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Volumn 203-204, Issue , 2002, Pages 207-209

Cerebrospinal fluid tissue transglutaminase in vascular dementia

Author keywords

Alzheimer's disease; Apoptosis; Tau protein; Tissue transglutaminase; Vascular dementia

Indexed keywords

AMYLOID BETA PROTEIN; BIOCHEMICAL MARKER; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

EID: 0037111190     PISSN: 0022510X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-510X(02)00292-7     Document Type: Conference Paper
Times cited : (6)

References (52)
  • 1
    • 0034974232 scopus 로고    scopus 로고
    • A review of the epidemiological transition in dementia-cross-national comparisons of the indices related to Alzheimer's disease and vascular dementia
    • Suh G.H., Shah A. A review of the epidemiological transition in dementia-cross-national comparisons of the indices related to Alzheimer's disease and vascular dementia. Acta Psychiatr. Scand. 104(1):2001;4-11.
    • (2001) Acta Psychiatr. Scand. , vol.104 , Issue.1 , pp. 4-11
    • Suh, G.H.1    Shah, A.2
  • 2
    • 0036370014 scopus 로고    scopus 로고
    • Clinicopathological validation study of four sets of clinical criteria for vascular dementia
    • Gold G., Bouras C., Canuto A.et al. Clinicopathological validation study of four sets of clinical criteria for vascular dementia. Am. J. Psychiatry. 159(1):2002;82-87.
    • (2002) Am. J. Psychiatry , vol.159 , Issue.1 , pp. 82-87
    • Gold, G.1    Bouras, C.2    Canuto, A.3
  • 3
    • 0036163065 scopus 로고    scopus 로고
    • Vascular dementia: A diagnosis running out of time
    • Stewart R. Vascular dementia: a diagnosis running out of time. Br. J. Psychiatry. 180:2002;152-156.
    • (2002) Br. J. Psychiatry , vol.180 , pp. 152-156
    • Stewart, R.1
  • 4
    • 33749201901 scopus 로고    scopus 로고
    • Outcome measures for probable vascular dementia and Alzheimer's disease with cerebrovascular disease
    • Gauthier S., Ferris S. Outcome measures for probable vascular dementia and Alzheimer's disease with cerebrovascular disease. Int. J. Clin. Pract., Suppl. 120:2001;29-39.
    • (2001) Int. J. Clin. Pract., Suppl. , vol.120 , pp. 29-39
    • Gauthier, S.1    Ferris, S.2
  • 5
    • 0035108753 scopus 로고    scopus 로고
    • Evaluation of CSF-tau and CSF-Abeta42 as diagnostic markers for Alzheimer disease in clinical practice
    • Andreasen N., Minthon L., Davidsson P.et al. Evaluation of CSF-tau and CSF-Abeta42 as diagnostic markers for Alzheimer disease in clinical practice. Arch. Neurol. 58(3):2001;373-379.
    • (2001) Arch. Neurol. , vol.58 , Issue.3 , pp. 373-379
    • Andreasen, N.1    Minthon, L.2    Davidsson, P.3
  • 6
    • 0034282184 scopus 로고    scopus 로고
    • Relationship between apoE genotype and CSF beta-amyloid (1-42) and tau in patients with probable and definite Alzheimer's disease
    • Tapiola T., Pirttila T., Mehta P.D., Alafuzofff I., Lehtovirta M., Soininen H. Relationship between apoE genotype and CSF beta-amyloid (1-42) and tau in patients with probable and definite Alzheimer's disease. Neurobiol. Aging. 21(5):2000;735-740.
    • (2000) Neurobiol. Aging , vol.21 , Issue.5 , pp. 735-740
    • Tapiola, T.1    Pirttila, T.2    Mehta, P.D.3    Alafuzofff, I.4    Lehtovirta, M.5    Soininen, H.6
  • 7
    • 0033953722 scopus 로고    scopus 로고
    • Three-year follow-up of cerebrospinal fluid tau, beta-amyloid 42 and 40 concentrations in Alzheimer's disease
    • Tapiola T., Pirttila T., Mikkonen M.et al. Three-year follow-up of cerebrospinal fluid tau, beta-amyloid 42 and 40 concentrations in Alzheimer's disease. Neurosci. Lett. 280(2):2000;119-122.
