메뉴 건너뛰기




Volumn 76, Issue , 2015, Pages 13-23

Pin1 cysteine-113 oxidation inhibits its catalytic activity and cellular function in Alzheimer's disease

Author keywords

Alzheimer's disease; APP; Oxidation; Pin1; Tau

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; DIAMINE; HYDROGEN PEROXIDE; PEPTIDYLPROLYL ISOMERASE PIN1; REACTIVE OXYGEN METABOLITE; TAU PROTEIN; ANTIBODY; NIMA-INTERACTING PEPTIDYLPROLYL ISOMERASE; PEPTIDYLPROLYL ISOMERASE;

EID: 84922347183     PISSN: 09699961     EISSN: 1095953X     Source Type: Journal    
DOI: 10.1016/j.nbd.2014.12.027     Document Type: Article
Times cited : (83)

References (77)
  • 2
    • 0026743110 scopus 로고
    • Distribution of Alzheimer-type pathologic changes in nondemented elderly individuals matches the pattern in Alzheimer's disease
    • Arriagada P.V., Marzloff K., Hyman B.T. Distribution of Alzheimer-type pathologic changes in nondemented elderly individuals matches the pattern in Alzheimer's disease. Neurology 1992, 42:1681-1688.
    • (1992) Neurology , vol.42 , pp. 1681-1688
    • Arriagada, P.V.1    Marzloff, K.2    Hyman, B.T.3
  • 3
    • 0042476570 scopus 로고    scopus 로고
    • Pin1 regulates the timing of mammalian primordial germ cell proliferation
    • Atchison F.W., Capel B., Means A.R. Pin1 regulates the timing of mammalian primordial germ cell proliferation. Development 2003, 130:3579-3586.
    • (2003) Development , vol.130 , pp. 3579-3586
    • Atchison, F.W.1    Capel, B.2    Means, A.R.3
  • 4
    • 84902595279 scopus 로고    scopus 로고
    • Cysteine-mediated dynamic hydrogen-bonding network in the active site of Pin1
    • Barman A., Hamelberg D. Cysteine-mediated dynamic hydrogen-bonding network in the active site of Pin1. Biochemistry 2014, 53:3839-3850.
    • (2014) Biochemistry , vol.53 , pp. 3839-3850
    • Barman, A.1    Hamelberg, D.2
  • 5
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • Behl C., Davis J.B., Lesley R., Schubert D. Hydrogen peroxide mediates amyloid beta protein toxicity. Cell 1994, 77:817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 7
    • 0036591849 scopus 로고    scopus 로고
    • Lipid peroxidation and protein oxidation in Alzheimer's disease brain: potential causes and consequences involving amyloid beta-peptide-associated free radical oxidative stress
    • Butterfield D.A., Lauderback C.M. Lipid peroxidation and protein oxidation in Alzheimer's disease brain: potential causes and consequences involving amyloid beta-peptide-associated free radical oxidative stress. Free Radic. Biol. Med. 2002, 32:1050-1060.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1050-1060
    • Butterfield, D.A.1    Lauderback, C.M.2
  • 8
    • 0035194145 scopus 로고    scopus 로고
    • Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid beta-peptide
    • Butterfield D.A., Drake J., Pocernich C., Castegna A. Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid beta-peptide. Trends Mol. Med. 2001, 7:548-554.
    • (2001) Trends Mol. Med. , vol.7 , pp. 548-554
    • Butterfield, D.A.1    Drake, J.2    Pocernich, C.3    Castegna, A.4
  • 10
    • 33646144212 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: insights into the development of Alzheimer's disease
    • Butterfield D.A., Poon H.F., St Clair D., Keller J.N., Pierce W.M., Klein J.B., Markesbery W.R. Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: insights into the development of Alzheimer's disease. Neurobiol. Dis. 2006, 22:223-232.
