메뉴 건너뛰기




Volumn 28, Issue 11, 2003, Pages 1725-1734

Lysosomes and Brain Aging in Mammals

Author keywords

Life span; Lysosome; Mammals; Metabolism; Mitochondria; Neurodegeneration

Indexed keywords

AGING; ANIMAL TISSUE; BASAL METABOLIC RATE; BRAIN METABOLISM; BRAIN SIZE; BRAIN SLICE; DNA DAMAGE; IMMUNOCYTOCHEMISTRY; LIFESPAN; LONGEVITY; LYSOSOME MEMBRANE; MAMMAL CELL; MITOCHONDRIAL MEMBRANE; NERVE DEGENERATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN STABILITY; REVIEW;

EID: 0142116349     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1026069223763     Document Type: Review
Times cited : (39)

References (61)
  • 1
    • 0015319592 scopus 로고
    • The biological clock: The mitochondria?
    • Harman, D. 1972. The biological clock: The mitochondria? J. Am. Geriatr. Soc. 20:145-147.
    • (1972) J. Am. Geriatr. Soc. , vol.20 , pp. 145-147
    • Harman, D.1
  • 3
    • 0003107920 scopus 로고
    • Relation of lifespan to brain weight and body weight in mammals
    • Wohstenholme G. E. W. and O'Connor, M., (eds.), CIBA Foundation, London
    • Sacher, G. A. 1959. Relation of lifespan to brain weight and body weight in mammals. in Wohstenholme, G. E. W. and O'Connor, M., (eds.), Collog Aging, CIBA Foundation, London.
    • (1959) Collog Aging
    • Sacher, G.A.1
  • 5
    • 0025863618 scopus 로고
    • Neuropathological staging of Alzheimer-related changes
    • Braak, H. and Braak, E. 1991. Neuropathological staging of Alzheimer-related changes. Acta Neuropathol. (Berl.) 82:239-259.
    • (1991) Acta Neuropathol. (Berl.) , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 6
    • 0002017421 scopus 로고
    • Proteases, neurostability, and brain aging: An hypothesis
    • Crook T., Bartus, R. Ferris, D. Garshon, N. (eds.), Mark Powley Assoc. (publisher) New York
    • Lynch, G., Larson, J., and Baudry, M. 1986. Proteases, neurostability, and brain aging: An hypothesis, in Crook, T., Bartus, R. Ferris, D. Garshon, N. (eds.), Treatment Development Strategies for Alzheimer's Disease, Mark Powley Assoc. (publisher) New York.
    • (1986) Treatment Development Strategies for Alzheimer's Disease
    • Lynch, G.1    Larson, J.2    Baudry, M.3
  • 7
    • 84957355538 scopus 로고
    • Body size and metabolic rate
    • Kleiber, M. 1947. Body size and metabolic rate. Physiol. Rev. 27:511-541.
    • (1947) Physiol. Rev. , vol.27 , pp. 511-541
    • Kleiber, M.1
  • 8
    • 0019978393 scopus 로고
    • Energy metabolism and body size: I. Is the 0.75 mass exponent of Kleiber's equation a statistical artifact?
    • Heusner, A. A. 1982. Energy metabolism and body size: I. Is the 0.75 mass exponent of Kleiber's equation a statistical artifact? Respir. Physiol. 48:1-12.
    • (1982) Respir. Physiol. , vol.48 , pp. 1-12
    • Heusner, A.A.1
  • 10
    • 0032439245 scopus 로고    scopus 로고
    • Mitochondrial free radical production and aging in mammals and birds
    • Barja, G. 1998. Mitochondrial free radical production and aging in mammals and birds. Ann. N Y Acad. Sci. 854:224-238.
    • (1998) Ann. N. Y. Acad. Sci. , vol.854 , pp. 224-238
    • Barja, G.1
  • 11
    • 0018834664 scopus 로고
    • Taxonomic differences in the mammalian lifespan-body weight relationship and the problem of brain weight
    • Economos, A. C. 1980. Taxonomic differences in the mammalian lifespan-body weight relationship and the problem of brain weight. Gerontology 26:90-98.
    • (1980) Gerontology , vol.26 , pp. 90-98
    • Economos, A.C.1
  • 12
    • 0021004982 scopus 로고
    • Energy metabolism, brain size and longevity in mammals
    • Hofman, M. A. 1983. Energy metabolism, brain size and longevity in mammals. Q. Rev. Biol. 58:495-512.