    • (2000) Neurosci. Lett. , vol.280 , Issue.2 , pp. 119-122
    • Tapiola, T.1    Pirttila, T.2    Mikkonen, M.3
  • 8
    • 0034440140 scopus 로고    scopus 로고
    • A unifying hypothesis of Alzheimer's disease: IV. Causation and sequence of events
    • Heininger K. A unifying hypothesis of Alzheimer's disease: IV. Causation and sequence of events. Rev. Neurosci. 11:2000;213-328.
    • (2000) Rev. Neurosci. , vol.11 , pp. 213-328
    • Heininger, K.1
  • 9
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang J., Lemaire H.G., Unterbeck A.et al. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature. 325(6106):1987;733-736.
    • (1987) Nature , vol.325 , Issue.6106 , pp. 733-736
    • Kang, J.1    Lemaire, H.G.2    Unterbeck, A.3
  • 11
    • 0022980104 scopus 로고
    • Alzheimer's disease: Tau proteins, the promoting factors of microtubule assembly, are major components of paired helical filaments
    • Delacourte A., Defossez A. Alzheimer's disease: tau proteins, the promoting factors of microtubule assembly, are major components of paired helical filaments. J. Neurol. Sci. 76(2-3):1986;173-186.
    • (1986) J. Neurol. Sci. , vol.76 , Issue.2-3 , pp. 173-186
    • Delacourte, A.1    Defossez, A.2
  • 12
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik K.S., Joachim C.L., Selkoe D.J. Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc. Natl. Acad. Sci. U. S. A. 83(11):1986;4044-4048.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , Issue.11 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 13
    • 0026595846 scopus 로고
    • Tau proteins of Alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms
    • Goedert M., Spillantini M.G., Cairns N.J., Crowther R.A. Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms. Neuron. 8(1):1992;159-168.
    • (1992) Neuron , vol.8 , Issue.1 , pp. 159-168
    • Goedert, M.1    Spillantini, M.G.2    Cairns, N.J.3    Crowther, R.A.4
  • 14
    • 0025904444 scopus 로고
    • A68: A major subunit of paired helical filaments and derivatized forms of normal tau
    • Lee V.M., Balin B.J., Otvos L. Jr., Trojanowski J.Q. A68: a major subunit of paired helical filaments and derivatized forms of normal tau. Science. 251(4994):1991;675-678.
    • (1991) Science , vol.251 , Issue.4994 , pp. 675-678
    • Lee, V.M.1    Balin, B.J.2    Otvos L., Jr.3    Trojanowski, J.Q.4
  • 16
    • 0034257067 scopus 로고    scopus 로고
    • Tissue transglutaminase: A possible role in neurodegenerative diseases
    • Lesort M., Tucholski J., Miller M.L., Johnson G.V. Tissue transglutaminase: a possible role in neurodegenerative diseases. Prog. Neurobiol. 61(5):2000;439-463.
    • (2000) Prog. Neurobiol. , vol.61 , Issue.5 , pp. 439-463
    • Lesort, M.1    Tucholski, J.2    Miller, M.L.3    Johnson, G.V.4
  • 17
    • 0035951672 scopus 로고    scopus 로고
    • Three different human tau isoforms and rat neurofilament light, middle and heavy chain proteins are cellular substrates for transglutaminase
    • Grierson A.J., Johnson G.V., Miller C.C. Three different human tau isoforms and rat neurofilament light, middle and heavy chain proteins are cellular substrates for transglutaminase. Neurosci. Lett. 298(1):2001;9-12.
    • (2001) Neurosci. Lett. , vol.298 , Issue.1 , pp. 9-12
    • Grierson, A.J.1    Johnson, G.V.2    Miller, C.C.3
  • 18
    • 0034990512 scopus 로고    scopus 로고
    • Tissue transglutaminase selectively modifies proteins associated with truncated mutant huntingtin in intact cells
    • Chun W., Lesort M., Tucholski J.et al. Tissue transglutaminase selectively modifies proteins associated with truncated mutant huntingtin in intact cells. Neurobiol. Dis. 8(3):2001;391-404.
    • (2001) Neurobiol. Dis. , vol.8 , Issue.3 , pp. 391-404
    • Chun, W.1    Lesort, M.2    Tucholski, J.3
  • 19
    • 0035795406 scopus 로고    scopus 로고
    • Tissue transglutaminase does not contribute to the formation of mutant huntingtin aggregates
    • Chun W., Lesort M., Tucholski J., Ross C.A., Johnson G.V. Tissue transglutaminase does not contribute to the formation of mutant huntingtin aggregates. J. Cell Biol. 153(1):2001;25-34.