    • (2006) Neurobiol. Dis. , vol.22 , pp. 223-232
    • Butterfield, D.A.1    Poon, H.F.2    St Clair, D.3    Keller, J.N.4    Pierce, W.M.5    Klein, J.B.6    Markesbery, W.R.7
  • 12
    • 79751537405 scopus 로고    scopus 로고
    • Amyloid beta impairs mitochondrial anterograde transport and degenerates synapses in Alzheimer's disease neurons
    • Calkins M.J., Reddy P.H. Amyloid beta impairs mitochondrial anterograde transport and degenerates synapses in Alzheimer's disease neurons. Biochim. Biophys. Acta 2011, 1812:507-513.
    • (2011) Biochim. Biophys. Acta , vol.1812 , pp. 507-513
    • Calkins, M.J.1    Reddy, P.H.2
  • 13
    • 84869095520 scopus 로고    scopus 로고
    • P73 haploinsufficiency causes tau hyperphosphorylation and tau kinase dysregulation in mouse models of aging and Alzheimer's disease
    • Cancino G.I., Miller F.D., Kaplan D.R. p73 haploinsufficiency causes tau hyperphosphorylation and tau kinase dysregulation in mouse models of aging and Alzheimer's disease. Neurobiol. Aging 2013, 34:387-399.
    • (2013) Neurobiol. Aging , vol.34 , pp. 387-399
    • Cancino, G.I.1    Miller, F.D.2    Kaplan, D.R.3
  • 17
    • 0026544937 scopus 로고
    • The effect of age and Alzheimer's disease on pyramidal neuron density in the individual fields of the hippocampal formation
    • Davies D.C., Horwood N., Isaacs S.L., Mann D.M. The effect of age and Alzheimer's disease on pyramidal neuron density in the individual fields of the hippocampal formation. Acta Neuropathol. (Berl) 1992, 83:510-517.
    • (1992) Acta Neuropathol. (Berl) , vol.83 , pp. 510-517
    • Davies, D.C.1    Horwood, N.2    Isaacs, S.L.3    Mann, D.M.4
  • 18
    • 84894448444 scopus 로고    scopus 로고
    • Regulation of protein conformation by Pin1 offers novel disease mechanisms and therapeutic approaches in Alzheimer's disease
    • Driver J.A., Zhou X.Z., Lu K.P. Regulation of protein conformation by Pin1 offers novel disease mechanisms and therapeutic approaches in Alzheimer's disease. Discov. Med. 2014, 17:93-99.
    • (2014) Discov. Med. , vol.17 , pp. 93-99
    • Driver, J.A.1    Zhou, X.Z.2    Lu, K.P.3
  • 21
    • 84891589937 scopus 로고    scopus 로고
    • Antisense oligonucleotide against GSK-3beta in brain of SAMP8 mice improves learning and memory and decreases oxidative stress: Involvement of transcription factor Nrf2 and implications for Alzheimer disease
    • Farr S.A., Ripley J.L., Sultana R., Zhang Z., Niehoff M.L., Platt T.L., Murphy M.P., Morley J.E., Kumar V., Butterfield D.A. Antisense oligonucleotide against GSK-3beta in brain of SAMP8 mice improves learning and memory and decreases oxidative stress: Involvement of transcription factor Nrf2 and implications for Alzheimer disease. Free Radic. Biol. Med. 2014, 67:387-395.
    • (2014) Free Radic. Biol. Med. , vol.67 , pp. 387-395
    • Farr, S.A.1    Ripley, J.L.2    Sultana, R.3    Zhang, Z.4    Niehoff, M.L.5    Platt, T.L.6    Murphy, M.P.7    Morley, J.E.8    Kumar, V.9    Butterfield, D.A.10
  • 22
    • 1242292029 scopus 로고    scopus 로고
    • Regulation of peptide bond cis/transisomerization by enzyme catalysis and its implication in physiological processes
    • Fischer G., Aumuller T. Regulation of peptide bond cis/transisomerization by enzyme catalysis and its implication in physiological processes. Rev. Physiol. Biochem. Pharmacol. 2003, 148:105-150.
