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Volumn 55, Issue 3, 2018, Pages 2653-2675

α-Synuclein Aggregates with β-Amyloid or Tau in Human Red Blood Cells: Correlation with Antioxidant Capability and Physical Exercise in Human Healthy Subjects

Author keywords

Antioxidant capability; Neurodegenerative diseases; Physical exercise; Protein misfolding; Tau; Synuclein; Synuclein heterocomplexes; Amyloid

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; TAU PROTEIN; AMYLOID BETA-PROTEIN (1-42); ANTIOXIDANT; BIOLOGICAL MARKER; PEPTIDE FRAGMENT; PROTEIN AGGREGATE;

EID: 85017589309     PISSN: 08937648     EISSN: 15591182     Source Type: Journal    
DOI: 10.1007/s12035-017-0523-5     Document Type: Article
Times cited : (31)

References (98)
  • 1
    • 84978864589 scopus 로고    scopus 로고
    • The role of oxidative stress in neurodegenerative diseases
    • PID: 26713080
    • Kim GH, Kim JE, Rhie SJ, Yoon S (2015) The role of oxidative stress in neurodegenerative diseases. Exp Neurobiol 24:325–340
    • (2015) Exp Neurobiol , vol.24 , pp. 325-340
    • Kim, G.H.1    Kim, J.E.2    Rhie, S.J.3    Yoon, S.4
  • 2
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • COI: 1:CAS:528:DC%2BD28XhtVyktbbO, PID: 17051205
    • Lin MT, Beal MF (2006) Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443:787–795
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 3
    • 84862297475 scopus 로고    scopus 로고
    • Mechanism of oxidative stress in neurodegeneration
    • Gandhi S, Abramov AY (2012) Mechanism of oxidative stress in neurodegeneration. Oxidative Med Cell Longev. doi:10.1155/2012/428010
    • (2012) Oxidative Med Cell Longev
    • Gandhi, S.1    Abramov, A.Y.2
  • 4
    • 33747173091 scopus 로고    scopus 로고
    • Protein carbonylation, cellular dysfunction, and disease progression
    • COI: 1:CAS:528:DC%2BD2sXlvFCltb0%3D, PID: 16796807
    • Dalle-Donne I, Aldini G, Carini M, Colombo R, Rossi R, Milzani A (2006) Protein carbonylation, cellular dysfunction, and disease progression. J Cell Mol Med 10:389–406
    • (2006) J Cell Mol Med , vol.10 , pp. 389-406
    • Dalle-Donne, I.1    Aldini, G.2    Carini, M.3    Colombo, R.4    Rossi, R.5    Milzani, A.6
  • 5
    • 2542455537 scopus 로고    scopus 로고
    • Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimer's disease
    • COI: 1:CAS:528:DC%2BD2cXksVGgt7o%3D, PID: 15172732
    • Klein WL, Stine WB, Teplow DB (2004) Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimer's disease. Neurobiol Aging 25:569–580
    • (2004) Neurobiol Aging , vol.25 , pp. 569-580
    • Klein, W.L.1    Stine, W.B.2    Teplow, D.B.3
  • 6
    • 84990246592 scopus 로고    scopus 로고
    • Pathogenic mechanisms of prion protein, amyloid-β and α-synuclein misfolding: the prion concept and neurotoxicity of protein oligomers
    • COI: 1:CAS:528:DC%2BC28Xhtlequ73N, PID: 27529376
    • Ugalde CL, Finkelstein DI, Lawson VA, Hill AF (2016) Pathogenic mechanisms of prion protein, amyloid-β and α-synuclein misfolding: the prion concept and neurotoxicity of protein oligomers. J Neurochem 139:162–180
    • (2016) J Neurochem , vol.139 , pp. 162-180
    • Ugalde, C.L.1    Finkelstein, D.I.2    Lawson, V.A.3    Hill, A.F.4
  • 8
    • 0030981585 scopus 로고    scopus 로고
    • Auguste D and Alzheimer's disease
    • COI: 1:STN:280:DyaK2szhtVejtQ%3D%3D, PID: 9167474
    • Maurer K, Volk S, Gerbaldo H (1997) Auguste D and Alzheimer's disease. Lancet 349:1546–1549
    • (1997) Lancet , vol.349 , pp. 1546-1549
    • Maurer, K.1    Volk, S.2    Gerbaldo, H.3
  • 11
    • 84859928720 scopus 로고    scopus 로고
    • Examining the mechanisms that link β-amyloid and α-synuclein pathologies
    • COI: 1:CAS:528:DC%2BC38Xnt1Ohtbk%3D, PID: 22546279
    • Marsh SE, Blurton-Jones M (2012) Examining the mechanisms that link β-amyloid and α-synuclein pathologies. Alzheimers Res Ther 4:11
    • (2012) Alzheimers Res Ther , vol.4 , pp. 11
    • Marsh, S.E.1    Blurton-Jones, M.2
  • 12
    • 0036827419 scopus 로고    scopus 로고
    • Emerging Alzheimer's disease therapies: focusing on the future
    • PID: 12470793
    • Trojanowski JQ (2002) Emerging Alzheimer's disease therapies: focusing on the future. Neurobiol Aging 23:985–990
    • (2002) Neurobiol Aging , vol.23 , pp. 985-990
    • Trojanowski, J.Q.1
  • 13
    • 1342321775 scopus 로고    scopus 로고
    • More than just two peas in a pod: common amyloidogenic properties of tau and alpha-synuclein in neurodegenerative diseases
    • COI: 1:CAS:528:DC%2BD2cXhsV2msrY%3D, PID: 15036877
    • Lee VM, Giasson BI, Trojanowski JQ (2004) More than just two peas in a pod: common amyloidogenic properties of tau and alpha-synuclein in neurodegenerative diseases. Trends Neurosci 27:129–134
    • (2004) Trends Neurosci , vol.27 , pp. 129-134
    • Lee, V.M.1    Giasson, B.I.2    Trojanowski, J.Q.3
  • 14
    • 33748584602 scopus 로고    scopus 로고
    • Interaction between Abeta peptide and alpha synuclein: molecular mechanisms in overlapping pathology of Alzheimer's and Parkinson's in dementia with Lewy body disease
    • COI: 1:CAS:528:DC%2BD28XptlSmtLs%3D, PID: 16947080
