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Volumn 302, Issue 3, 2012, Pages

Current perspectives on cardiac amyloidosis

Author keywords

Cardiomyocytes; Heart

Indexed keywords

AMYLOID; AMYLOID A PROTEIN; AMYLOID PRECURSOR PROTEIN; ANGIOTENSIN RECEPTOR ANTAGONIST; APOLIPOPROTEIN A1; ATRIAL NATRIURETIC FACTOR; BETA 2 MICROGLOBULIN; BETA ADRENERGIC RECEPTOR BLOCKING AGENT; BORTEZOMIB; CALCIUM CHANNEL BLOCKING AGENT; CYCLOPHOSPHAMIDE; CYSTATIN C; DEXAMETHASONE; DIGOXIN; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; GELSOLIN; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN LIGHT CHAIN; INSULIN; LACTADHERIN; LACTOFERRIN; LENALIDOMIDE; MELPHALAN; PREALBUMIN; PRION PROTEIN; PROCALCITONIN; PROLACTIN; SERUM AMYLOID P; SMALL INTERFERING RNA; THALIDOMIDE;

EID: 84856448913     PISSN: 03636135     EISSN: 15221539     Source Type: Journal    
DOI: 10.1152/ajpheart.00815.2011     Document Type: Review
Times cited : (68)