    • (1983) Q. Rev. Biol. , vol.58 , pp. 495-512
    • Hofman, M.A.1
  • 13
    • 0038326624 scopus 로고    scopus 로고
    • Neurofibrillary tangles, amyloid, and memory in aging and mild cognitive impairment
    • Guillozet, A. L. Weintraub, S., Mash, D. C., and Mesulam, M. M. 2003. Neurofibrillary tangles, amyloid, and memory in aging and mild cognitive impairment. Arch. Neurol. 60:729-736.
    • (2003) Arch. Neurol. , vol.60 , pp. 729-736
    • Guillozet, A.L.1    Weintraub, S.2    Mash, D.C.3    Mesulam, M.M.4
  • 14
    • 0036224457 scopus 로고    scopus 로고
    • Alzheimer's neurofibrillary pathology and the spectrum of cognitive function: Findings from the Num Study
    • Riley, K. P., Snowdon, D. A., and Markesbery, W. R. 2002. Alzheimer's neurofibrillary pathology and the spectrum of cognitive function: Findings from the Num Study. Ann. Neurol. 51:567-577.
    • (2002) Ann. Neurol. , vol.51 , pp. 567-577
    • Riley, K.P.1    Snowdon, D.A.2    Markesbery, W.R.3
  • 17
    • 0035093896 scopus 로고    scopus 로고
    • Immunohistochemical investigation of the brain of aged dogs: I. Detection of neurofibrillary tangles and of 4-hydroxynonenal protein, an oxidative damage product, in senile plaques
    • Papaioannou, N., Tooten, P. C., van Ederen, A. M., Bohl, J. R., Rofina, J., Tsangaris, T., Gruys, E. 2001. Immunohistochemical investigation of the brain of aged dogs: I. Detection of neurofibrillary tangles and of 4-hydroxynonenal protein, an oxidative damage product, in senile plaques. Amyloid 8:11-21.
    • (2001) Amyloid , vol.8 , pp. 11-21
    • Papaioannou, N.1    Tooten, P.C.2    Van Ederen, A.M.3    Bohl, J.R.4    Rofina, J.5    Tsangaris, T.6    Gruys, E.7
  • 18
    • 0028210962 scopus 로고
    • Abnormally phosphorylated tau protein related to the formation of neurofibrillary tangles and neuropil threads in the cerebral cortex of sheep and goat
    • Braak, H., Braak, E., and Strothjohann, M. 1994. Abnormally phosphorylated tau protein related to the formation of neurofibrillary tangles and neuropil threads in the cerebral cortex of sheep and goat. Neurosci. Lett. 171:1-4.
    • (1994) Neurosci. Lett. , vol.171 , pp. 1-4
    • Braak, H.1    Braak, E.2    Strothjohann, M.3
  • 19
    • 0033635056 scopus 로고    scopus 로고
    • Age-related progression of tau pathology in brains of baboons
    • Schultz, C., Hubbard, G. B., Rub, U., Braak, E., and Braak, H. 2000. Age-related progression of tau pathology in brains of baboons. Neurobiol. Aging 21:905-912.
    • (2000) Neurobiol. Aging , vol.21 , pp. 905-912
    • Schultz, C.1    Hubbard, G.B.2    Rub, U.3    Braak, E.4    Braak, H.5
  • 20
    • 0030833582 scopus 로고    scopus 로고
    • Beta-amyloid (A beta) deposition in the brains of aged orangutans
    • Gearing, M., Tigges, J., and Mori, H., and Mirra, S. S. 1997. Beta-amyloid (A beta) deposition in the brains of aged orangutans. Neurobiol. Aging 18:139-146.
    • (1997) Neurobiol. Aging , vol.18 , pp. 139-146
    • Gearing, M.1    Tigges, J.2    Mori, H.3    Mirra, S.S.4
  • 21
    • 0019128901 scopus 로고
    • Age-related alterations of the proximal axon segment in lamina IIIab-pyramidal cells of the human isocortex: A Golgi and fine structural study
    • Braak, E., Braak, H., Strenge, H., and Muhtaroglu, A. U. 1980. Age-related alterations of the proximal axon segment in lamina IIIab-pyramidal cells of the human isocortex: A Golgi and fine structural study. J. Hirnforsch. 21:531-553.