    • Mandal PK, Pettegrew JW, Masliah E, Hamilton RL, Mandal R (2006) Interaction between Abeta peptide and alpha synuclein: molecular mechanisms in overlapping pathology of Alzheimer's and Parkinson's in dementia with Lewy body disease. Neurochem Res 31:1153–1162
    • (2006) Neurochem Res , vol.31 , pp. 1153-1162
    • Mandal, P.K.1    Pettegrew, J.W.2    Masliah, E.3    Hamilton, R.L.4    Mandal, R.5
  • 16
    • 22144442365 scopus 로고    scopus 로고
    • Interaction between tau and alpha-synuclein proteins is impaired in the presence of P301L tau mutation
    • COI: 1:CAS:528:DC%2BD2MXmt1ejt7s%3D, PID: 15904919
    • Benussi L, Ghidoni R, Paterlini A, Nicosia F, Alberici AC, Signorini S, Barbiero L, Binetti G (2005) Interaction between tau and alpha-synuclein proteins is impaired in the presence of P301L tau mutation. Exp Cell Res 308:78–84
    • (2005) Exp Cell Res , vol.308 , pp. 78-84
    • Benussi, L.1    Ghidoni, R.2    Paterlini, A.3    Nicosia, F.4    Alberici, A.C.5    Signorini, S.6    Barbiero, L.7    Binetti, G.8
  • 19
    • 0033520474 scopus 로고    scopus 로고
    • Alpha-synuclein binds to Tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356
    • COI: 1:CAS:528:DyaK1MXmtVWiu70%3D, PID: 10464279
    • Jensen PH, Hager H, Nielsen MS, Hojrup P, Gliemann J, Jakes R (1999) Alpha-synuclein binds to Tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356. J Biol Chem 274:25481–25489
    • (1999) J Biol Chem , vol.274 , pp. 25481-25489
    • Jensen, P.H.1    Hager, H.2    Nielsen, M.S.3    Hojrup, P.4    Gliemann, J.5    Jakes, R.6
  • 20
    • 0032991227 scopus 로고    scopus 로고
    • Biomarkers of Alzheimer disease
    • COI: 1:STN:280:DyaK1M3gsFSqsA%3D%3D, PID: 10190817
    • Growdon JH (1999) Biomarkers of Alzheimer disease. Arch Neurol 56:281–283
    • (1999) Arch Neurol , vol.56 , pp. 281-283
    • Growdon, J.H.1
  • 21
    • 0033599707 scopus 로고    scopus 로고
    • Soluble interleukin-1 receptor type II levels are elevated in cerebrospinal fluid in Alzheimer's disease patients
    • COI: 1:CAS:528:DyaK1MXisV2gs7Y%3D, PID: 10216202
    • Garlind A, Brauner A, Höjeberg B, Basun H, Schultzberg M (1999) Soluble interleukin-1 receptor type II levels are elevated in cerebrospinal fluid in Alzheimer's disease patients. Brain Res 826:112–116
    • (1999) Brain Res , vol.826 , pp. 112-116
    • Garlind, A.1    Brauner, A.2    Höjeberg, B.3    Basun, H.4    Schultzberg, M.5
  • 22
    • 0034705173 scopus 로고    scopus 로고
    • Increased CSF levels of nerve growth factor in patients with Alzheimer's disease
    • COI: 1:CAS:528:DC%2BD3cXktVOlu74%3D, PID: 10822447
    • Hock C, Heese K, Müller-Spahn F, Huber P, Riesen W, Nitsch RM, Otten U (2000) Increased CSF levels of nerve growth factor in patients with Alzheimer's disease. Neurology 54:2009–2011
    • (2000) Neurology , vol.54 , pp. 2009-2011
    • Hock, C.1    Heese, K.2    Müller-Spahn, F.3    Huber, P.4    Riesen, W.5    Nitsch, R.M.6    Otten, U.7
  • 23
    • 0035066999 scopus 로고    scopus 로고
    • Tracking of Alzheimer's disease progression with cerebrospinal fluid tau protein phosphorylated at threonine 231
    • COI: 1:STN:280:DC%2BD3M3hvVyrtw%3D%3D, PID: 11310639
    • Hampel H, Buerger K, Kohnken R, Teipel SJ, Zinkowski R, Moeller HJ, Rapoport SI, Davies P (2001) Tracking of Alzheimer's disease progression with cerebrospinal fluid tau protein phosphorylated at threonine 231. Ann Neurol 49:545–546
    • (2001) Ann Neurol , vol.49 , pp. 545-546
    • Hampel, H.1    Buerger, K.2    Kohnken, R.3    Teipel, S.J.4    Zinkowski, R.5    Moeller, H.J.6    Rapoport, S.I.7    Davies, P.8
  • 24
    • 0035108753 scopus 로고    scopus 로고
    • Evaluation of CSF-tau and CSF-Abeta42 as diagnostic markers for Alzheimer disease in clinical practice
    • COI: 1:STN:280:DC%2BD3M7pvVCjuw%3D%3D, PID: 11255440
    • Andreasen N, Minthon L, Davidsson P, Vanmechelen E, Vanderstichele H, Winblad B, Blennow K (2001) Evaluation of CSF-tau and CSF-Abeta42 as diagnostic markers for Alzheimer disease in clinical practice. Arch Neurol 58:373–379
    • (2001) Arch Neurol , vol.58 , pp. 373-379
    • Andreasen, N.1    Minthon, L.2    Davidsson, P.3    Vanmechelen, E.4    Vanderstichele, H.5    Winblad, B.6    Blennow, K.7
  • 25
    • 0142257913 scopus 로고    scopus 로고
    • Proteins in cerebrospinal fluid and blood: barriers, CSF flow rate and source-related dynamics
    • COI: 1:CAS:528:DC%2BD3sXns1Kgs7c%3D, PID: 14530572
    • Reiber H (2003) Proteins in cerebrospinal fluid and blood: barriers, CSF flow rate and source-related dynamics. Restor Neurol Neurosci 21:79–96
    • (2003) Restor Neurol Neurosci , vol.21 , pp. 79-96
    • Reiber, H.1
  • 26
    • 84863248390 scopus 로고    scopus 로고
    • Oxidative stress in neurodegenerative diseases
    • COI: 1:CAS:528:DC%2BC38XmvVeiu7g%3D, PID: 25774178
    • Chen X, Guo C, Kong J (2012) Oxidative stress in neurodegenerative diseases. Neural Regen Res 7:376–385
    • (2012) Neural Regen Res , vol.7 , pp. 376-385
    • Chen, X.1    Guo, C.2    Kong, J.3
  • 27
    • 0037157533 scopus 로고    scopus 로고
    • Defining neurodegenerative diseases