    • (2001) J. Cell Biol. , vol.153 , Issue.1 , pp. 25-34
    • Chun, W.1    Lesort, M.2    Tucholski, J.3    Ross, C.A.4    Johnson, G.V.5
  • 20
    • 0033764710 scopus 로고    scopus 로고
    • Transglutaminase-induced cross-linking of tau proteins in progressive supranuclear palsy
    • Zemaitaitis M.O., Lee J.M., Troncoso J.C., Muma N.A. Transglutaminase-induced cross-linking of tau proteins in progressive supranuclear palsy. J. Neuropathol. Exp. Neurol. 59(11):2000;983-989.
    • (2000) J. Neuropathol. Exp. Neurol. , vol.59 , Issue.11 , pp. 983-989
    • Zemaitaitis, M.O.1    Lee, J.M.2    Troncoso, J.C.3    Muma, N.A.4
  • 21
    • 0025823541 scopus 로고
    • Cross-linking of laminin-nidogen complexes by tissue transglutaminase. A novel mechanism for basement membrane stabilization
    • Aeschlimann D., Paulsson M. Cross-linking of laminin-nidogen complexes by tissue transglutaminase. A novel mechanism for basement membrane stabilization. J. Biol. Chem. 266(23):1991;15308-15317.
    • (1991) J. Biol. Chem. , vol.266 , Issue.23 , pp. 15308-15317
    • Aeschlimann, D.1    Paulsson, M.2
  • 22
    • 0028322985 scopus 로고
    • Transglutaminases: Protein cross-linking enzymes in tissues and body fluids
    • Aeschlimann D., Paulsson M. Transglutaminases: protein cross-linking enzymes in tissues and body fluids. Thromb. Haemost. 71(4):1994;402-415.
    • (1994) Thromb. Haemost. , vol.71 , Issue.4 , pp. 402-415
    • Aeschlimann, D.1    Paulsson, M.2
  • 23
    • 0029862039 scopus 로고    scopus 로고
    • Transglutaminase induction by various cell death and apoptosis pathways
    • Fesus L., Madi A., Balajthy Z., Nemes Z., Szondy Z. Transglutaminase induction by various cell death and apoptosis pathways. Experientia. 52(10-11):1996;942-949.
    • (1996) Experientia , vol.52 , Issue.10-11 , pp. 942-949
    • Fesus, L.1    Madi, A.2    Balajthy, Z.3    Nemes, Z.4    Szondy, Z.5
  • 24
    • 0026348625 scopus 로고
    • Apoptosis: Molecular mechanisms in programmed cell death
    • Fesus L., Davies P.J., Piacentini M. Apoptosis: molecular mechanisms in programmed cell death. Eur. J. Cell Biol. 56(2):1991;170-177.
    • (1991) Eur. J. Cell Biol. , vol.56 , Issue.2 , pp. 170-177
    • Fesus, L.1    Davies, P.J.2    Piacentini, M.3
  • 25
    • 0025881544 scopus 로고
    • Apoptosis: A potential role for cytosolic transglutaminase and its importance in tumour progression
    • Knight C.R., Rees R.C., Griffin M. Apoptosis: a potential role for cytosolic transglutaminase and its importance in tumour progression. Biochim. Biophys. Acta. 1096(4):1991;312-318.
    • (1991) Biochim. Biophys. Acta , vol.1096 , Issue.4 , pp. 312-318
    • Knight, C.R.1    Rees, R.C.2    Griffin, M.3
  • 26
    • 0002520649 scopus 로고    scopus 로고
    • Intron-exon swapping of transglutaminase mRNA and neuronal tau aggregation in Alzheimer's disease
    • Citron B.A., SantaCruz K.S., Davies P.J., Festoff B.W. Intron-exon swapping of transglutaminase mRNA and neuronal tau aggregation in Alzheimer's disease. J. Biol. Chem. 29:2000;29.
    • (2000) J. Biol. Chem. , vol.29 , pp. 29
    • Citron, B.A.1    SantaCruz, K.S.2    Davies, P.J.3    Festoff, B.W.4
  • 27
    • 0033373675 scopus 로고    scopus 로고
    • Elevated transglutaminase-induced bonds in PHF tau in Alzheimer's disease
    • Norlund M.A., Lee J.M., Zainelli G.M., Muma N.A. Elevated transglutaminase-induced bonds in PHF tau in Alzheimer's disease. Brain Res. 851(1-2):1999;154-163.