References (112)
  • 8
    • 3543107213 scopus 로고    scopus 로고
    • Two different types of amyloid deposits-apolipo-protein A-IV and transthyretin-in a patient systemic amyloidosis with
    • Bergstrom J, Murphy CL, Weiss DT, Solomon A, Sletten K, Hellman U, Westermark P. Two different types of amyloid deposits-apolipo-protein A-IV and transthyretin-in a patient systemic amyloidosis with. Lab Invest 84: 981-988, 2004.
    • (2004) Lab Invest , vol.84 , pp. 981-988
    • Bergstrom, J.1    Murphy, C.L.2    Weiss, D.T.3    Solomon, A.4    Sletten, K.5    Hellman, U.6    Westermark, P.7
  • 9
    • 77950371336 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their tissue inhibitors in cardiac amyloidosis: Relationship to structural, functional myocardial changes and to light chain amyloid deposition
    • Biolo A, Ramamurthy S, Connors LH, O'Hara CJ, Meier-Ewert HK, Soo Hoo PT, Sawyer DB, Seldin DC, Sam F. Matrix metalloproteinases and their tissue inhibitors in cardiac amyloidosis: relationship to structural, functional myocardial changes and to light chain amyloid deposition. Circ Heart Fail 1: 249-257, 2008.
    • (2008) Circ Heart Fail , vol.1 , pp. 249-257
    • Biolo, A.1    Ramamurthy, S.2    Connors, L.H.3    O'Hara, C.J.4    Meier-Ewert, H.K.5    Soo Hoo, P.T.6    Sawyer, D.B.7    Seldin, D.C.8    Sam, F.9
  • 11
    • 2342525940 scopus 로고    scopus 로고
    • Human amyloidogenic light chains directly impair cardiomyocyte function through an increase in cellular oxidant stress
    • Brenner DA, Jain M, Pimentel DR, Wang B, Connors LH, Skinner M, Apstein CS, Liao R. Human amyloidogenic light chains directly impair cardiomyocyte function through an increase in cellular oxidant stress. Circ Res 94: 1008-1010, 2004.
    • (2004) Circ Res , vol.94 , pp. 1008-1010
    • Brenner, D.A.1    Jain, M.2    Pimentel, D.R.3    Wang, B.4    Connors, L.H.5    Skinner, M.6    Apstein, C.S.7    Liao, R.8
  • 12
    • 30344467836 scopus 로고    scopus 로고
    • Cardiac conduction alterations in a French family with amyloidosis of the Finnish type with the p. Asp187Tyr mutation in the GSN gene
    • Chastan N, Baert-Desurmont S, Saugier-Veber P, Derumeaux G, Cabot A, Frebourg T, Hannequin D. Cardiac conduction alterations in a French family with amyloidosis of the Finnish type with the p. Asp187Tyr mutation in the GSN gene. Muscle Nerve 33: 113-119, 2006.
    • (2006) Muscle Nerve , vol.33 , pp. 113-119
    • Chastan, N.1    Baert-Desurmont, S.2    Saugier-Veber, P.3    Derumeaux, G.4    Cabot, A.5    Frebourg, T.6    Hannequin, D.7
  • 14
    • 77951776829 scopus 로고    scopus 로고
    • Alzheimer's disease: Strategies for disease modification
    • Citron M. Alzheimer's disease: strategies for disease modification. Nat Rev Drug Discov 9: 387-398 2010.
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 387-398
    • Citron, M.1
  • 15
    • 37049002704 scopus 로고    scopus 로고
    • Heterogeneity in primary structure, post-translational modifications, and germline gene usage of nine full-length amyloidogenic kappa1 immunoglobulin light chains
    • Connors LH, Jiang Y, Budnik M, Theberge R, Prokaeva T, Bodi KL, Seldin DC, Costello CE, Skinner M. Heterogeneity in primary structure, post-translational modifications, and germline gene usage of nine full-length amyloidogenic kappa1 immunoglobulin light chains. Biochemistry 46: 14259-14271, 2007.
    • (2007) Biochemistry , vol.46 , pp. 14259-14271
    • Connors, L.H.1    Jiang, Y.2    Budnik, M.3    Theberge, R.4    Prokaeva, T.5    Bodi, K.L.6    Seldin, D.C.7    Costello, C.E.8    Skinner, M.9
  • 16
    • 78650295571 scopus 로고    scopus 로고
    • Effect of lysine modification on the stability and cellular binding of human amyloidogenic light chains
    • Davern S, Murphy CL, O'Neill H, Wall JS, Weiss DT, Solomon A. Effect of lysine modification on the stability and cellular binding of human amyloidogenic light chains. Biochim Biophys Acta 1812: 32-40, 2010.
    • (2010) Biochim Biophys Acta , vol.1812 , pp. 32-40
    • Davern, S.1    Murphy, C.L.2    O'Neill, H.3    Wall, J.S.4    Weiss, D.T.5    Solomon, A.6
  • 18
    • 15544377122 scopus 로고    scopus 로고
    • Rnai as an experimental and therapeutic tool to study and regulate physiological and disease processes
    • Dillon CP, Sandy P, Nencioni A, Kissler S, Rubinson DA, Van Parijs L. Rnai as an experimental and therapeutic tool to study and regulate physiological and disease processes. Annu Rev Physiol 67: 147-173, 2005.
    • (2005) Annu Rev Physiol , vol.67 , pp. 147-173
    • Dillon, C.P.1    Sandy, P.2    Nencioni, A.3    Kissler, S.4    Rubinson, D.A.5    van Parijs, L.6
  • 21
    • 0030587249 scopus 로고    scopus 로고
    • Resolution of heart failure in patients with AL amyloidosis
    • Dubrey S, Mendes L, Skinner M, Falk RH. Resolution of heart failure in patients with AL amyloidosis. Ann Intern Med 125: 481-484, 1996.