    • PID: 12077015
    • Williams A (2002) Defining neurodegenerative diseases. BMJ 324:1465–1466
    • (2002) BMJ , vol.324 , pp. 1465-1466
    • Williams, A.1
  • 28
    • 77956216928 scopus 로고    scopus 로고
    • Reactive oxygen species: stuck in the middle of neurodegeneration
    • PID: 20421690
    • Patten DA, Germain M, Kelly MA, Slack RS (2010) Reactive oxygen species: stuck in the middle of neurodegeneration. J Alzheimers Dis 20(Suppl 2):S357–S367
    • (2010) J Alzheimers Dis , vol.20 , pp. S357-S367
    • Patten, D.A.1    Germain, M.2    Kelly, M.A.3    Slack, R.S.4
  • 29
    • 79955664287 scopus 로고    scopus 로고
    • Oxidative stress treatment for clinical trials in neurodegenerative diseases
    • COI: 1:CAS:528:DC%2BC3MXltFGrtrY%3D, PID: 21422516
    • Ienco EC, LoGerfo A, Carlesi C, Orsucci D, Ricci G, Mancuso M, Siciliano G (2011) Oxidative stress treatment for clinical trials in neurodegenerative diseases. J Alzheimers Dis 24(Suppl 2):111–126
    • (2011) J Alzheimers Dis , vol.24 , pp. 111-126
    • Ienco, E.C.1    LoGerfo, A.2    Carlesi, C.3    Orsucci, D.4    Ricci, G.5    Mancuso, M.6    Siciliano, G.7
  • 30
    • 79955646829 scopus 로고    scopus 로고
    • Brain mitochondrial dysfunction in aging, neurodegeneration, and Parkinson's disease
    • PID: 20890446
    • Navarro A, Boveris A (2010) Brain mitochondrial dysfunction in aging, neurodegeneration, and Parkinson's disease. Front Aging Neurosci. doi:10.3389/fnagi.2010.00034
    • (2010) Front Aging Neurosci
    • Navarro, A.1    Boveris, A.2
  • 31
    • 77955965172 scopus 로고    scopus 로고
    • Cellular stress responses: cell survival and cell death
    • Fulda S, Gorman AM, Hori O, Samali A (2010) Cellular stress responses: cell survival and cell death. Int J Cell Biol. doi:10.1155/2010/214074
    • (2010) Int J Cell Biol
    • Fulda, S.1    Gorman, A.M.2    Hori, O.3    Samali, A.4
  • 32
    • 0028068186 scopus 로고
    • Free radicals, antioxidants, and human disease: curiosity, cause, or consequence?
    • COI: 1:CAS:528:DyaK2cXmsFamurg%3D, PID: 7915779
    • Halliwell B (1994) Free radicals, antioxidants, and human disease: curiosity, cause, or consequence? Lancet 344:721–724
    • (1994) Lancet , vol.344 , pp. 721-724
    • Halliwell, B.1
  • 33
    • 84864934604 scopus 로고    scopus 로고
    • Antioxidant therapies for Alzheimer's disease
    • Feng Y, Wang X (2012) Antioxidant therapies for Alzheimer's disease. Oxidative Med Cell Longev. doi:10.1155/2012/472932
    • (2012) Oxidative Med Cell Longev
    • Feng, Y.1    Wang, X.2
  • 34
    • 84988833531 scopus 로고    scopus 로고
    • Antioxidants as a preventive therapeutic option for age related neurodegenerative diseases
    • Singh S (2015) Antioxidants as a preventive therapeutic option for age related neurodegenerative diseases. Ther Targets Neurol Dis. doi:10.14800/ttnd.592
    • (2015) Ther Targets Neurol Dis
    • Singh, S.1
  • 35
    • 33645299025 scopus 로고    scopus 로고
    • Ageing and neuronal vulnerability
    • COI: 1:CAS:528:DC%2BD28Xis1GksrY%3D, PID: 16552414
    • Mattson MP, Magnus T (2006) Ageing and neuronal vulnerability. Nat Rev Neurosci 7:278–294
    • (2006) Nat Rev Neurosci , vol.7 , pp. 278-294
    • Mattson, M.P.1    Magnus, T.2
  • 36
    • 84980413704 scopus 로고    scopus 로고
    • Physical exercise, reactive oxygen species and neuroprotection
    • COI: 1:CAS:528:DC%2BC28XhvVOjtb0%3D, PID: 26828019
    • Radak Z, Suzuki K, Higuchi M, Balogh L, Boldogh I, Koltai E (2016) Physical exercise, reactive oxygen species and neuroprotection. Free Radic Biol Med 98:187–196
    • (2016) Free Radic Biol Med , vol.98 , pp. 187-196
    • Radak, Z.1    Suzuki, K.2    Higuchi, M.3    Balogh, L.4    Boldogh, I.5    Koltai, E.6
  • 37
    • 84884502539 scopus 로고    scopus 로고
    • Bridging animal and human models of exercise-induced brain plasticity
    • PID: 24029446
    • Voss MW, Vivar C, Kramer AF, van Praag H (2013) Bridging animal and human models of exercise-induced brain plasticity. Trends Cogn Sci 17:525–544
    • (2013) Trends Cogn Sci , vol.17 , pp. 525-544
    • Voss, M.W.1    Vivar, C.2    Kramer, A.F.3    van Praag, H.4
  • 38
    • 84894122899 scopus 로고    scopus 로고
    • Human neuromuscular structure and function in old age: a brief review
    • PID: 27011872
    • Power GA, Dalton BH, Rice CL (2013) Human neuromuscular structure and function in old age: a brief review. J Sport Health Sci 2:215–226
    • (2013) J Sport Health Sci , vol.2 , pp. 215-226
    • Power, G.A.1    Dalton, B.H.2    Rice, C.L.3
  • 39
    • 0041659266 scopus 로고    scopus 로고
    • Exercise-induced changes in hippocampal brain-derived neurotrophic factor and neurotrophin-3: effects of rat strain
    • COI: 1:CAS:528:DC%2BD3sXmt1aitr4%3D, PID: 12914971
    • Johnson RA, Mitchell GS (2003) Exercise-induced changes in hippocampal brain-derived neurotrophic factor and neurotrophin-3: effects of rat strain. Brain Res 983:108–114
    • (2003) Brain Res , vol.983 , pp. 108-114
    • Johnson, R.A.1    Mitchell, G.S.2
  • 40
    • 20044377403 scopus 로고    scopus 로고