    • (1980) J. Hirnforsch. , vol.21 , pp. 531-553
    • Braak, E.1    Braak, H.2    Strenge, H.3    Muhtaroglu, A.U.4
  • 22
    • 0018649369 scopus 로고
    • Spindle-shaped appendages of IIIab-pyramids filled with lipofuscin: A striking pathological change of the senescent human isocortex
    • Braak, H. 1979. Spindle-shaped appendages of IIIab-pyramids filled with lipofuscin: A striking pathological change of the senescent human isocortex. Acta Neuropathol. (Berl.) 46:197-202.
    • (1979) Acta Neuropathol. (Berl.) , vol.46 , pp. 197-202
    • Braak, H.1
  • 24
    • 0036934160 scopus 로고    scopus 로고
    • Amyloid-beta deposits in the cerebral cortex of the aged common marmoset (Callithrix jacchus): Incidence and chemical composition
    • Geula, C., Nagykery, N., and Wu, C. K. 2002. Amyloid-beta deposits in the cerebral cortex of the aged common marmoset (Callithrix jacchus): Incidence and chemical composition. Acta Neuropathol. (Berl.) 103:48-58.
    • (2002) Acta Neuropathol. (Berl.) , vol.103 , pp. 48-58
    • Geula, C.1    Nagykery, N.2    Wu, C.K.3
  • 25
    • 0038417092 scopus 로고    scopus 로고
    • Distribution, progression and chemical composition of cortical amyloid-beta deposits in aged rhesus monkeys: Similarities to the human
    • Sani, S., Traul, D., Klink, A., Niaraki, N., Gonzalo-Ruiz, A., Wu, C. K., and Geula, C. 2003. Distribution, progression and chemical composition of cortical amyloid-beta deposits in aged rhesus monkeys: Similarities to the human. Acta Neuropathol. (Berl.) 105:145-156.
    • (2003) Acta Neuropathol. (Berl.) , vol.105 , pp. 145-156
    • Sani, S.1    Traul, D.2    Klink, A.3    Niaraki, N.4    Gonzalo-Ruiz, A.5    Wu, C.K.6    Geula, C.7
  • 27
    • 0036751980 scopus 로고    scopus 로고
    • Brain aging in the canine: A diet enriched in antioxidants reduces cognitive dysfunction
    • Cotman, C. W., Head, E., Muggenburg, B. A., Zicker, S., and Milgram, N. W. 2002. Brain aging in the canine: A diet enriched in antioxidants reduces cognitive dysfunction. Neurobiol. Aging 23:809-818.
    • (2002) Neurobiol. Aging , vol.23 , pp. 809-818
    • Cotman, C.W.1    Head, E.2    Muggenburg, B.A.3    Zicker, S.4    Milgram, N.W.5
  • 29
    • 0027332522 scopus 로고
    • Beta-amyloid accumulation in aged canine brain: A model of early plaque formation in Alzheimer's disease
    • Cummings, B. J., Su, J. H., Cotman, C. W., White, R., and Russell, M. J. 1993. Beta-amyloid accumulation in aged canine brain: A model of early plaque formation in Alzheimer's disease. Neurobiol. Aging 14:547-560.
    • (1993) Neurobiol. Aging , vol.14 , pp. 547-560
    • Cummings, B.J.1    Su, J.H.2    Cotman, C.W.3    White, R.4    Russell, M.J.5
  • 30
    • 0030805991 scopus 로고    scopus 로고
    • Frequency of stages of Alzheimer-related lesions in different age categories
    • Braak, H. and Braak, E. 1997. Frequency of stages of Alzheimer-related lesions in different age categories. Neurobiol. Aging 18: 351-357.
    • (1997) Neurobiol. Aging , vol.18 , pp. 351-357
    • Braak, H.1    Braak, E.2
  • 31
    • 0142109143 scopus 로고
    • Lipofuscin and ceroid pigments: State of the art
    • Kitani, K., Ivy, G. O., and Shimasaki, H. 1995. Lipofuscin and ceroid pigments: State of the art. Gerontology 41(suppl 2):1-330.
    • (1995) Gerontology , vol.41 , Issue.SUPPL. 2 , pp. 1-330
    • Kitani, K.1    Ivy, G.O.2    Shimasaki, H.3
  • 32
    • 0028090564 scopus 로고
    • Age-related accumulation of lipofuscin in three different regions of rat brain
    • Oenzil, F., Kishikawa, M., Mizuno, T., and Nakano, M. 1994. Age-related accumulation of lipofuscin in three different regions of rat brain. Mech. Ageing Dev. 76:157-163.