    • (1999) Brain Res. , vol.851 , Issue.1-2 , pp. 154-163
    • Norlund, M.A.1    Lee, J.M.2    Zainelli, G.M.3    Muma, N.A.4
  • 28
    • 0024597647 scopus 로고
    • Differential expression of tissue transglutaminase in human cells. An immunohistochemical study
    • Thomazy V., Fesus L. Differential expression of tissue transglutaminase in human cells. An immunohistochemical study. Cell Tissue Res. 255(1):1989;215-224.
    • (1989) Cell Tissue Res. , vol.255 , Issue.1 , pp. 215-224
    • Thomazy, V.1    Fesus, L.2
  • 29
    • 0029614688 scopus 로고
    • Purification and characterization of rat brain transglutaminase
    • Ohashi H., Itoh Y., Birckbichler P.J., Takeuchi Y. Purification and characterization of rat brain transglutaminase. J. Biochem. (Tokyo). 118(6):1995;1271-1278.
    • (1995) J. Biochem. (Tokyo) , vol.118 , Issue.6 , pp. 1271-1278
    • Ohashi, H.1    Itoh, Y.2    Birckbichler, P.J.3    Takeuchi, Y.4
  • 30
    • 0027480066 scopus 로고
    • Covalent modification of synapsin I by a tetanus toxin-activated transglutaminase
    • Facchiano F., Benfenati F., Valtorta F., Luini A. Covalent modification of synapsin I by a tetanus toxin-activated transglutaminase. J. Biol. Chem. 268(7):1993;4588-4591.
    • (1993) J. Biol. Chem. , vol.268 , Issue.7 , pp. 4588-4591
    • Facchiano, F.1    Benfenati, F.2    Valtorta, F.3    Luini, A.4
  • 31
    • 0034796349 scopus 로고    scopus 로고
    • Plasticity and stabilization of neuromuscular and CNS synapses: Interactions between thrombin protease signaling pathways and tissue transglutaminase
    • Festoff B.W., Suo Z., Citron B.A. Plasticity and stabilization of neuromuscular and CNS synapses: interactions between thrombin protease signaling pathways and tissue transglutaminase. Int. Rev. Cytol. 211:2001;153-177.
    • (2001) Int. Rev. Cytol. , vol.211 , pp. 153-177
    • Festoff, B.W.1    Suo, Z.2    Citron, B.A.3
  • 32
    • 0025822888 scopus 로고
    • Protein cross-linking by transglutaminase induced in long-term potentiation in the Ca1 region of hippocampal slices
    • Friedrich P., Fesus L., Tarcsa E., Czeh G. Protein cross-linking by transglutaminase induced in long-term potentiation in the Ca1 region of hippocampal slices. Neuroscience. 43(2-3):1991;331-334.
    • (1991) Neuroscience , vol.43 , Issue.2-3 , pp. 331-334
    • Friedrich, P.1    Fesus, L.2    Tarcsa, E.3    Czeh, G.4
  • 33
    • 0027249085 scopus 로고
    • Rapid and transient alterations in transglutaminase activity in rat superior cervical ganglia following denervation or axotomy
    • Ando M., Kunii S., Tatematsu T., Nagata Y. Rapid and transient alterations in transglutaminase activity in rat superior cervical ganglia following denervation or axotomy. Neurosci. Res. 17(1):1993;47-52.
    • (1993) Neurosci. Res. , vol.17 , Issue.1 , pp. 47-52
    • Ando, M.1    Kunii, S.2    Tatematsu, T.3    Nagata, Y.4
  • 34
    • 0035863525 scopus 로고    scopus 로고
    • Tissue transglutaminase is essential for neurite outgrowth in human neuroblastoma SH-SY5Y cells
    • Tucholski J., Lesort M., Johnson G.V. Tissue transglutaminase is essential for neurite outgrowth in human neuroblastoma SH-SY5Y cells. Neuroscience. 102(2):2001;481-491.
    • (2001) Neuroscience , vol.102 , Issue.2 , pp. 481-491
    • Tucholski, J.1    Lesort, M.2    Johnson, G.V.3
  • 35
    • 0026644491 scopus 로고
    • Cell cycle kinetics, tissue transglutaminase and programmed cell death (apoptosis)
    • el Alaoui S., Mian S., Lawry J., Quash G., Griffin M. Cell cycle kinetics, tissue transglutaminase and programmed cell death (apoptosis). FEBS Lett. 311(2):1992;174-178.
