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- Andersen P., Sundberg S. H., Sveen O., Wigström H. Specific long-lasting potentiation of synaptic transmission in hippocampal slices. Nature. 1977 Apr 21;266(5604):736–737. doi: 10.1038/266736a0. [DOI] [PubMed] [Google Scholar]
- Bliss T. V., Collingridge G. L. A synaptic model of memory: long-term potentiation in the hippocampus. Nature. 1993 Jan 7;361(6407):31–39. doi: 10.1038/361031a0. [DOI] [PubMed] [Google Scholar]
- Bliss T. V., Gardner-Medwin A. R. Long-lasting potentiation of synaptic transmission in the dentate area of the unanaestetized rabbit following stimulation of the perforant path. J Physiol. 1973 Jul;232(2):357–374. doi: 10.1113/jphysiol.1973.sp010274. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bliss T. V., Lomo T. Long-lasting potentiation of synaptic transmission in the dentate area of the anaesthetized rabbit following stimulation of the perforant path. J Physiol. 1973 Jul;232(2):331–356. doi: 10.1113/jphysiol.1973.sp010273. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Borner C., Filipuzzi I., Wartmann M., Eppenberger U., Fabbro D. Biosynthesis and posttranslational modifications of protein kinase C in human breast cancer cells. J Biol Chem. 1989 Aug 15;264(23):13902–13909. [PubMed] [Google Scholar]
- Bourne H. R., Nicoll R. Molecular machines integrate coincident synaptic signals. Cell. 1993 Jan;72 (Suppl):65–75. doi: 10.1016/s0092-8674(05)80029-7. [DOI] [PubMed] [Google Scholar]
- Cole A. J., Saffen D. W., Baraban J. M., Worley P. F. Rapid increase of an immediate early gene messenger RNA in hippocampal neurons by synaptic NMDA receptor activation. Nature. 1989 Aug 10;340(6233):474–476. doi: 10.1038/340474a0. [DOI] [PubMed] [Google Scholar]
- Crick F. Memory and molecular turnover. Nature. 1984 Nov 8;312(5990):101–101. doi: 10.1038/312101a0. [DOI] [PubMed] [Google Scholar]
- De Bondt H. L., Rosenblatt J., Jancarik J., Jones H. D., Morgan D. O., Kim S. H. Crystal structure of cyclin-dependent kinase 2. Nature. 1993 Jun 17;363(6430):595–602. doi: 10.1038/363595a0. [DOI] [PubMed] [Google Scholar]
- Flint A. J., Paladini R. D., Koshland D. E., Jr Autophosphorylation of protein kinase C at three separated regions of its primary sequence. Science. 1990 Jul 27;249(4967):408–411. doi: 10.1126/science.2377895. [DOI] [PubMed] [Google Scholar]
- Frey U., Huang Y. Y., Kandel E. R. Effects of cAMP simulate a late stage of LTP in hippocampal CA1 neurons. Science. 1993 Jun 11;260(5114):1661–1664. doi: 10.1126/science.8389057. [DOI] [PubMed] [Google Scholar]
- Goelet P., Castellucci V. F., Schacher S., Kandel E. R. The long and the short of long-term memory--a molecular framework. 1986 Jul 31-Aug 6Nature. 322(6078):419–422. doi: 10.1038/322419a0. [DOI] [PubMed] [Google Scholar]
- Hanks S. K., Quinn A. M., Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science. 1988 Jul 1;241(4861):42–52. doi: 10.1126/science.3291115. [DOI] [PubMed] [Google Scholar]
- Hanson P. I., Schulman H. Neuronal Ca2+/calmodulin-dependent protein kinases. Annu Rev Biochem. 1992;61:559–601. doi: 10.1146/annurev.bi.61.070192.003015. [DOI] [PubMed] [Google Scholar]
- Hegde A. N., Goldberg A. L., Schwartz J. H. Regulatory subunits of cAMP-dependent protein kinases are degraded after conjugation to ubiquitin: a molecular mechanism underlying long-term synaptic plasticity. Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7436–7440. doi: 10.1073/pnas.90.16.7436. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Huang K. P., Chan K. F., Singh T. J., Nakabayashi H., Huang F. L. Autophosphorylation of rat brain Ca2+-activated and phospholipid-dependent protein kinase. J Biol Chem. 1986 Sep 15;261(26):12134–12140. [PubMed] [Google Scholar]
- Inoue M., Kishimoto A., Takai Y., Nishizuka Y. Studies on a cyclic nucleotide-independent protein kinase and its proenzyme in mammalian tissues. II. Proenzyme and its activation by calcium-dependent protease from rat brain. J Biol Chem. 1977 Nov 10;252(21):7610–7616. [PubMed] [Google Scholar]
