produced a marked increase in the IC 50 value. Leu 4 and Val 10 were also sensitive to replacement, but some hydrophobic amino acids could substitute for these residues. Although replacement of Ala 3, Glu 8, Ala 12, and Leu 13 by other residues produced no significant increase in the IC 50, the substitution of Lys for Ala 3 decreased the IC 50. An AIP analog (KK LRRQEA DAY), in which Ala 3 and Val 10 were replaced with Lys and Phe, respectively, showed an IC 50 value as low as 4 nM, suggesting that it is a useful tool for studying the physiological roles of CaMKII.
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CaMKIINtides inhibit kinase activity with high affinity by binding across the entire substrate binding site and therefore also block GluN2B binding.
“They inhibit kinase activity with high affinity by binding across the entire substrate binding site (FIGURE 2B7) (61, 147, 153), and therefore also block GluN2B binding (152, 154).”
From Synaptic memory and CaMKII (2023) · cites this paper as [147]
The Results and discussion report that AIP potently inhibits CaMKII and binds a substrate-binding site. The paper studies AIP, not CaMKIINtides, and does not establish binding across the entire substrate-binding site. The citing sentence attaches different references to the GluN2B claim, so that part is not attributed to this source. (LLM, conf=0.84)
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PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 315,771 · see citing works
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961 · see citing works
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 · see citing works
The Multifunctional Calcium/Calmodulin-Dependent Protein Kinase: From Form to Function
Braun, A. P., & Schulman, H. (1995) · Annual Review of Physiology · doi:10.1146/annurev.ph.57.030195.002221 · Cited by 820 · see citing works
[17] The kinetics of reversible tight-binding inhibition
Williams, J. W., & Morrison, J. F. (1979) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(79)63019-7 · Cited by 693 · see citing works
Songyang, Z., Lu, K. P., Kwon, Y. T., Tsai, L., Filhol, O., Cochet, C., Brickey, D. A., Soderling, T. R., Bartleson, C., Graves, D. J., et al. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.11.6486 · Cited by 550 · see citing works
Hanson, P. I., Kapiloff, M. S., Lou, L. L., Rosenfeld, M. G., & Schulman, H. (1989) · Neuron · doi:10.1016/0896-6273(89)90115-3 · Cited by 290 · see citing works
A Novel Highly Specific and Potent Inhibitor of Calmodulin-Dependent Protein Kinase II
Ishida, A., Kameshita, I., Okuno, S., Kitani, T., & Fujisawa, H. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.2040 · Cited by 289 · see citing works
Self-citationOtmakhov, N., Griffith, L. C., & Lisman, J. E. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-14-05357.1997 · Cited by 207 · see citing works
Isolation and characterization of two distinct forms of protein kinase C.
Woodgett, J. R., & Hunter, T. R. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61272-4 · Cited by 191 · see citing works
Hashimoto, Y., & Soderling, T. R. (1987) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(87)90048-8 · Cited by 175 · see citing works
Learning mechanisms: the case for CaM-KII
Lisman, J., Malenka, R. C., Nicoll, R. A., & Malinow, R. (1997) · Science · doi:10.1126/science.276.5321.2001 · Cited by 147 · see citing works
Takasawa, S., Ishida, A., Nata, K., Nakagawa, K., Noguchi, N., Tohgo, A., Kato, I., Yonekura, H., Fujisawa, H., & Okamoto, H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.51.30257 · Cited by 106 · see citing works