    • (1994) Mech. Ageing Dev. , vol.76 , pp. 157-163
    • Oenzil, F.1    Kishikawa, M.2    Mizuno, T.3    Nakano, M.4
  • 33
    • 0028323067 scopus 로고
    • Age-related changes in activities and localizations of cathepsins D, E, B, and L in the rat brain tissues
    • Nakanishi, H., Tominaga, K., Amano, T., Hirotsu, I., Inoue, T., and Yamamoto, K. 1994. Age-related changes in activities and localizations of cathepsins D, E, B, and L in the rat brain tissues. Exp. Neurol. 126:119-128.
    • (1994) Exp. Neurol. , vol.126 , pp. 119-128
    • Nakanishi, H.1    Tominaga, K.2    Amano, T.3    Hirotsu, I.4    Inoue, T.5    Yamamoto, K.6
  • 37
    • 0031022255 scopus 로고    scopus 로고
    • Increased expression of cathepsins E and D in neurons of the aged rat brain and their colocalization with lipofuscin and carboxy-terminal fragments of Alzheimer amyloid precursor protein
    • Nakanishi, H., Amano, T., Sastradipura, D. F., Yoshimine, Y., Tsukuba, T., Tanabe, K., Hirotsu, I., Ohono, T., and Yamamoto, K. 1997. Increased expression of cathepsins E and D in neurons of the aged rat brain and their colocalization with lipofuscin and carboxy-terminal fragments of Alzheimer amyloid precursor protein. J. Neurochem. 68:739-749.
    • (1997) J. Neurochem. , vol.68 , pp. 739-749
    • Nakanishi, H.1    Amano, T.2    Sastradipura, D.F.3    Yoshimine, Y.4    Tsukuba, T.5    Tanabe, K.6    Hirotsu, I.7    Ohono, T.8    Yamamoto, K.9
  • 39
    • 0026327404 scopus 로고
    • Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease
    • Cataldo, A. M., Paskevich, P. A., Kominami, E., and Nixon, R. A. 1991. Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease. Proc. Natl. Acad. Sci. USA 88:10998-11002.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10998-11002
    • Cataldo, A.M.1    Paskevich, P.A.2    Kominami, E.3    Nixon, R.A.4
  • 40
    • 0033025080 scopus 로고    scopus 로고
    • Quantitative decrease in synaptophysin message expression and increase in cathepsin D message expression in Alzheimer disease neurons containing neurofibrillary tangles
    • Callahan, L. M., Vaules, W. A., and Coleman, P. D. 1999. Quantitative decrease in synaptophysin message expression and increase in cathepsin D message expression in Alzheimer disease neurons containing neurofibrillary tangles. J. Neuropathol. Exp. Neurol. 58:275-287.
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , pp. 275-287
    • Callahan, L.M.1    Vaules, W.A.2    Coleman, P.D.3
  • 41
    • 0028812394 scopus 로고
    • Elevated levels of the endosomal-lysosomal proteinase cathepsin D in cerebrospinal fluid in Alzheimer disease
    • Schwagerl, A. L., Mohan, P. S., Cataldo, A. M., Vonsattel, J. P., Kowall, N. W., and Nixon, R. A. 1995. Elevated levels of the endosomal-lysosomal proteinase cathepsin D in cerebrospinal fluid in Alzheimer disease. J. Neurochem. 64:443-446.
    • (1995) J. Neurochem. , vol.64 , pp. 443-446
    • Schwagerl, A.L.1    Mohan, P.S.2    Cataldo, A.M.3    Vonsattel, J.P.4    Kowall, N.W.5    Nixon, R.A.6
  • 42
    • 0034008566 scopus 로고    scopus 로고
    • Regionally selective changes in brain lysosomes occur in the transition from young adulthood to middle age in rats
    • Bi, X., Yong, A. P., Zhou, J., Gall, C. M., and Lynch, G. 2000. Regionally selective changes in brain lysosomes occur in the transition from young adulthood to middle age in rats. Neuroscience 97:395-404.
    • (2000) Neuroscience , vol.97 , pp. 395-404
    • Bi, X.1    Yong, A.P.2    Zhou, J.3    Gall, C.M.4    Lynch, G.5
  • 43
    • 0043233071 scopus 로고    scopus 로고
    • Spatial patterns of mammalian brain aging: Distribution of cathepsin D immunoreactive cell bodies and dystrophic dendrites in aging dogs resembles that in Alzheimer's disease
    • Bi, X., Head, E., Cotman, C., and Lynch, G. 2003. Spatial patterns of mammalian brain aging: Distribution of cathepsin D immunoreactive cell bodies and dystrophic dendrites in aging dogs resembles that in Alzheimer's disease. J. Comp. Neurol. 464:371-381.