- Jessell T. M., Kandel E. R. Synaptic transmission: a bidirectional and self-modifiable form of cell-cell communication. Cell. 1993 Jan;72 (Suppl):1–30. doi: 10.1016/s0092-8674(05)80025-x. [DOI] [PubMed] [Google Scholar]
- Kandel E. R., Schwartz J. H. Molecular biology of learning: modulation of transmitter release. Science. 1982 Oct 29;218(4571):433–443. doi: 10.1126/science.6289442. [DOI] [PubMed] [Google Scholar]
- Kennedy M. B. Regulation of synaptic transmission in the central nervous system: long-term potentiation. Cell. 1989 Dec 1;59(5):777–787. doi: 10.1016/0092-8674(89)90601-6. [DOI] [PubMed] [Google Scholar]
- Klann E., Chen S. J., Sweatt J. D. Mechanism of protein kinase C activation during the induction and maintenance of long-term potentiation probed using a selective peptide substrate. Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8337–8341. doi: 10.1073/pnas.90.18.8337. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lisman J. E. A mechanism for memory storage insensitive to molecular turnover: a bistable autophosphorylating kinase. Proc Natl Acad Sci U S A. 1985 May;82(9):3055–3057. doi: 10.1073/pnas.82.9.3055. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mayford M., Barzilai A., Keller F., Schacher S., Kandel E. R. Modulation of an NCAM-related adhesion molecule with long-term synaptic plasticity in Aplysia. Science. 1992 May 1;256(5057):638–644. doi: 10.1126/science.1585176. [DOI] [PubMed] [Google Scholar]
- Mochly-Rosen D., Koshland D. E., Jr Domain structure and phosphorylation of protein kinase C. J Biol Chem. 1987 Feb 15;262(5):2291–2297. [PubMed] [Google Scholar]
- Nicoll R. A., Kauer J. A., Malenka R. C. The current excitement in long-term potentiation. Neuron. 1988 Apr;1(2):97–103. doi: 10.1016/0896-6273(88)90193-6. [DOI] [PubMed] [Google Scholar]
- Nishizuka Y. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science. 1992 Oct 23;258(5082):607–614. doi: 10.1126/science.1411571. [DOI] [PubMed] [Google Scholar]
- Norbury C., Nurse P. Animal cell cycles and their control. Annu Rev Biochem. 1992;61:441–470. doi: 10.1146/annurev.bi.61.070192.002301. [DOI] [PubMed] [Google Scholar]
- Ohno S., Konno Y., Akita Y., Yano A., Suzuki K. A point mutation at the putative ATP-binding site of protein kinase C alpha abolishes the kinase activity and renders it down-regulation-insensitive. A molecular link between autophosphorylation and down-regulation. J Biol Chem. 1990 Apr 15;265(11):6296–6300. [PubMed] [Google Scholar]
- Sacktor T. C., Osten P., Valsamis H., Jiang X., Naik M. U., Sublette E. Persistent activation of the zeta isoform of protein kinase C in the maintenance of long-term potentiation. Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8342–8346. doi: 10.1073/pnas.90.18.8342. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schwartz J. H., Greenberg S. M. Molecular mechanisms for memory: second-messenger induced modifications of protein kinases in nerve cells. Annu Rev Neurosci. 1987;10:459–476. doi: 10.1146/annurev.ne.10.030187.002331. [DOI] [PubMed] [Google Scholar]
- Schwartzkroin P. A., Wester K. Long-lasting facilitation of a synaptic potential following tetanization in the in vitro hippocampal slice. Brain Res. 1975 May 16;89(1):107–119. doi: 10.1016/0006-8993(75)90138-9. [DOI] [PubMed] [Google Scholar]
- Silva A. J., Paylor R., Wehner J. M., Tonegawa S. Impaired spatial learning in alpha-calcium-calmodulin kinase II mutant mice. Science. 1992 Jul 10;257(5067):206–211. doi: 10.1126/science.1321493. [DOI] [PubMed] [Google Scholar]
- Silva A. J., Stevens C. F., Tonegawa S., Wang Y. Deficient hippocampal long-term potentiation in alpha-calcium-calmodulin kinase II mutant mice. Science. 1992 Jul 10;257(5067):201–206. doi: 10.1126/science.1378648. [DOI] [PubMed] [Google Scholar]
- Takahashi J. S., Kornhauser J. M., Koumenis C., Eskin A. Molecular approaches to understanding circadian oscillations. Annu Rev Physiol. 1993;55:729–753. doi: 10.1146/annurev.ph.55.030193.003501. [DOI] [PubMed] [Google Scholar]