Self-citationStabilization 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 70 · see citing works
Self-citationCalcium/Calmodulin‐Dependent Kinase II Phosphorylates Drosophila Visual Arrestin
Kahn, E. S., & Matsumoto, H. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68010169.x · Cited by 65 · see citing works
Structure and regulation of calcium/calmodulin-dependent protein kinases II and IV
Soderling, T. R. (1996) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(96)00105-7 · Cited by 59 · see citing works
Hayashi, Y., Ishida, A., Katagiri, H., Mishina, M., Fujisawa, H., Manabe, T., & Takahashi, T. (1997) · Brain Research. Molecular Brain Research · doi:10.1016/s0169-328x(97)00073-9 · Cited by 40 · see citing works
Self-citationFernandez, A. (1991) · Experimental Cell Research · doi:10.1016/0014-4827(91)90398-e · Cited by 32 · see citing works
Calmodulin‐dependent protein kinase II
Fujisawa, H. (1990) · BioEssays · doi:10.1002/bies.950120106 · Cited by 27 · see citing works
Self-citationOkuno, S., & Fujisawa, H. (1990) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(90)90206-u · Cited by 26 · see citing works
Self-citationInactivation of Ca2+/Calmodulin-Dependent Protein Kinase II by Ca2+/Calmodulin1
Ishida, A., Kitani, T., Okuno, S., & Fujisawa, H. (1994) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a124460 · Cited by 25 · see citing works
Self-citationAcylation of the Group in Neuropeptide Y(12-36) Increases Binding Affinity for the Y2 Receptor
Murase, S., Yumoto, N., Petukhov, M., & Yoshikawa, S. (1996) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a021213 · Cited by 16 · see citing works
Self-citationKameshita, I., & Fujisawa, H. (1995) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a124726 · Cited by 9 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Structure–function of the multifunctional Ca2+/calmodulin-dependent protein kinase II
HUDMON, A., & SCHULMAN, H. (2002) · Biochemical Journal · doi:10.1042/bj20020228 · Cited by 615 · see citing works
CaMKII: a central molecular organizer of synaptic plasticity, learning and memory
Yasuda, R., Hayashi, Y., & Hell, J. W. (2022) · Nature Reviews Neuroscience · doi:10.1038/s41583-022-00624-2 · Cited by 431 · see citing works
Timmins, J. M., Özcan, L., Seimon, T. A., Li, G., Malagelada, C., Backs, J., Backs, T., Bassel‐Duby, R., Olson, E. N., Anderson, M. E., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38857 · Cited by 422 · see citing works
Zha, X., Wemmie, J. A., Green, S. H., & Welsh, M. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608018103 · Cited by 189 · see citing works
Regulation of Human CLC-3 Channels by Multifunctional Ca2+/Calmodulin-dependent Protein Kinase
Huang, P., Liu, J., Di, A., Robinson, N. C., Musch, M. W., Kaetzel, M. A., & Nelson, D. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009376200 · Cited by 149 · see citing works
Murakoshi, H., Shin, M. E., Parra-Bueno, P., Szatmari, E. M., Shibata, A. C. E., & Yasuda, R. (2017) · Neuron · doi:10.1016/j.neuron.2017.02.036 · Cited by 140 · see citing works
Lim, W.-S., Timmins, J. M., Seimon, T. A., Sadler, A. J., Kolodgie, F. D., Virmani, R., & Tabas, I. A. (2008) · Circulation · doi:10.1161/circulationaha.107.711275 · Cited by 141 · see citing works
Nicoll, R. A., & Schulman, H. (2023) · Physiological Reviews · doi:10.1152/physrev.00034.2022 · Cited by 126 · see citing works
“They inhibit kinase activity with high af fi nity by binding across the entire substrate binding site ( FIGURE 2 B7 ) (61, 147, 153), and therefore also block GluN2B binding (152, 154).”