    • (2003) Rev. Physiol. Biochem. Pharmacol. , vol.148 , pp. 105-150
    • Fischer, G.1    Aumuller, T.2
  • 25
    • 0025969656 scopus 로고
    • Neocortical neuronal subpopulations labeled by a monoclonal antibody to calbindin exhibit differential vulnerability in Alzheimer's disease
    • Hof P.R., Morrison J.H. Neocortical neuronal subpopulations labeled by a monoclonal antibody to calbindin exhibit differential vulnerability in Alzheimer's disease. Exp. Neurol. 1991, 111:293-301.
    • (1991) Exp. Neurol. , vol.111 , pp. 293-301
    • Hof, P.R.1    Morrison, J.H.2
  • 26
    • 0032559238 scopus 로고    scopus 로고
    • Prolyl isomerase and nuclear function
    • Hunter T. Prolyl isomerase and nuclear function. Cell 1998, 92:141-143.
    • (1998) Cell , vol.92 , pp. 141-143
    • Hunter, T.1
  • 28
    • 0034620559 scopus 로고    scopus 로고
    • Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase
    • Jez J.M., Ferrer J.L., Bowman M.E., Dixon R.A., Noel J.P. Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase. Biochemistry 2000, 39:890-902.
    • (2000) Biochemistry , vol.39 , pp. 890-902
    • Jez, J.M.1    Ferrer, J.L.2    Bowman, M.E.3    Dixon, R.A.4    Noel, J.P.5
  • 31
  • 34
    • 80053304845 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis-trans isomerase Pin1 in ageing, cancer and Alzheimer disease
    • Lee T.H., Pastorino L., Lu K.P. Peptidyl-prolyl cis-trans isomerase Pin1 in ageing, cancer and Alzheimer disease. Expert Rev. Mol. Med. 2011, 13:e21.
    • (2011) Expert Rev. Mol. Med. , vol.13 , pp. e21
    • Lee, T.H.1    Pastorino, L.2    Lu, K.P.3
  • 38
    • 80053299231 scopus 로고    scopus 로고
    • Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins
    • Liou Y.C., Zhou X.Z., Lu K.P. Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins. Trends Biochem. Sci. 2011, 36:501-514.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 501-514
    • Liou, Y.C.1    Zhou, X.Z.2    Lu, K.P.3
  • 39
    • 84883674898 scopus 로고    scopus 로고
    • The redox biochemistry of protein sulfenylation and sulfinylation
    • Lo Conte M., Carroll K.S. The redox biochemistry of protein sulfenylation and sulfinylation. J. Biol. Chem. 2013, 288:26480-26488.
    • (2013) J. Biol. Chem. , vol.288 , pp. 26480-26488
    • Lo Conte, M.1    Carroll, K.S.2
  • 40
    • 84892995278 scopus 로고    scopus 로고
    • Pin1, a new player in the fate of HIF-1alpha degradation: an hypothetical mechanism inside vascular damage as Alzheimer's disease risk factor
    • Lonati E., Brambilla A., Milani C., Masserini M., Palestini P., Bulbarelli A. Pin1, a new player in the fate of HIF-1alpha degradation: an hypothetical mechanism inside vascular damage as Alzheimer's disease risk factor. Front. Cell. Neurosci. 2014, 8:1.
    • (2014) Front. Cell. Neurosci. , vol.8 , pp. 1
    • Lonati, E.1    Brambilla, A.2    Milani, C.3    Masserini, M.4    Palestini, P.5    Bulbarelli, A.6
  • 41
    • 1842763560 scopus 로고    scopus 로고
    • Pinning down cell signaling, cancer and Alzheimer's disease
    • Lu K.P. Pinning down cell signaling, cancer and Alzheimer's disease. Trends Biochem. Sci. 2004, 29:200-209.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 200-209
    • Lu, K.P.1
  • 42
    • 35448945269 scopus 로고    scopus 로고
    • The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease
    • Lu K.P., Zhou X.Z. The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease. Nat. Rev. Mol. Cell Biol. 2007, 8:904-916.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 904-916
    • Lu, K.P.1    Zhou, X.Z.2
  • 43
    • 0029916122 scopus 로고    scopus 로고
    • A human peptidyl-prolyl isomerase essential for regulation of mitosis
    • Lu K.P., Hanes S.D., Hunter T. A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature 1996, 380:544-547.