    • (2003) J. Comp. Neurol. , vol.464 , pp. 371-381
    • Bi, X.1    Head, E.2    Cotman, C.3    Lynch, G.4
  • 45
    • 0021675999 scopus 로고
    • Inhibitors of lysosomal enzymes: Accumulation of lipofuscin-like dense bodies in the brain
    • Ivy, G. O., Schottler, F., Wenzel, J., Baudry, M., and Lynch, G. 1984. Inhibitors of lysosomal enzymes: Accumulation of lipofuscin-like dense bodies in the brain. Science 226:985-987.
    • (1984) Science , vol.226 , pp. 985-987
    • Ivy, G.O.1    Schottler, F.2    Wenzel, J.3    Baudry, M.4    Lynch, G.5
  • 46
    • 0024467482 scopus 로고
    • Anomalous accumulation of tau and ubiquitin immunoreactivities in rat brain caused by protease inhibition and by normal aging: A clue to PHF pathogenesis?
    • Ivy, G. O., Kitani, K., and Ihara, Y. 1989. Anomalous accumulation of tau and ubiquitin immunoreactivities in rat brain caused by protease inhibition and by normal aging: A clue to PHF pathogenesis? Brain Res. 498:360-365.
    • (1989) Brain Res. , vol.498 , pp. 360-365
    • Ivy, G.O.1    Kitani, K.2    Ihara, Y.3
  • 47
    • 0028171520 scopus 로고
    • Induction of beta-amyloid-containing polypeptides in hippocampus: Evidence for a concomitant loss of synaptic proteins and interactions with an excitotoxin
    • Babr, B. A., Abai, B., Gall, C. M., Vanderklish, P. W., Hoffman, K. B., and Lynch, G. 1994. Induction of beta-amyloid-containing polypeptides in hippocampus: Evidence for a concomitant loss of synaptic proteins and interactions with an excitotoxin. Exp. Neurol. 129:81-94.
    • (1994) Exp. Neurol. , vol.129 , pp. 81-94
    • Babr, B.A.1    Abai, B.2    Gall, C.M.3    Vanderklish, P.W.4    Hoffman, K.B.5    Lynch, G.6
  • 48
    • 0030905260 scopus 로고    scopus 로고
    • Suppression of cathepsins B and L causes a proliferation of lysosomes and the formation of meganeurites in hippocampus
    • Bednarski, E., Ribak, C. E., and Lynch, G. 1997. Suppression of cathepsins B and L causes a proliferation of lysosomes and the formation of meganeurites in hippocampus. J. Neurosci. 17:4006-4021.
    • (1997) J. Neurosci. , vol.17 , pp. 4006-4021
    • Bednarski, E.1    Ribak, C.E.2    Lynch, G.3
  • 49
    • 0032837802 scopus 로고    scopus 로고
    • Lysosomal protease inhibitors induce meganeurites and tangle-like structures in entorhinohippocampal regions vulnerable to Alzheimer's disease
    • Bi, X., Zhou, J., and Lynch, G. 1999. Lysosomal protease inhibitors induce meganeurites and tangle-like structures in entorhinohippocampal regions vulnerable to Alzheimer's disease. Exp. Neurol. 158:312-327.
    • (1999) Exp. Neurol. , vol.158 , pp. 312-327
    • Bi, X.1    Zhou, J.2    Lynch, G.3
  • 50
    • 0032931344 scopus 로고    scopus 로고
    • Lysosomal dysfunction results in lamina-specific meganeurite formation but not apoptosis in frontal cortex
    • Yong, A. P., Bednarski, E., Gall, C. M., Lynch, G., and Ribak, C. E. 1999. Lysosomal dysfunction results in lamina-specific meganeurite formation but not apoptosis in frontal cortex. Exp. Neurol. 157:150-160.
    • (1999) Exp. Neurol. , vol.157 , pp. 150-160
    • Yong, A.P.1    Bednarski, E.2    Gall, C.M.3    Lynch, G.4    Ribak, C.E.5
  • 51
    • 0034030039 scopus 로고    scopus 로고
    • Novel cathepsin D inhibitors block the formation of hyperphosphorylated tau fragments in hippocampus
    • Bi, X., Haque, T. S., Zhou, J., Skillman, A. G., Lin, B., Lee, C. E., Kuntz, I. D., Ellman, J. A., and Lynch, G. 2000. Novel cathepsin D inhibitors block the formation of hyperphosphorylated tau fragments in hippocampus. J. Neurochem. 74:1469-1477.