    • Environmental enrichment reduces Abeta levels and amyloid deposition in transgenic mice
    • COI: 1:CAS:528:DC%2BD2MXis1yhtr4%3D, PID: 15766532
    • Lazarov O, Robinson J, Tang YP, Hairston IS, Korade-Mirnics Z, Lee VM et al (2005) Environmental enrichment reduces Abeta levels and amyloid deposition in transgenic mice. Cell 120:701–713
    • (2005) Cell , vol.120 , pp. 701-713
    • Lazarov, O.1    Robinson, J.2    Tang, Y.P.3    Hairston, I.S.4    Korade-Mirnics, Z.5    Lee, V.M.6
  • 41
    • 84955677869 scopus 로고    scopus 로고
    • Voluntary running attenuates memory loss, decreases neuropathological changes and induces neurogenesis in a mouse model of Alzheimer's disease
    • COI: 1:CAS:528:DC%2BC28XhvVOqsw%3D%3D, PID: 25763997
    • Tapia-Rojas C, Aranguiz F, Varela-Nallar L, Inestrosa NC (2016) Voluntary running attenuates memory loss, decreases neuropathological changes and induces neurogenesis in a mouse model of Alzheimer's disease. Brain Pathol 26:62–74
    • (2016) Brain Pathol , vol.26 , pp. 62-74
    • Tapia-Rojas, C.1    Aranguiz, F.2    Varela-Nallar, L.3    Inestrosa, N.C.4
  • 42
    • 84881155436 scopus 로고    scopus 로고
    • Physical activity and amyloid-β plasma and brain levels: results from the Australian imaging, biomarkers and lifestyle study of ageing
    • COI: 1:CAS:528:DC%2BC3sXht1SlsbjJ, PID: 22889922
    • Brown BM, Peiffer JJ, Taddei K, Lui JK, Laws SM, Gupta VB et al (2013) Physical activity and amyloid-β plasma and brain levels: results from the Australian imaging, biomarkers and lifestyle study of ageing. Mol Psychiatry 18:875–881
    • (2013) Mol Psychiatry , vol.18 , pp. 875-881
    • Brown, B.M.1    Peiffer, J.J.2    Taddei, K.3    Lui, J.K.4    Laws, S.M.5    Gupta, V.B.6
  • 43
    • 80052669106 scopus 로고    scopus 로고
    • Neurodegenerative diseases: exercising toward neurogenesis and neuroregeneration
    • PID: 20725635
    • Ang ET, Tai YK, Lo SQ, Seet R, Soong TW (2010) Neurodegenerative diseases: exercising toward neurogenesis and neuroregeneration. Front Aging Neurosci. doi:10.3389/fnagi.2010.00025
    • (2010) Front Aging Neurosci
    • Ang, E.T.1    Tai, Y.K.2    Lo, S.Q.3    Seet, R.4    Soong, T.W.5
  • 44
    • 77953445792 scopus 로고    scopus 로고
    • Markers of oxidative stress in erythrocytes and plasma during aging in humans
    • Pandey KB, Rizvi SI (2010) Markers of oxidative stress in erythrocytes and plasma during aging in humans. Oxidative Med Cell Longev 3:2–12
    • (2010) Oxidative Med Cell Longev , vol.3 , pp. 2-12
    • Pandey, K.B.1    Rizvi, S.I.2
  • 45
    • 84930642027 scopus 로고    scopus 로고
    • Detection of α-synuclein oligomers in red blood cells as a potential biomarker of Parkinson's disease
    • COI: 1:CAS:528:DC%2BC2MXos1emur8%3D, PID: 25998655
    • Wang X, Yu S, Li F, Feng T (2015) Detection of α-synuclein oligomers in red blood cells as a potential biomarker of Parkinson's disease. Neurosci Lett 599:115–119
    • (2015) Neurosci Lett , vol.599 , pp. 115-119
    • Wang, X.1    Yu, S.2    Li, F.3    Feng, T.4
  • 48
    • 0020410785 scopus 로고
    • Psychophysical bases of perceived exertion
    • COI: 1:STN:280:DyaL3s7hsVChsw%3D%3D, PID: 7154893
    • Borg GA (1982) Psychophysical bases of perceived exertion. Med Sci Sports Exerc 14:377–381
    • (1982) Med Sci Sports Exerc , vol.14 , pp. 377-381
    • Borg, G.A.1
  • 49
    • 0031437331 scopus 로고    scopus 로고
    • The psychophysical and heart rate relationship between treadmill and deep-water running
    • PID: 11676696
    • Hamer P, Slocombe B (1997) The psychophysical and heart rate relationship between treadmill and deep-water running. Aust J Physiother 43:265–271
    • (1997) Aust J Physiother , vol.43 , pp. 265-271
    • Hamer, P.1    Slocombe, B.2
  • 51
    • 82655171636 scopus 로고    scopus 로고
    • Phosphorylated α-synuclein can be detected in blood plasma and is potentially a useful biomarker for Parkinson's disease
    • COI: 1:CAS:528:DC%2BC3MXhs1Wlt73E, PID: 21865317
    • Foulds PG, Mitchell JD, Parker A, Turner R, Green G, Diggle P et al (2011) Phosphorylated α-synuclein can be detected in blood plasma and is potentially a useful biomarker for Parkinson's disease. FASEB J 25:4127–4137
    • (2011) FASEB J , vol.25 , pp. 4127-4137
    • Foulds, P.G.1    Mitchell, J.D.2    Parker, A.3    Turner, R.4    Green, G.5    Diggle, P.6
  • 52
    • 33645833848 scopus 로고    scopus 로고
    • Detection of oligomeric forms of alpha-synuclein protein in human plasma as a potential biomarker for Parkinson's disease
    • COI: 1:CAS:528:DC%2BD28Xis1Wlu70%3D, PID: 16507759
    • El-Agnaf OM, Salem SA, Paleologou KE, Curran MD, Gibson MJ, Court JA et al (2006) Detection of oligomeric forms of alpha-synuclein protein in human plasma as a potential biomarker for Parkinson's disease. FASEB J 20:419–425
    • (2006) FASEB J , vol.20 , pp. 419-425
    • El-Agnaf, O.M.1    Salem, S.A.2    Paleologou, K.E.3    Curran, M.D.4    Gibson, M.J.5    Court, J.A.6
  • 54
    • 84898651980 scopus 로고    scopus 로고
    • A rapid and efficient immunoenzymatic assay to detect receptor protein interactions: G protein-coupled receptors