BackgroundHardingham, N. R., & Fox, K. D. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.0652-06.2006 · Cited by 123 · see citing works
Ca2+/Calmodulin-dependent Protein Kinase II Is Required for Microcystin-induced Apoptosis
Fladmark, K. E., Brustugun, O. T., Mellgren, G., Krakstad, C., Bøe, R., Vintermyr, O. K., Schulman, H., & Døskeland, S. O. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109049200 · Cited by 117 · see citing works
Lactococcin Q, a Novel Two-Peptide Bacteriocin Produced by Lactococcus lactis QU 4
Zendo, T., Koga, S., Shigeri, Y., Nakayama, J., & Sonomoto, K. (2006) · Applied and Environmental Microbiology · doi:10.1128/aem.72.5.3383-3389.2006 · Cited by 103 · see citing works
Self-citationMemory Erasure Experiments Indicate a Critical Role of CaMKII in Memory Storage
Rossetti, T., Banerjee, S., Kim, C., Leubner, M., Lamar, C., Gupta, P., Lee, B., Neve, R., & Lisman, J. (2017) · Neuron · doi:10.1016/j.neuron.2017.09.010 · Cited by 94 · see citing works
Synthesis and application of caged peptides and proteins
Shigeri, Y., Tatsu, Y., & Yumoto, N. (2001) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(01)00148-6 · Cited by 81 · see citing works
Self-citationJemil, I., Mora, L., Nasri, R., Abdelhedi, O., Aristoy, M., Hajji, M., Nasri, M., & Toldrá, F. (2016) · Food Research International · doi:10.1016/j.foodres.2016.08.020 · Cited by 80 · see citing works
Bok, J., Wang, Q., Huang, J., & Green, S. H. (2007) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2007.05.008 · Cited by 79 · see citing works
Zhu, L., Almaça, J., Dadi, P., Hong, H., Sakamoto, W., Rossi, M., Lee, R. J., Vierra, N., Lu, H.-Y., Cui, Y.-H., et al. (2017) · Nature Communications · doi:10.1038/ncomms14295 · Cited by 82 · see citing works
Robinson, N. C., Huang, P., Kaetzel, M. A., Lamb, F. S., & Nelson, D. J. (2004) · The Journal of Physiology · doi:10.1113/jphysiol.2003.058032 · Cited by 69 · see citing works
Spehr, J., Hagendorf, S., Weiss, J., Spehr, M., Leinders‐Zufall, T., & Zufall, F. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.5416-08.2009 · Cited by 70 · see citing works
Synaptic memory requires CaMKII
Tao, W., Lee, J., Chen, X., Díaz-Alonso, J., Zhou, J., Pleasure, S., & Nicoll, R. A. (2021) · eLife · doi:10.7554/elife.60360 · Cited by 72 · see citing works
Colinas, O., Gallego, M., Setién, R., López‐López, J. R., Pérez-García, M. T., & Casis, Ó. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01373.2005 · Cited by 61 · see citing works
CaMKII binds both substrates and activators at the active site
Özden, C., Sloutsky, R., Mitsugi, T., Santos, N., Agnello, E., Gaubitz, C., Foster, J., Lapinskas, E., Esposito, E. A., Saneyoshi, T., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111064 · Cited by 61 · see citing works
Barr, R. K., Boehm, I., Attwood, P. V., Watt, P. M., & Bogoyevitch, M. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402181200 · Cited by 61 · see citing works
Ishida, A., Shigeri, Y., Taniguchi, T., & Kameshita, I. (2003) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2003.09.003 · Cited by 56 · see citing works
Self-citationKan, M.-C., Oruganty-Das, A., Cooper-Morgan, A., Jin, G., Swanger, S. A., Bassell, G. J., Florman, H. M., van Leyen, K., & Richter, J. D. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00716-10 · Cited by 53 · see citing works
Hardingham, N. R., Wright, N. F., Dachtler, J., & Fox, K. D. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.018 · Cited by 48 · see citing works
Characterization of apoptosis-genes associated with NMDA mediated cell death in the adult rat retina
Laabich, A., Li, G., & Cooper, N. G. F. (2001) · Molecular Brain Research · doi:10.1016/s0169-328x(01)00116-4 · Cited by 47 · see citing works
Ackermann, F., Zitranski, N., Borth, H., Buech, T. R. H., Gudermann, T. W., & Boekhoff, I. (2009) · Journal of Cell Science · doi:10.1242/jcs.058263 · Cited by 44 · see citing works