    • (1996) Ann Intern Med , vol.125 , pp. 481-484
    • Dubrey, S.1    Mendes, L.2    Skinner, M.3    Falk, R.H.4
  • 22
    • 0031913337 scopus 로고    scopus 로고
    • The clinical features of immunoglobulin light-chain (AL) amyloidosis with heart involvement
    • Dubrey SW, Cha K, Anderson J, Chamarthi B, Reisinger J, Skinner M, Falk RH. The clinical features of immunoglobulin light-chain (AL) amyloidosis with heart involvement. QJM 91: 141-157, 1998.
    • (1998) QJM , vol.91 , pp. 141-157
    • Dubrey, S.W.1    Cha, K.2    Anderson, J.3    Chamarthi, B.4    Reisinger, J.5    Skinner, M.6    Falk, R.H.7
  • 23
    • 0030744403 scopus 로고    scopus 로고
    • Familial and primary (AL) cardiac amyloidosis: Echocardiographically similar diseases with distinctly different clinical outcomes
    • Dubrey SW, Cha K, Skinner M, LaValley M, Falk RH. Familial and primary (AL) cardiac amyloidosis: echocardiographically similar diseases with distinctly different clinical outcomes. Heart 78: 74-82, 1997.
    • (1997) Heart , vol.78 , pp. 74-82
    • Dubrey, S.W.1    Cha, K.2    Skinner, M.3    Lavalley, M.4    Falk, R.H.5
  • 24
    • 0025114431 scopus 로고
    • Immunoglobulin heavy-chain-associated amyloidosis
    • Eulitz M, Weiss DT, Solomon A. Immunoglobulin heavy-chain-associated amyloidosis. Proc Natl Acad Sci USA 87: 6542-6546, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6542-6546
    • Eulitz, M.1    Weiss, D.T.2    Solomon, A.3
  • 25
    • 80052286754 scopus 로고    scopus 로고
    • Cardiac amyloidosis: A treatable disease, often overlooked
    • Falk RH. Cardiac amyloidosis: a treatable disease, often overlooked. Circulation 124: 1079-1085, 2011.
    • (2011) Circulation , vol.124 , pp. 1079-1085
    • Falk, R.H.1
  • 26
    • 25444434458 scopus 로고    scopus 로고
    • Diagnosis and management of the cardiac amyloidoses
    • Falk RH. Diagnosis and management of the cardiac amyloidoses. Circulation 112: 2047-2060, 2005.
    • (2005) Circulation , vol.112 , pp. 2047-2060
    • Falk, R.H.1
  • 29
    • 78851472260 scopus 로고    scopus 로고
    • Immunoglobulin light chain amyloidosis: 2011 update on diagnosis, risk-stratification, and management
    • Gertz MA. Immunoglobulin light chain amyloidosis: 2011 update on diagnosis, risk-stratification, and management. Am J Hematol 86: 180-186, 2011.
    • (2011) Am J Hematol , vol.86 , pp. 180-186
    • Gertz, M.A.1
  • 30
    • 23244448608 scopus 로고    scopus 로고
    • Definition of organ involvement and treatment response in immunoglobulin light chain amyloidosis (AL): A consensus opinion from the 10th International Symposium on Amyloid and Amyloidosis, Tours, France, 18-22 April 2004
    • Gertz MA, Comenzo R, Falk RH, Fermand JP, Hazenberg BP, Hawkins PN, Merlini G, Moreau P, Ronco P, Sanchorawala V, Sezer O, Solomon A, Grateau G. Definition of organ involvement and treatment response in immunoglobulin light chain amyloidosis (AL): a consensus opinion from the 10th International Symposium on Amyloid and Amyloidosis, Tours, France, 18-22 April 2004. Am J Hematol 79: 319-328, 2005.
    • (2005) Am J Hematol , vol.79 , pp. 319-328
    • Gertz, M.A.1    Comenzo, R.2    Falk, R.H.3    Fermand, J.P.4    Hazenberg, B.P.5    Hawkins, P.N.6    Merlini, G.7    Moreau, P.8    Ronco, P.9    Sanchorawala, V.10    Sezer, O.11    Solomon, A.12    Grateau, G.13
  • 34
    • 71049187207 scopus 로고    scopus 로고
    • Cardiac transplantation should be considered in selected patients with either AL or hereditary forms of amyloidosis: The UK National Amyloidosis Centre experience
    • author reply 787-788
    • Gibbs SD, Sattianayagam PT, Hawkins PN, Gillmore JD. Cardiac transplantation should be considered in selected patients with either AL or hereditary forms of amyloidosis: the UK National Amyloidosis Centre experience. Intern Med J 39: 786-787; author reply 787-788, 2009.
    • (2009) Intern Med J , vol.39 , pp. 786-787
    • Gibbs, S.D.1    Sattianayagam, P.T.2    Hawkins, P.N.3    Gillmore, J.D.4
  • 35
    • 33646868587 scopus 로고    scopus 로고
    • Drug insight: Emerging therapies for amy-loidosis
    • Gillmore JD, Hawkins PN. Drug insight: emerging therapies for amy-loidosis. Nat Clin Pract Nephrol 2: 263-270, 2006.
    • (2006) Nat Clin Pract Nephrol , vol.2 , pp. 263-270
    • Gillmore, J.D.1    Hawkins, P.N.2
  • 38
    • 79251510886 scopus 로고    scopus 로고
    • Evidence for a functional role of the molecular chaperone clusterin in amyloidotic cardiomyopathy
    • Greene MJ, Sam F, Soo Hoo PT, Patel RS, Seldin DC, Connors LH. Evidence for a functional role of the molecular chaperone clusterin in amyloidotic cardiomyopathy. Am J Pathol 178: 61-68, 2011.
    • (2011) Am J Pathol , vol.178 , pp. 61-68
    • Greene, M.J.1    Sam, F.2    Soo Hoo, P.T.3    Patel, R.S.4    Seldin, D.C.5    Connors, L.H.6