    • COI: 1:CAS:528:DC%2BC2cXhtlWlur7O, PID: 24733071
    • Zappelli E, Daniele S, Abbracchio MP, Martini C, Trincavelli ML (2014) A rapid and efficient immunoenzymatic assay to detect receptor protein interactions: G protein-coupled receptors. Int J Mol Sci 15:6252–6264
    • (2014) Int J Mol Sci , vol.15 , pp. 6252-6264
    • Zappelli, E.1    Daniele, S.2    Abbracchio, M.P.3    Martini, C.4    Trincavelli, M.L.5
  • 55
    • 84899080685 scopus 로고    scopus 로고
    • Apoptosis therapy in cancer: the first single-molecule co-activating p53 and the translocator protein in glioblastoma
    • PID: 24756113
    • Daniele S, Taliani S, Da Pozzo E, Giacomelli C, Costa B, Trincavelli ML et al (2014) Apoptosis therapy in cancer: the first single-molecule co-activating p53 and the translocator protein in glioblastoma. Sci Rep 4:4749
    • (2014) Sci Rep , vol.4 , pp. 4749
    • Daniele, S.1    Taliani, S.2    Da Pozzo, E.3    Giacomelli, C.4    Costa, B.5    Trincavelli, M.L.6
  • 56
    • 0031974341 scopus 로고    scopus 로고
    • A rapid gas chromatographic assay for determining oxyradical scavenging capacity of antioxidants and biological fluids
    • COI: 1:CAS:528:DyaK2sXotVSju70%3D, PID: 9438561
    • Winston GW, Regoli F, Dugas AJ, Fong JH, Blanchard KA (1998) A rapid gas chromatographic assay for determining oxyradical scavenging capacity of antioxidants and biological fluids. Free Radic Biol Med 24:480–493
    • (1998) Free Radic Biol Med , vol.24 , pp. 480-493
    • Winston, G.W.1    Regoli, F.2    Dugas, A.J.3    Fong, J.H.4    Blanchard, K.A.5
  • 57
    • 0032971525 scopus 로고    scopus 로고
    • Quantification of total oxidant scavenging capacity of antioxidants for peroxynitrite, peroxyl radicals, and hydroxyl radicals
    • COI: 1:CAS:528:DyaK1MXit1yktLc%3D, PID: 10198274
    • Regoli F, Winston GW (1999) Quantification of total oxidant scavenging capacity of antioxidants for peroxynitrite, peroxyl radicals, and hydroxyl radicals. Toxicol Appl Pharmacol 156:96–105
    • (1999) Toxicol Appl Pharmacol , vol.156 , pp. 96-105
    • Regoli, F.1    Winston, G.W.2
  • 58
    • 20144387438 scopus 로고    scopus 로고
    • Physical activity, plasma antioxidant capacity, and endothelium-dependent vasodilation in young and older men
    • COI: 1:CAS:528:DC%2BD2MXjtlags7w%3D, PID: 15831361
    • Franzoni F, Ghiadoni L, Galetta F, Plantinga Y, Lubrano V, Huang Y et al (2005) Physical activity, plasma antioxidant capacity, and endothelium-dependent vasodilation in young and older men. Am J Hypertens 18:510–516
    • (2005) Am J Hypertens , vol.18 , pp. 510-516
    • Franzoni, F.1    Ghiadoni, L.2    Galetta, F.3    Plantinga, Y.4    Lubrano, V.5    Huang, Y.6
  • 59
    • 84970015774 scopus 로고    scopus 로고
    • Effects of recombinant human erythropoietin high mimicking abuse doses on oxidative stress processes in rats
    • COI: 1:CAS:528:DC%2BC28XptFekt7g%3D, PID: 27470373
    • Bianchi S, Fusi J, Franzoni F, Giovannini L, Galetta F, Mannari C et al (2016) Effects of recombinant human erythropoietin high mimicking abuse doses on oxidative stress processes in rats. Biomed Pharmacother 82:355–363
    • (2016) Biomed Pharmacother , vol.82 , pp. 355-363
    • Bianchi, S.1    Fusi, J.2    Franzoni, F.3    Giovannini, L.4    Galetta, F.5    Mannari, C.6
  • 60
    • 33749049965 scopus 로고    scopus 로고
    • An in vitro study on the free radical scavenging capacity of ergothioneine: comparison with reduced glutathione, uric acid and trolox
    • COI: 1:CAS:528:DC%2BD28XhtVagtLfN, PID: 16930933
    • Franzoni F, Colognato R, Galetta F, Laurenza I, Barsotti M, Di Stefano R et al (2006) An in vitro study on the free radical scavenging capacity of ergothioneine: comparison with reduced glutathione, uric acid and trolox. Biomed Pharmacother 60:453–457
    • (2006) Biomed Pharmacother , vol.60 , pp. 453-457
    • Franzoni, F.1    Colognato, R.2    Galetta, F.3    Laurenza, I.4    Barsotti, M.5    Di Stefano, R.6
  • 61
    • 85041355755 scopus 로고    scopus 로고
    • Non-denaturing purification of alpha-Synuclein from erythrocytes
    • Bartels T, Choi J, Kim N, Selkoe D (2011) Non-denaturing purification of alpha-Synuclein from erythrocytes. Protoc Exch. doi:10.1038/protex.2011.254
    • (2011) Protoc Exch
    • Bartels, T.1    Choi, J.2    Kim, N.3    Selkoe, D.4
  • 63
    • 69249239132 scopus 로고    scopus 로고
    • Antiparallel beta-sheet: a signature structure of the oligomeric amyloid beta-peptide
    • COI: 1:CAS:528:DC%2BD1MXosV2hu74%3D, PID: 19435461
    • Cerf E, Sarroukh R, Tamamizu-Kato S, Breydo L, Derclaye S, Dufrêne YF et al (2009) Antiparallel beta-sheet: a signature structure of the oligomeric amyloid beta-peptide. Biochem J 421:415–423
    • (2009) Biochem J , vol.421 , pp. 415-423
    • Cerf, E.1    Sarroukh, R.2    Tamamizu-Kato, S.3    Breydo, L.4    Derclaye, S.5    Dufrêne, Y.F.6
  • 64
    • 84940063508 scopus 로고    scopus 로고
    • Prion-protein-interacting amyloid-β oligomers of high molecular weight are tightly correlated with memory impairment in multiple Alzheimer mouse models
    • COI: 1:CAS:528:DC%2BC2MXhtFGns7rO, PID: 26018073