Distinct phosphorylation states of mammalian CaMKIIβ control the induction and maintenance of sleep
Tone, D., Ode, K. L., Zhang, Q., Fujishima, H., Yamada, R. G., Nagashima, Y., Matsumoto, K., Wen, Z., Yoshida, S. Y., Mitani, T. T., et al. (2022) · PLoS Biology · doi:10.1371/journal.pbio.3001813 · Cited by 42 · see citing works
Phillips, K. G., Hardingham, N. R., & Fox, K. D. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.3984-08.2008 · Cited by 43 · see citing works
Jung, S., Reed, B. J., & Sweet, I. R. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00282.2009 · Cited by 43 · see citing works
Studying CaMKII: Tools and standards
Brown, C. N., & Bayer, K. U. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.113982 · Cited by 39 · see citing works
Integrins are involved in synaptogenesis, cell spreading, and adhesion in the postnatal brain
Nikonenko, I., Toni, N., Moosmayer, M., Shigeri, Y., Müller, D., & Jones, L. S. (2003) · Developmental Brain Research · doi:10.1016/s0165-3806(02)00590-4 · Cited by 40 · see citing works
Self-citationNeuroprotective effect of AIP on N-methyl-d-aspartate-induced cell death in retinal neurons
Laabich, A., & Cooper, N. G. F. (2000) · Molecular Brain Research · doi:10.1016/s0169-328x(00)00226-6 · Cited by 39 · see citing works
The role of CaMKII in BDNF-mediated neuroprotection of retinal ganglion cells (RGC-5)
Fan, W., Agarwal, N. A., & Cooper, N. G. F. (2005) · Brain Research · doi:10.1016/j.brainres.2005.10.030 · Cited by 38 · see citing works
Yamanaka, I., Miki, M., Asakawa, K., Kawakami, K., Oda, Y., & Hirata, H. (2013) · Genes to Cells · doi:10.1111/gtc.12032 · Cited by 37 · see citing works
Itami, C., & Kimura, F. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.2506-12.2012 · Cited by 35 · see citing works
Watterson, D., Mirzoeva, S., Guo, L.-Y., Whyte, A., Bourguignon, J., Hibert, M., Haiech, J., & Eldik, L. V. V. (2001) · Neurochemistry International · doi:10.1016/s0197-0186(01)00053-5 · Cited by 33 · see citing works
Rose, A. J., Alsted, T. J., Kobberø, J. B., & Richter, E. A. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2006.127464 · Cited by 36 · see citing works
Liu, Z., Zhang, J.-J., Liu, X., & Yu, L. (2012) · Neuroscience Letters · doi:10.1016/j.neulet.2012.05.003 · Cited by 34 · see citing works
Hayes, M., Mora, L., & Lucáková, S. (2022) · Biomolecules · doi:10.3390/biom12121806 · Cited by 32 · see citing works
Karls, A. S., & Mynlieff, M. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13259 · Cited by 25 · see citing works
Tatsu, Y., Shigeri, Y., Ishida, A., Kameshita, I., Fujisawa, H., & Yumoto, N. (1999) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(99)00140-7 · Cited by 23 · see citing works
Self-citationRetinal ganglion cell death and neuroprotection: Involvement of the CaMKIIα gene
Fan, W., Agarwal, N. A., Kumar, M. D., & Cooper, N. G. F. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2005.06.008 · Cited by 22 · see citing works
Carter, S., Pitt, S. J., Colyer, J., & Sitsapesan, R. M. (2011) · The Journal of Membrane Biology · doi:10.1007/s00232-011-9339-9 · Cited by 21 · see citing works
Heme-induced Trypanosoma cruzi proliferation is mediated by CaM kinase II
Souza, C. F., Carneiro, A. B., da Silveira, A. B., Laranja, G. A. T., Silva-Neto, M. A. C., da Costa, S. C. G., & Paes, M. C. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.09.135 · Cited by 20 · see citing works
Cooper, N. G. F., Laabich, A., Fan, W., & Wang, X. (2008) · Progress in brain research · doi:10.1016/s0079-6123(08)01136-9 · Cited by 20 · see citing works
Zha, X., Dailey, M. E., & Green, S. H. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22033 · Cited by 20 · see citing works
Kobayashi, Y., Fukuda, T., Tanaka, M., & Matsui, T. (2012) · FEBS Open Bio · doi:10.1016/j.fob.2012.04.005 · Cited by 19 · see citing works