    • (2000) J. Neurochem. , vol.74 , pp. 1469-1477
    • Bi, X.1    Haque, T.S.2    Zhou, J.3    Skillman, A.G.4    Lin, B.5    Lee, C.E.6    Kuntz, I.D.7    Ellman, J.A.8    Lynch, G.9
  • 52
    • 0029845397 scopus 로고    scopus 로고
    • Cytosolic proteolysis of tau by cathepsin D in hippocampus following suppression of cathepsins B and L
    • Bednarski, E. and Lynch, G. 1996. Cytosolic proteolysis of tau by cathepsin D in hippocampus following suppression of cathepsins B and L. J. Neurochem. 67:1846-1855.
    • (1996) J. Neurochem. , vol.67 , pp. 1846-1855
    • Bednarski, E.1    Lynch, G.2
  • 53
    • 0035902583 scopus 로고    scopus 로고
    • Rapid induction of intraneuronal neurofibrillary tangles in apolipoprotein E-deficient mice
    • Bi, X., Yong, A. P., Zhou, J., Ribak, C. E., and Lynch, G. 2001. Rapid induction of intraneuronal neurofibrillary tangles in apolipoprotein E-deficient mice. Proc. Natl. Acad. Sci. USA 98:8832-8837.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8832-8837
    • Bi, X.1    Yong, A.P.2    Zhou, J.3    Ribak, C.E.4    Lynch, G.5
  • 54
    • 77049171682 scopus 로고
    • Structural and functional organization of mammalian cerebral cortex: The correlation of neuron density with brain size
    • Tower, D. B. 1954. Structural and functional organization of mammalian cerebral cortex: The correlation of neuron density with brain size. J. Comp. Neurol. 101:19-51.
    • (1954) J. Comp. Neurol. , vol.101 , pp. 19-51
    • Tower, D.B.1
  • 55
    • 0035292635 scopus 로고    scopus 로고
    • Principles underlying mammalian neocortical scaling
    • Changizi, M. A. 2001. Principles underlying mammalian neocortical scaling. Biol. Cybern. 84:207-215.
    • (2001) Biol. Cybern. , vol.84 , pp. 207-215
    • Changizi, M.A.1
  • 57
    • 0000936753 scopus 로고
    • Cell counts in the primate cerebral cortex
    • Shariff, G. A. 1953. Cell counts in the primate cerebral cortex. J. Comp. Neurol. 98:381-400.
    • (1953) J. Comp. Neurol. , vol.98 , pp. 381-400
    • Shariff, G.A.1
  • 58
    • 0022591085 scopus 로고
    • A comparative study of soluble calcium-dependent proteolytic activity in brain
    • Baudry, M., Simonson, L., Dubrin, R., and Lynch, G. 1986. A comparative study of soluble calcium-dependent proteolytic activity in brain. J. Neurobiol. 17:15-28.
    • (1986) J. Neurobiol. , vol.17 , pp. 15-28
    • Baudry, M.1    Simonson, L.2    Dubrin, R.3    Lynch, G.4
  • 59
    • 0036848631 scopus 로고    scopus 로고
    • Induction and experience-dependent consolidation of stable long-term potentiation lasting months in the hippocampus
    • Abraham, W. C., Logan, B., Greenwood, J. M., and Dragunow, M. 2002. Induction and experience-dependent consolidation of stable long-term potentiation lasting months in the hippocampus. J. Neurosci. 22:9626-9634.
    • (2002) J. Neurosci. , vol.22 , pp. 9626-9634
    • Abraham, W.C.1    Logan, B.2    Greenwood, J.M.3    Dragunow, M.4
  • 60
    • 0023485206 scopus 로고
    • Stable hippocampal long-term potentiation elicited by 'theta' pattern stimulation
    • Staubli, U. and Lynch, G. 1987. Stable hippocampal long-term potentiation elicited by 'theta' pattern stimulation. Brain Res. 435:227-234.
    • (1987) Brain Res. , vol.435 , pp. 227-234
    • Staubli, U.1    Lynch, G.2
  • 61
    • 0025263801 scopus 로고
    • Stable depression of potentiated synaptic responses in the hippocampus with 1-5 Hz stimulation
    • Staubli, U. and Lynch, G. 1990. Stable depression of potentiated synaptic responses in the hippocampus with 1-5 Hz stimulation. Brain Res. 513:113-118.
    • (1990) Brain Res. , vol.513 , pp. 113-118
    • Staubli, U.1    Lynch, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.