    • (1996) Nature , vol.380 , pp. 544-547
    • Lu, K.P.1    Hanes, S.D.2    Hunter, T.3
  • 44
    • 0033600242 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
    • Lu P.J., Wulf G., Zhou X.Z., Davies P., Lu K.P. The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein. Nature 1999, 399:784-788.
    • (1999) Nature , vol.399 , pp. 784-788
    • Lu, P.J.1    Wulf, G.2    Zhou, X.Z.3    Davies, P.4    Lu, K.P.5
  • 45
    • 0037322816 scopus 로고    scopus 로고
    • Proline-directed phosphorylation and isomerization in mitotic regulation and in Alzheimer's disease
    • Lu K.P., Liou Y.C., Vincent I. Proline-directed phosphorylation and isomerization in mitotic regulation and in Alzheimer's disease. BioEssays 2003, 25:174-181.
    • (2003) BioEssays , vol.25 , pp. 174-181
    • Lu, K.P.1    Liou, Y.C.2    Vincent, I.3
  • 46
    • 84904760940 scopus 로고    scopus 로고
    • Geniposide attenuates mitochondrial dysfunction and memory deficits in APP/PS1 transgenic mice
    • Lv C., Liu X., Liu H., Chen T., Zhang W. Geniposide attenuates mitochondrial dysfunction and memory deficits in APP/PS1 transgenic mice. Curr. Alzheimer Res. 2014, 11:580-587.
    • (2014) Curr. Alzheimer Res. , vol.11 , pp. 580-587
    • Lv, C.1    Liu, X.2    Liu, H.3    Chen, T.4    Zhang, W.5
  • 47
    • 84863230253 scopus 로고    scopus 로고
    • Prolyl isomerase Pin1 promotes amyloid precursor protein (APP) turnover by inhibiting glycogen synthase kinase-3beta (GSK3beta) activity: novel mechanism for Pin1 to protect against Alzheimer disease
    • Ma S.L., Pastorino L., Zhou X.Z., Lu K.P. Prolyl isomerase Pin1 promotes amyloid precursor protein (APP) turnover by inhibiting glycogen synthase kinase-3beta (GSK3beta) activity: novel mechanism for Pin1 to protect against Alzheimer disease. J. Biol. Chem. 2012, 287:6969-6973.
    • (2012) J. Biol. Chem. , vol.287 , pp. 6969-6973
    • Ma, S.L.1    Pastorino, L.2    Zhou, X.Z.3    Lu, K.P.4
  • 49
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesbery W.R. Oxidative stress hypothesis in Alzheimer's disease. Free Radic. Biol. Med. 1997, 23:134-147.
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 50
    • 0028916920 scopus 로고
    • Different amyloidogenic peptides share a similar mechanism of neurotoxicity involving reactive oxygen species and calcium
    • Mattson M.P., Goodman Y. Different amyloidogenic peptides share a similar mechanism of neurotoxicity involving reactive oxygen species and calcium. Brain Res. 1995, 676:219-224.
    • (1995) Brain Res. , vol.676 , pp. 219-224
    • Mattson, M.P.1    Goodman, Y.2
  • 52
    • 84859185373 scopus 로고    scopus 로고
    • Proline isomer-specific antibodies reveal the early pathogenic tau conformation in Alzheimer's disease
    • Nakamura K., Greenwood A., Binder L., Bigio E.H., Denial S., Nicholson L., Zhou X.Z., Lu K.P. Proline isomer-specific antibodies reveal the early pathogenic tau conformation in Alzheimer's disease. Cell 2012, 149:232-244.