    • Kostylev MA, Kaufman AC, Nygaard HB, Patel P, Haas LT, Gunther EC et al (2015) Prion-protein-interacting amyloid-β oligomers of high molecular weight are tightly correlated with memory impairment in multiple Alzheimer mouse models. J Biol Chem 290:17415–17438
    • (2015) J Biol Chem , vol.290 , pp. 17415-17438
    • Kostylev, M.A.1    Kaufman, A.C.2    Nygaard, H.B.3    Patel, P.4    Haas, L.T.5    Gunther, E.C.6
  • 65
    • 84915747184 scopus 로고    scopus 로고
    • Disruption of amyloid plaques integrity affects the soluble oligomers content from Alzheimer disease brains
    • PID: 25485545
    • Jimenez S, Navarro V, Moyano J, Sanchez-Mico M, Torres M, Davila JC et al (2014) Disruption of amyloid plaques integrity affects the soluble oligomers content from Alzheimer disease brains. PLoS One 9(12):e114041
    • (2014) PLoS One , vol.9 , Issue.12
    • Jimenez, S.1    Navarro, V.2    Moyano, J.3    Sanchez-Mico, M.4    Torres, M.5    Davila, J.C.6
  • 66
    • 37849028683 scopus 로고    scopus 로고
    • Red blood cells are the major source of alpha-synuclein in blood
    • COI: 1:CAS:528:DC%2BD1cXhsFyqtLo%3D, PID: 18182779
    • Barbour R, Kling K, Anderson JP, Banducci K, Cole T, Diep L et al (2008) Red blood cells are the major source of alpha-synuclein in blood. Neurodegener Dis 5:55–59
    • (2008) Neurodegener Dis , vol.5 , pp. 55-59
    • Barbour, R.1    Kling, K.2    Anderson, J.P.3    Banducci, K.4    Cole, T.5    Diep, L.6
  • 68
    • 33646091514 scopus 로고    scopus 로고
    • Low molecular weight species of tau in Alzheimer's disease are dependent on tau phosphorylation sites but not on delayed post-mortem delay in tissue processing
    • COI: 1:CAS:528:DC%2BD28XjvFShurw%3D, PID: 16488541
    • Santpere G, Puig B, Ferrer I (2006) Low molecular weight species of tau in Alzheimer's disease are dependent on tau phosphorylation sites but not on delayed post-mortem delay in tissue processing. Neurosci Lett 399:106–110
    • (2006) Neurosci Lett , vol.399 , pp. 106-110
    • Santpere, G.1    Puig, B.2    Ferrer, I.3
  • 69
    • 22844453232 scopus 로고    scopus 로고
    • Assessment of total antioxidant capacity in human plasma
    • Goraca A (2004) Assessment of total antioxidant capacity in human plasma. Folia Med (Plovdiv) 46:16–21
    • (2004) Folia Med (Plovdiv) , vol.46 , pp. 16-21
    • Goraca, A.1
  • 70
    • 84979263294 scopus 로고    scopus 로고
    • APOE genotype and stress response—a mini review
    • PID: 27457486
    • Dose J, Huebbe P, Nebel A, Rimbach G (2016) APOE genotype and stress response—a mini review. Lipids Health Dis 15:121
    • (2016) Lipids Health Dis , vol.15 , pp. 121
    • Dose, J.1    Huebbe, P.2    Nebel, A.3    Rimbach, G.4
  • 71
    • 77954033257 scopus 로고    scopus 로고
    • Amyloid imaging results from the Australian Imaging, Biomarkers and Lifestyle (AIBL) study of aging
    • PID: 20472326
    • Rowe CC, Ellis KA, Rimajova M, Bourgeat P, Pike KE, Jones G et al (2010) Amyloid imaging results from the Australian Imaging, Biomarkers and Lifestyle (AIBL) study of aging. Neurobiol Aging 31:1275–1283
    • (2010) Neurobiol Aging , vol.31 , pp. 1275-1283
    • Rowe, C.C.1    Ellis, K.A.2    Rimajova, M.3    Bourgeat, P.4    Pike, K.E.5    Jones, G.6
  • 72
    • 84859482874 scopus 로고    scopus 로고
    • Exercise engagement as a moderator of the effects of APOE genotype on amyloid deposition
    • PID: 22232206
    • Head D, Bugg JM, Goate AM, Fagan AM, Mintun MA, Benzinger T et al (2012) Exercise engagement as a moderator of the effects of APOE genotype on amyloid deposition. Arch Neurol 69:636–643
    • (2012) Arch Neurol , vol.69 , pp. 636-643
    • Head, D.1    Bugg, J.M.2    Goate, A.M.3    Fagan, A.M.4    Mintun, M.A.5    Benzinger, T.6
  • 73
    • 84881525560 scopus 로고    scopus 로고
    • Oxidative stress and the pathogenesis of Alzheimer's disease
    • Zhao Y, Zhao B (2013) Oxidative stress and the pathogenesis of Alzheimer's disease. Oxidative Med Cell Longev. doi:10.1155/2013/316523
    • (2013) Oxidative Med Cell Longev
    • Zhao, Y.1    Zhao, B.2
  • 75
    • 77957285061 scopus 로고    scopus 로고
    • Early noninvasive diagnosis of neurodegenerative diseases
    • Danev SI, St Stoyanov D (2010) Early noninvasive diagnosis of neurodegenerative diseases. Folia Med (Plovdiv) 52:5–13
    • (2010) Folia Med (Plovdiv) , vol.52 , pp. 5-13
    • Danev, S.I.1    St Stoyanov, D.2
  • 76
    • 67349184808 scopus 로고    scopus 로고
    • Neuropathology of nondemented aging: presumptive evidence for preclinical Alzheimer disease
    • PID: 19376612
    • Price JL, McKeel DW, Buckles VD, Roe CM, Xiong C, Grundman M et al (2009) Neuropathology of nondemented aging: presumptive evidence for preclinical Alzheimer disease. Neurobiol Aging 30:1026–1036
    • (2009) Neurobiol Aging , vol.30 , pp. 1026-1036
    • Price, J.L.1    McKeel, D.W.2    Buckles, V.D.3    Roe, C.M.4    Xiong, C.5    Grundman, M.6
  • 77
    • 3242769758 scopus 로고    scopus 로고
    • Influence of genetic variants in UGT1A1 and UGT1A9 on the in vivo glucuronidation of SN-38
    • COI: 1:CAS:528:DC%2BD2cXmslGqtLg%3D, PID: 15286088