    • (1992) FEBS Lett. , vol.311 , Issue.2 , pp. 174-178
    • El Alaoui, S.1    Mian, S.2    Lawry, J.3    Quash, G.4    Griffin, M.5
  • 36
    • 0023159034 scopus 로고
    • Induction and activation of tissue transglutaminase during programmed cell death
    • Fesus L., Thomazy V., Falus A. Induction and activation of tissue transglutaminase during programmed cell death. FEBS Lett. 224(1):1987;104-108.
    • (1987) FEBS Lett. , vol.224 , Issue.1 , pp. 104-108
    • Fesus, L.1    Thomazy, V.2    Falus, A.3
  • 37
    • 0029976253 scopus 로고    scopus 로고
    • DNA damage and apoptosis in Alzheimer's disease: Colocalization with c-Jun immunoreactivity, relationship to brain area, and effect of postmortem delay
    • Anderson A.J., Su J.H., Cotman C.W. DNA damage and apoptosis in Alzheimer's disease: colocalization with c-Jun immunoreactivity, relationship to brain area, and effect of postmortem delay. J. Neurosci. 16(5):1996;1710-1719.
    • (1996) J. Neurosci. , vol.16 , Issue.5 , pp. 1710-1719
    • Anderson, A.J.1    Su, J.H.2    Cotman, C.W.3
  • 38
    • 0029245289 scopus 로고
    • A potential role for apoptosis in neurodegeneration and Alzheimer's disease
    • Cotman C.W., Anderson A.J. A potential role for apoptosis in neurodegeneration and Alzheimer's disease. Mol. Neurobiol. 10(1):1995;19-45.
    • (1995) Mol. Neurobiol. , vol.10 , Issue.1 , pp. 19-45
    • Cotman, C.W.1    Anderson, A.J.2
  • 39
    • 0028060558 scopus 로고
    • Tissue transglutaminase and apoptosis: Sense and antisense transfection studies with human neuroblastoma cells
    • Melino G., Annicchiarico-Petruzzelli M., Piredda L.et al. Tissue transglutaminase and apoptosis: sense and antisense transfection studies with human neuroblastoma cells. Mol. Cell. Biol. 14(10):1994;6584-6596.
    • (1994) Mol. Cell. Biol. , vol.14 , Issue.10 , pp. 6584-6596
    • Melino, G.1    Annicchiarico-Petruzzelli, M.2    Piredda, L.3
  • 40
    • 0026705663 scopus 로고
    • Expression of tissue transglutaminase in Balb-C 3T3 fibroblasts: Effects on cellular morphology and adhesion
    • Gentile V., Thomazy V., Piacentini M., Fesus L., Davies P.J. Expression of tissue transglutaminase in Balb-C 3T3 fibroblasts: effects on cellular morphology and adhesion. J. Cell Biol. 119(2):1992;463-474.
    • (1992) J. Cell Biol. , vol.119 , Issue.2 , pp. 463-474
    • Gentile, V.1    Thomazy, V.2    Piacentini, M.3    Fesus, L.4    Davies, P.J.5
  • 41
    • 0033004913 scopus 로고    scopus 로고
    • Identification of 'tissue' transglutaminase binding proteins in neural cells committed to apoptosis
    • Piredda L., Farrace M.G., Lo Bello M.et al. Identification of 'tissue' transglutaminase binding proteins in neural cells committed to apoptosis. FASEB J. 13(2):1999;355-364.
    • (1999) FASEB J. , vol.13 , Issue.2 , pp. 355-364
    • Piredda, L.1    Farrace, M.G.2    Lo Bello, M.3
  • 43
    • 0033607671 scopus 로고    scopus 로고
    • Inhibition of "tissue" transglutaminase increases cell survival by preventing apoptosis
    • Oliverio S., Amendola A., Rodolfo C., Spinedi A., Piacentini M. Inhibition of "tissue" transglutaminase increases cell survival by preventing apoptosis. J. Biol. Chem. 274(48):1999;34123-34128.
    • (1999) J. Biol. Chem. , vol.274 , Issue.48 , pp. 34123-34128
    • Oliverio, S.1    Amendola, A.2    Rodolfo, C.3    Spinedi, A.4    Piacentini, M.5
  • 44
    • 0034022634 scopus 로고    scopus 로고
    • Tissue transglutaminase in the small intestine of the mouse as a marker for apoptotic cells. Colocalization with DNA fragmentation
    • Aschoff A.P., Gunther E., Jirikowski G.F. Tissue transglutaminase in the small intestine of the mouse as a marker for apoptotic cells. Colocalization with DNA fragmentation. Histochem. Cell Biol. 113(4):2000;313-317.