    • (2012) Cell , vol.149 , pp. 232-244
    • Nakamura, K.1    Greenwood, A.2    Binder, L.3    Bigio, E.H.4    Denial, S.5    Nicholson, L.6    Zhou, X.Z.7    Lu, K.P.8
  • 53
    • 70449519969 scopus 로고    scopus 로고
    • Contribution of hypoxia to Alzheimer's disease: is HIF-1alpha a mediator of neurodegeneration?
    • Ogunshola O.O., Antoniou X. Contribution of hypoxia to Alzheimer's disease: is HIF-1alpha a mediator of neurodegeneration?. Cell. Mol. Life Sci. 2009, 66:3555-3563.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 3555-3563
    • Ogunshola, O.O.1    Antoniou, X.2
  • 54
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Met. Enzymol. 1997, 276:307-326.
    • (1997) Met. Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 56
    • 84861486615 scopus 로고    scopus 로고
    • Alzheimer's disease-related loss of Pin1 function influences the intracellular localization and the processing of AbetaPP
    • Pastorino L., Ma S.L., Balastik M., Huang P., Pandya D., Nicholson L., Lu K.P. Alzheimer's disease-related loss of Pin1 function influences the intracellular localization and the processing of AbetaPP. J. Alzheimers Dis. 2012, 30:277-297.
    • (2012) J. Alzheimers Dis. , vol.30 , pp. 277-297
    • Pastorino, L.1    Ma, S.L.2    Balastik, M.3    Huang, P.4    Pandya, D.5    Nicholson, L.6    Lu, K.P.7
  • 57
    • 0345512210 scopus 로고
    • Anatomical correlates of the distribution of the pathological changes in the neocortex in Alzheimer disease
    • Pearson R.C., Esiri M.M., Hiorns R.W., Wilcock G.K., Powell T.P. Anatomical correlates of the distribution of the pathological changes in the neocortex in Alzheimer disease. Proc. Natl. Acad. Sci. U. S. A. 1985, 82:4531-4534.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 4531-4534
    • Pearson, R.C.1    Esiri, M.M.2    Hiorns, R.W.3    Wilcock, G.K.4    Powell, T.P.5
  • 58
    • 10644275378 scopus 로고    scopus 로고
    • An antibody-based method for monitoring in vivo oxidation of protein tyrosine phosphatases
    • Persson C., Kappert K., Engstrom U., Ostman A., Sjoblom T. An antibody-based method for monitoring in vivo oxidation of protein tyrosine phosphatases. Methods 2005, 35:37-43.
    • (2005) Methods , vol.35 , pp. 37-43
    • Persson, C.1    Kappert, K.2    Engstrom, U.3    Ostman, A.4    Sjoblom, T.5
  • 60
    • 0142157635 scopus 로고    scopus 로고
    • Pin1 colocalization with phosphorylated tau in Alzheimer's disease and other tauopathies
    • Ramakrishnan P., Dickson D.W., Davies P. Pin1 colocalization with phosphorylated tau in Alzheimer's disease and other tauopathies. Neurobiol. Dis. 2003, 14:251-264.
    • (2003) Neurobiol. Dis. , vol.14 , pp. 251-264
    • Ramakrishnan, P.1    Dickson, D.W.2    Davies, P.3
  • 61
    • 0008233581 scopus 로고    scopus 로고
    • Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent
    • Ranganathan R., Lu K.P., Hunter T., Noel J.P. Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell 1997, 89:875-886.