    • Paoluzzi L, Singh AS, Price DK, Danesi R, Mathijssen RH, Verweij J et al (2004) Influence of genetic variants in UGT1A1 and UGT1A9 on the in vivo glucuronidation of SN-38. J Clin Pharmacol 44:854–860
    • (2004) J Clin Pharmacol , vol.44 , pp. 854-860
    • Paoluzzi, L.1    Singh, A.S.2    Price, D.K.3    Danesi, R.4    Mathijssen, R.H.5    Verweij, J.6
  • 78
    • 84869109864 scopus 로고    scopus 로고
    • Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice
    • COI: 1:CAS:528:DC%2BC38Xhs1GntL7L, PID: 23161999
    • Luk KC, Kehm V, Carroll J, Zhang B, O'Brien P, Trojanowski JQ et al (2012) Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science 338:949–953
    • (2012) Science , vol.338 , pp. 949-953
    • Luk, K.C.1    Kehm, V.2    Carroll, J.3    Zhang, B.4    O'Brien, P.5    Trojanowski, J.Q.6
  • 79
    • 33747878233 scopus 로고    scopus 로고
    • Very long term studies of the seeding of beta-amyloidosis in primates
    • COI: 1:CAS:528:DC%2BD28XosleqsLo%3D
    • Ridley RM, Baker HF, Windle CP, Cummings RM (2006) Very long term studies of the seeding of beta-amyloidosis in primates. J Neural Transm (Vienna) 113:1243–1251
    • (2006) J Neural Transm (Vienna) , vol.113 , pp. 1243-1251
    • Ridley, R.M.1    Baker, H.F.2    Windle, C.P.3    Cummings, R.M.4
  • 80
    • 0035863055 scopus 로고    scopus 로고
    • Age-dependent changes in brain, CSF, and plasma amyloid (beta) protein in the Tg2576 transgenic mouse model of Alzheimer's disease
    • COI: 1:CAS:528:DC%2BD3MXnslCguw%3D%3D, PID: 11160418
    • Kawarabayashi T, Younkin LH, Saido TC, Shoji M, Ashe KH, Younkin SG (2001) Age-dependent changes in brain, CSF, and plasma amyloid (beta) protein in the Tg2576 transgenic mouse model of Alzheimer's disease. J Neurosci 21:372–381
    • (2001) J Neurosci , vol.21 , pp. 372-381
    • Kawarabayashi, T.1    Younkin, L.H.2    Saido, T.C.3    Shoji, M.4    Ashe, K.H.5    Younkin, S.G.6
  • 81
    • 0030035294 scopus 로고    scopus 로고
    • Fate of cerebrospinal fluid-borne amyloid beta-peptide: rapid clearance into blood and appreciable accumulation by cerebral arteries
    • COI: 1:CAS:528:DyaK28XksFCjtbg%3D, PID: 8764620
    • Ghersi-Egea JF, Gorevic PD, Ghiso J, Frangione B, Patlak CS, Fenstermacher JD (1996) Fate of cerebrospinal fluid-borne amyloid beta-peptide: rapid clearance into blood and appreciable accumulation by cerebral arteries. J Neurochem 67:880–883
    • (1996) J Neurochem , vol.67 , pp. 880-883
    • Ghersi-Egea, J.F.1    Gorevic, P.D.2    Ghiso, J.3    Frangione, B.4    Patlak, C.S.5    Fenstermacher, J.D.6
  • 82
    • 2542475986 scopus 로고    scopus 로고
    • Clearing amyloid through the blood-brain barrier
    • COI: 1:CAS:528:DC%2BD2cXksVyks7c%3D, PID: 15140180
    • Zlokovic BV (2004) Clearing amyloid through the blood-brain barrier. J Neurochem 89:807–811
    • (2004) J Neurochem , vol.89 , pp. 807-811
    • Zlokovic, B.V.1
  • 83
    • 78149392229 scopus 로고    scopus 로고
    • Peripherally applied Abeta-containing inoculates induce cerebral beta-amyloidosis
    • COI: 1:CAS:528:DC%2BC3cXhtl2isbjI, PID: 20966215
    • Eisele YS, Obermüller U, Heilbronner G, Baumann F, Kaeser SA, Wolburg H et al (2010) Peripherally applied Abeta-containing inoculates induce cerebral beta-amyloidosis. Science 330:980–982
    • (2010) Science , vol.330 , pp. 980-982
    • Eisele, Y.S.1    Obermüller, U.2    Heilbronner, G.3    Baumann, F.4    Kaeser, S.A.5    Wolburg, H.6
  • 84
    • 0035902619 scopus 로고    scopus 로고
    • Peripheral anti-A beta antibody alters CNS and plasma A beta clearance and decreases brain A beta burden in a mouse model of Alzheimer's disease
    • COI: 1:CAS:528:DC%2BD3MXls1Wiurk%3D, PID: 11438712
    • DeMattos RB, Bales KR, Cummins DJ, Dodart JC, Paul SM, Holtzman DM (2001) Peripheral anti-A beta antibody alters CNS and plasma A beta clearance and decreases brain A beta burden in a mouse model of Alzheimer's disease. Proc Natl Acad Sci U S A 98:8850–8855
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 8850-8855
    • DeMattos, R.B.1    Bales, K.R.2    Cummins, D.J.3    Dodart, J.C.4    Paul, S.M.5    Holtzman, D.M.6
  • 85
    • 84895419048 scopus 로고    scopus 로고
    • Red blood cell oxidative stress impairs oxygen delivery and induces red blood cell aging
    • PID: 24616707
    • Mohanty JG, Nagababu E, Rifkind JM (2014) Red blood cell oxidative stress impairs oxygen delivery and induces red blood cell aging. Front Physiol 5:84
    • (2014) Front Physiol , vol.5 , pp. 84
    • Mohanty, J.G.1    Nagababu, E.2    Rifkind, J.M.3
  • 86
    • 77954553684 scopus 로고    scopus 로고
    • Exercise plays a preventive role against Alzheimer's disease
    • PID: 20182027
    • Radak Z, Hart N, Sarga L, Koltai E, Atalay M, Ohno H et al (2010) Exercise plays a preventive role against Alzheimer's disease. J Alzheimers Dis 20:777–783
    • (2010) J Alzheimers Dis , vol.20 , pp. 777-783
    • Radak, Z.1    Hart, N.2    Sarga, L.3    Koltai, E.4    Atalay, M.5    Ohno, H.6
  • 87
    • 0035102044 scopus 로고    scopus 로고
    • Antioxidant enzyme activities and malondialdehyde levels related to aging