    • (2000) Histochem. Cell Biol. , vol.113 , Issue.4 , pp. 313-317
    • Aschoff, A.P.1    Gunther, E.2    Jirikowski, G.F.3
  • 45
    • 0343569927 scopus 로고    scopus 로고
    • Increased cerebrospinal fluid fas (Apo-1) levels in Alzheimer's disease. Relationship with IL-6 concentrations
    • Martinez M., Fernandez-Vivancos E., Frank A., De la Fuente M., Hernanz A. Increased cerebrospinal fluid fas (Apo-1) levels in Alzheimer's disease. Relationship with IL-6 concentrations. Brain Res. 869(1-2):2000;216-219.
    • (2000) Brain Res. , vol.869 , Issue.1-2 , pp. 216-219
    • Martinez, M.1    Fernandez-Vivancos, E.2    Frank, A.3    De la Fuente, M.4    Hernanz, A.5
  • 46
    • 0032425260 scopus 로고    scopus 로고
    • Transglutaminase-catalyzed protein cross-linking in the molecular program of apoptosis and its relationship to neuronal processes
    • Fesus L. Transglutaminase-catalyzed protein cross-linking in the molecular program of apoptosis and its relationship to neuronal processes. Cell. Mol. Neurobiol. 18(6):1998;683-694.
    • (1998) Cell. Mol. Neurobiol. , vol.18 , Issue.6 , pp. 683-694
    • Fesus, L.1
  • 47
    • 0034743767 scopus 로고    scopus 로고
    • N(epsilon)(gamma-glutamyl)lysine in cerebrospinal fluid marks Alzheimer type and vascular dementia
    • Nemes Z., Fesus L., Egerhazi A., Keszthelyi A., Degrell I.M. N(epsilon)(gamma-glutamyl)lysine in cerebrospinal fluid marks Alzheimer type and vascular dementia. Neurobiol. Aging. 22(3):2001;403-406.
    • (2001) Neurobiol. Aging , vol.22 , Issue.3 , pp. 403-406
    • Nemes, Z.1    Fesus, L.2    Egerhazi, A.3    Keszthelyi, A.4    Degrell, I.M.5
  • 48
    • 0017680149 scopus 로고
    • The epsilon-(gamma-glutamyl)lysine crosslink and the catalytic role of transglutaminases
    • Folk J.E., Finlayson J.S. The epsilon-(gamma-glutamyl)lysine crosslink and the catalytic role of transglutaminases. Adv. Protein Chem. 31:1977;1-133.
    • (1977) Adv. Protein Chem. , vol.31 , pp. 1-133
    • Folk, J.E.1    Finlayson, J.S.2
  • 49
    • 0026636023 scopus 로고
    • Calcium as sculptor and destroyer of neural circuitry
    • Mattson M.P. Calcium as sculptor and destroyer of neural circuitry. Exp. Gerontol. 27(1):1992;29-49.
    • (1992) Exp. Gerontol. , vol.27 , Issue.1 , pp. 29-49
    • Mattson, M.P.1
  • 50
    • 0029096258 scopus 로고
    • Transglutaminase cross-linking of the tau protein
    • Miller M.L., Johnson G.V. Transglutaminase cross-linking of the tau protein. J. Neurochem. 65(4):1995;1760-1770.
    • (1995) J. Neurochem. , vol.65 , Issue.4 , pp. 1760-1770
    • Miller, M.L.1    Johnson, G.V.2
  • 51
    • 0027184294 scopus 로고
    • Transglutaminase catalyzes the formation of sodium dodecyl sulfate-insoluble, Alz-50-reactive polymers of tau
    • Dudek S.M., Johnson G.V. Transglutaminase catalyzes the formation of sodium dodecyl sulfate-insoluble, Alz-50-reactive polymers of tau. J. Neurochem. 61(3):1993;1159-1162.
    • (1993) J. Neurochem. , vol.61 , Issue.3 , pp. 1159-1162
    • Dudek, S.M.1    Johnson, G.V.2
  • 52
    • 0028356872 scopus 로고
    • Immunohistochemical localization of tissue transglutaminase and Bcl-2 in rat uterine tissues during embryo implantation and post-partum involution
    • Piacentini M., Autuori F. Immunohistochemical localization of tissue transglutaminase and Bcl-2 in rat uterine tissues during embryo implantation and post-partum involution. Differentiation. 57(1):1994;51-61.
    • (1994) Differentiation , vol.57 , Issue.1 , pp. 51-61
    • Piacentini, M.1    Autuori, F.2


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