    • (1997) Cell , vol.89 , pp. 875-886
    • Ranganathan, R.1    Lu, K.P.2    Hunter, T.3    Noel, J.P.4
  • 62
    • 0034840950 scopus 로고    scopus 로고
    • Pin1 regulates turnover and subcellular localization of beta-catenin by inhibiting its interaction with APC
    • Ryo A., Nakamura N., Wulf G., Liou Y.C., Lu K.P. Pin1 regulates turnover and subcellular localization of beta-catenin by inhibiting its interaction with APC. Nat. Cell Biol. 2001, 3:793-801.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 793-801
    • Ryo, A.1    Nakamura, N.2    Wulf, G.3    Liou, Y.C.4    Lu, K.P.5
  • 64
    • 0031010333 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman E.R., Berlett B.S. Reactive oxygen-mediated protein oxidation in aging and disease. Chem. Res. Toxicol. 1997, 10:485-494.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 485-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 68
    • 0035177565 scopus 로고    scopus 로고
    • Utilizing the peptidyl-prolyl cis-trans isomerase pin1 as a probe of its phosphorylated target proteins. Examples of binding to nuclear proteins in a human kidney cell line and to tau in Alzheimer's diseased brain
    • Thorpe J.R., Morley S.J., Rulten S.L. Utilizing the peptidyl-prolyl cis-trans isomerase pin1 as a probe of its phosphorylated target proteins. Examples of binding to nuclear proteins in a human kidney cell line and to tau in Alzheimer's diseased brain. J. Histochem. Cytochem. 2001, 49:97-108.
    • (2001) J. Histochem. Cytochem. , vol.49 , pp. 97-108
    • Thorpe, J.R.1    Morley, S.J.2    Rulten, S.L.3
  • 69
    • 5144224351 scopus 로고    scopus 로고
    • Shortfalls in the peptidyl-prolyl cis-trans isomerase protein Pin1 in neurons are associated with frontotemporal dementias
    • Thorpe J.R., Mosaheb S., Hashemzadeh-Bonehi L., Cairns N.J., Kay J.E., Morley S.J., Rulten S.L. Shortfalls in the peptidyl-prolyl cis-trans isomerase protein Pin1 in neurons are associated with frontotemporal dementias. Neurobiol. Dis. 2004, 17:237-249.
    • (2004) Neurobiol. Dis. , vol.17 , pp. 237-249
    • Thorpe, J.R.1    Mosaheb, S.2    Hashemzadeh-Bonehi, L.3    Cairns, N.J.4    Kay, J.E.5    Morley, S.J.6    Rulten, S.L.7
  • 71
    • 0035796405 scopus 로고    scopus 로고
    • Pin1 is overexpressed in breast cancer and potentiates the transcriptional activity of phosphorylated c-Jun towards the cyclin D1 gene
    • Wulf G.M., Ryo A., Wulf G.G., Lee S.W., Niu T., Lu K.P. Pin1 is overexpressed in breast cancer and potentiates the transcriptional activity of phosphorylated c-Jun towards the cyclin D1 gene. EMBO J. 2001, 20:3459-3472.
    • (2001) EMBO J. , vol.20 , pp. 3459-3472
    • Wulf, G.M.1    Ryo, A.2    Wulf, G.G.3    Lee, S.W.4    Niu, T.5    Lu, K.P.6
  • 72
    • 18344387559 scopus 로고    scopus 로고
    • Phosphorylation-specific prolyl isomerization: Is there an underlying theme?
    • Wulf G., Finn G., Suizu F., Lu K.P. Phosphorylation-specific prolyl isomerization: Is there an underlying theme?. Nat. Cell Biol. 2005, 7:435-441.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 435-441
    • Wulf, G.1    Finn, G.2    Suizu, F.3    Lu, K.P.4
  • 74
    • 0033133579 scopus 로고    scopus 로고
    • In vitro and in vivo oxidative stress associated with Alzheimer's amyloid beta-peptide (1-42)
    • (discussion 339-342)
    • Yatin S.M., Varadarajan S., Link C.D., Butterfield D.A. In vitro and in vivo oxidative stress associated with Alzheimer's amyloid beta-peptide (1-42). Neurobiol. Aging 1999, 20:325-330. (discussion 339-342).
    • (1999) Neurobiol. Aging , vol.20 , pp. 325-330
    • Yatin, S.M.1    Varadarajan, S.2    Link, C.D.3    Butterfield, D.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.