Dias, A., de Nonohay, U., & Blessmann, G. (2012) · Arquivos rio-grandenses de medicina · Cited by 18 · see citing works
Kumrungsee, T., Saiki, T., Akiyama, S., Nakashima, K., Tanaka, M., Kobayashi, Y., & Matsui, T. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.07.020 · Cited by 13 · see citing works
Optogenetic Techniques for Manipulating and Sensing G Protein-Coupled Receptor Signaling
Abreu, N., & Levitz, J. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0755-8_2 · Cited by 13 · see citing works
Kinumi, T., Niki, E., Shigeri, Y., & Matsumoto, H. (2005) · The Journal of Biochemistry · doi:10.1093/jb/mvi178 · Cited by 13 · see citing works
Self-citationStevens, I. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4637 · Cited by 11 · see citing works
ATP-conjugated peptide inhibitors for calmodulin-dependent protein kinase II
Ahn, D., Han, K.-C., Kwon, H. S., & Yang, E. G. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.09.070 · Cited by 10 · see citing works
Regulation of signaling proteins in the brain by light
Lamprecht, R. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2019.101638 · Cited by 8 · see citing works
Fiumelli, H., Herrera‐López, G., Lemtiri‐Chlieh, F., Mottier, L., Girgis, J., Benadiba, C., Jourdain, P., Carrano, N., Mahmood, H., Ooi, A., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.21.624499 · Cited by 3 · see citing works
Controlling Protein Function by Caged Compounds
Giordano, A., Zarbakhsh, S., & Schultz, C. (2007) · Chemical biology · doi:10.1002/9783527619375.ch3b · Cited by 2 · see citing works
Analysis Of CPEB Family Protein Member CPEB4 Function In Mammalian Neurons: A Dissertation
Kan, K. (2008) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/k2p5-k961
Photochemical Enzyme Regulation
Peng, L., & Goeldner, M. P. (2008) · Protein Science Encyclopedia · doi:10.1002/9783527610754.fa18
Realization of phosphorylation hypothesis of sleep by mammalian CaMKIIβPreprint
Tone, D., Ode, K. L., Zhang, Q., Fujishima, H., Yamada, R. G., Nagashima, Y., Matsumoto, K., Wen, Z., Yoshida, S. Y., Mitani, T. T., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.11.463945
Abstracts of Communications of the 1999 Meeting of the Japanese Society for Neurochemistry (JSN)
(2000) · Neurochemical Research · doi:10.1023/a:1017272726209
CaMKII mechanisms in plasticity, learning and memory: Approaches and concepts
Bayer, K. U., Brown, C. N., & Giese, K.-P. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15754-7.00057-2
Role of the Cytoplasmic Polyadenylation Element Binding Proteins in Neuron: A Dissertation
Oruganty-Das, A. (2013) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/m2tw29
- Authors
- Ishida, A., Shigeri, Y., Tatsu, Y., Uegaki, K., Kameshita, I., Okuno, S., Kitani, T., Yumoto, N., & Fujisawa, H.
- Affiliations
- Asahikawa Medical University (JP)
- National Institute of Advanced Industrial Science and Technology (JP)
- Corresponding author
- Fujisawa, Hitoshi
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1998-05
- Volume
- 427
- Issue
- 1
- Pages
- 115-118
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2055847058
- Cited by
- 64
- References
- 23
- Citations by year
- 2024: 3 · 2023: 1 · 2022: 4 · 2021: 2 · 2020: 1 · 2019: 1 · 2017: 3 · 2016: 2 · 2015: 1 · 2014: 1 · 2013: 2 · 2012: 4
- FWCI
- 0.93
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (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 › Chemical Synthesis and Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- calcium/calmodulin-dependent protein kinase II, CaMKII inhibitor, peptide inhibitors, amino acid substitutions, site-directed mutagenesis, IC50, peptide analogues
- MeSH terms
- Animals, Cerebral Cortex, Peptide Fragments, Peptides, Structure-Activity Relationship, Calcium-Calmodulin-Dependent Protein Kinases, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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