    • COI: 1:CAS:528:DC%2BD3MXhvVahs74%3D, PID: 11249925
    • Inal ME, Kanbak G, Sunal E (2001) Antioxidant enzyme activities and malondialdehyde levels related to aging. Clin Chim Acta 305:75–80
    • (2001) Clin Chim Acta , vol.305 , pp. 75-80
    • Inal, M.E.1    Kanbak, G.2    Sunal, E.3
  • 88
    • 84868520286 scopus 로고    scopus 로고
    • Physical training exerts neuroprotective effects in the regulation of neurochemical factors in an animal model of Parkinson's disease
    • COI: 1:CAS:528:DC%2BC38Xhs12mur7M, PID: 23041759
    • Tuon T, Valvassori SS, Lopes-Borges J, Luciano T, Trom CB, Silva LA et al (2012) Physical training exerts neuroprotective effects in the regulation of neurochemical factors in an animal model of Parkinson's disease. Neuroscience 227:305–312
    • (2012) Neuroscience , vol.227 , pp. 305-312
    • Tuon, T.1    Valvassori, S.S.2    Lopes-Borges, J.3    Luciano, T.4    Trom, C.B.5    Silva, L.A.6
  • 89
    • 77956363424 scopus 로고    scopus 로고
    • Exercise and Alzheimer's disease biomarkers in cognitively normal older adults
    • COI: 1:CAS:528:DC%2BC3cXht1SqtLbK, PID: 20818789
    • Liang KY, Mintun MA, Fagan AM, Goate AM, Bugg JM, Holtzman DM et al (2010) Exercise and Alzheimer's disease biomarkers in cognitively normal older adults. Ann Neurol 68:311–318
    • (2010) Ann Neurol , vol.68 , pp. 311-318
    • Liang, K.Y.1    Mintun, M.A.2    Fagan, A.M.3    Goate, A.M.4    Bugg, J.M.5    Holtzman, D.M.6
  • 91
    • 84934335505 scopus 로고    scopus 로고
    • Long-term treadmill exercise attenuates tau pathology in P301S tau transgenic mice
    • PID: 25432085
    • Ohia-Nwoko O, Montazari S, Lau YS, Eriksen JL (2014) Long-term treadmill exercise attenuates tau pathology in P301S tau transgenic mice. Mol Neurodegener 9:54
    • (2014) Mol Neurodegener , vol.9 , pp. 54
    • Ohia-Nwoko, O.1    Montazari, S.2    Lau, Y.S.3    Eriksen, J.L.4
  • 92
    • 0032500599 scopus 로고    scopus 로고
    • Binding of alpha-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation
    • COI: 1:CAS:528:DyaK1cXmslajsbw%3D, PID: 9756856
    • Jensen PH, Nielsen MS, Jakes R, Dotti CG, Goedert M (1998) Binding of alpha-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation. J Biol Chem 273:26292–26294
    • (1998) J Biol Chem , vol.273 , pp. 26292-26294
    • Jensen, P.H.1    Nielsen, M.S.2    Jakes, R.3    Dotti, C.G.4    Goedert, M.5
  • 93
    • 0035834076 scopus 로고    scopus 로고
    • Beta-amyloid peptides enhance alpha-synuclein accumulation and neuronal deficits in a transgenic mouse model linking Alzheimer's disease and Parkinson's disease
    • COI: 1:CAS:528:DC%2BD3MXns1Cjt7w%3D, PID: 11572944
    • Masliah E, Rockenstein E, Veinbergs I, Sagara Y, Mallory M, Hashimoto M et al (2001) Beta-amyloid peptides enhance alpha-synuclein accumulation and neuronal deficits in a transgenic mouse model linking Alzheimer's disease and Parkinson's disease. Proc Natl Acad Sci U S A 98:12245–12250
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 12245-12250
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3    Sagara, Y.4    Mallory, M.5    Hashimoto, M.6
  • 94
    • 0028813090 scopus 로고
    • Exercise, training and red blood cell turnover
    • COI: 1:STN:280:DyaK2M3lvVOhtw%3D%3D, PID: 7740249
    • Smith JA (1995) Exercise, training and red blood cell turnover. Sports Med 19:9–31
    • (1995) Sports Med , vol.19 , pp. 9-31
    • Smith, J.A.1
  • 95
    • 84904381675 scopus 로고    scopus 로고
    • Regulation of red cell life-span, erythropoiesis, senescence, and clearance
    • PID: 25101005
    • Kaestner L, Bogdanova A (2014) Regulation of red cell life-span, erythropoiesis, senescence, and clearance. Front Physiol 5:269
    • (2014) Front Physiol , vol.5 , pp. 269
    • Kaestner, L.1    Bogdanova, A.2
  • 96
    • 84871013033 scopus 로고    scopus 로고
    • Reticulocytes in sports medicine: an update
    • COI: 1:CAS:528:DC%2BC3sXpt1OnsL4%3D, PID: 23461135
    • Lombardi G, Colombini A, Lanteri P, Banfi G (2013) Reticulocytes in sports medicine: an update. Adv Clin Chem 59:125–153
    • (2013) Adv Clin Chem , vol.59 , pp. 125-153
    • Lombardi, G.1    Colombini, A.2    Lanteri, P.3    Banfi, G.4
  • 97
    • 84856417936 scopus 로고    scopus 로고
    • Effects of exercise training on red blood cell production: implications for anemia
    • PID: 22301865
    • Hu M, Lin W (2012) Effects of exercise training on red blood cell production: implications for anemia. Acta Haematol 127:156–164
    • (2012) Acta Haematol , vol.127 , pp. 156-164
    • Hu, M.1    Lin, W.2
  • 98
    • 80054729350 scopus 로고    scopus 로고
    • Reticulocyte and haemoglobin profiles in elite triathletes over four consecutive seasons
    • PID: 21707935
    • Díaz V, Lombardi G, Ricci C, Jacobs RA, Montalvo Z, Lundby C et al (2011) Reticulocyte and haemoglobin profiles in elite triathletes over four consecutive seasons. Int J Lab Hematol 33:638–644
    • (2011) Int J Lab Hematol , vol.33 , pp. 638-644
    • Díaz, V.1    Lombardi, G.2    Ricci, C.3    Jacobs, R.A.4    Montalvo, Z.5    Lundby, C.6


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