  • 42
    • 70849124339 scopus 로고    scopus 로고
    • Beta(2)-microglobulin: From physiology to amyloidosis
    • Heegaard NH. Beta(2)-microglobulin: from physiology to amyloidosis. Amyloid 16: 151-173, 2009.
    • (2009) Amyloid , vol.16 , pp. 151-173
    • Heegaard, N.H.1
  • 43
    • 33644834054 scopus 로고    scopus 로고
    • Role of islet amyloid in type 2 diabetes mellitus
    • Hoppener JW, Lips CJ. Role of islet amyloid in type 2 diabetes mellitus. Int J Biochem Cell Biol 38: 726-736, 2006.
    • (2006) Int J Biochem Cell Biol , vol.38 , pp. 726-736
    • Hoppener, J.W.1    Lips, C.J.2
  • 49
    • 13244254047 scopus 로고    scopus 로고
    • Amyloid in the cardiovascular system: A review
    • Kholova I, Niessen HW. Amyloid in the cardiovascular system: a review. J Clin Pathol 58: 125-133, 2005.
    • (2005) J Clin Pathol , vol.58 , pp. 125-133
    • Kholova, I.1    Niessen, H.W.2
  • 50
    • 0035812658 scopus 로고    scopus 로고
    • Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillo-genesis
    • Kirkitadze MD, Condron MM, Teplow DB. Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillo-genesis. J Mol Biol 312: 1103-1119, 2001.
    • (2001) J Mol Biol , vol.312 , pp. 1103-1119
    • Kirkitadze, M.D.1    Condron, M.M.2    Teplow, D.B.3
  • 52
    • 78149425311 scopus 로고    scopus 로고
    • The critical role of the constant region in thermal stability and aggregation of amyloidogenic immunoglobulin light chain
    • Klimtchuk ES, Gursky O, Patel RS, Laporte KL, Connors LH, Skinner M, Seldin DC. The critical role of the constant region in thermal stability and aggregation of amyloidogenic immunoglobulin light chain. Biochemistry 49: 9848-9857, 2010.
    • (2010) Biochemistry , vol.49 , pp. 9848-9857
    • Klimtchuk, E.S.1    Gursky, O.2    Patel, R.S.3    Laporte, K.L.4    Connors, L.H.5    Skinner, M.6    Seldin, D.C.7
  • 54
    • 0034796505 scopus 로고    scopus 로고
    • Amyloidosis: A convoluted story
    • Kyle RA. Amyloidosis: a convoluted story. Br J Haematol 114: 529-538, 2001.
    • (2001) Br J Haematol , vol.114 , pp. 529-538
    • Kyle, R.A.1
  • 55
    • 76849091134 scopus 로고    scopus 로고
    • Can Alzheimer disease be prevented by amyloid-beta immunotherapy?
    • Lemere CA, Masliah E. Can Alzheimer disease be prevented by amyloid-beta immunotherapy? Nat Rev Neurol 6: 108-119. 2010.
    • (2010) Nat Rev Neurol , vol.6 , pp. 108-119
    • Lemere, C.A.1    Masliah, E.2
  • 57
    • 0035797855 scopus 로고    scopus 로고
    • Infusion of light chains from patients with cardiac amyloid-osis causes diastolic dysfunction in isolated mouse hearts
    • Liao R, Jain M, Teller P, Connors LH, Ngoy S, Skinner M, Falk RH, Apstein CS. Infusion of light chains from patients with cardiac amyloid-osis causes diastolic dysfunction in isolated mouse hearts. Circulation 104: 1594-1597, 2001.
    • (2001) Circulation , vol.104 , pp. 1594-1597
    • Liao, R.1    Jain, M.2    Teller, P.3    Connors, L.H.4    Ngoy, S.5    Skinner, M.6    Falk, R.H.7    Apstein, C.S.8
  • 59
    • 78649280232 scopus 로고    scopus 로고
    • Comparison of amyloid fibril formation by two closely related immunoglobulin light chain variable domains
    • Martin DJ, Ramirez-Alvarado M. Comparison of amyloid fibril formation by two closely related immunoglobulin light chain variable domains. Amyloid 17: 129-136, 2010.
    • (2010) Amyloid , vol.17 , pp. 129-136
    • Martin, D.J.1    Ramirez-Alvarado, M.2
  • 60
    • 0025966199 scopus 로고
    • Isolation and characterization of cardiac amyloid in familial amyloid polyneuropathy type IV (Finnish): Relation of the amyloid protein to variant gelsolin
    • Maury CP, Baumann M. Isolation and characterization of cardiac amyloid in familial amyloid polyneuropathy type IV (Finnish): relation of the amyloid protein to variant gelsolin. Biochim Biophys Acta 1096: 84-86, 1990.
    • (1990) Biochim Biophys Acta , vol.1096 , pp. 84-86
    • Maury, C.P.1    Baumann, M.2
  • 61
    • 0042709605 scopus 로고    scopus 로고
    • Molecular mechanisms of amyloidosis
    • Merlini G, Bellotti V. Molecular mechanisms of amyloidosis. N Engl J Med 349: 583-596, 2003.
    • (2003) N Engl J Med , vol.349 , pp. 583-596
    • Merlini, G.1    Bellotti, V.2
  • 62
    • 79955842001 scopus 로고    scopus 로고
    • Amyloidosis: Pathogenesis and new therapeutic options
    • Merlini G, Seldin DC, Gertz MA. Amyloidosis: pathogenesis and new therapeutic options. J Clin Oncol 29: 1924-1933, 2011.
    • (2011) J Clin Oncol , vol.29 , pp. 1924-1933
    • Merlini, G.1    Seldin, D.C.2    Gertz, M.A.3
  • 68
    • 1442275655 scopus 로고    scopus 로고
    • Immunoglobulin kappa light chain and its amyloidogenic mutants: A molecular dynamics study
    • Nowak M. Immunoglobulin kappa light chain and its amyloidogenic mutants: a molecular dynamics study. Proteins 55: 11-21, 2004.
    • (2004) Proteins , vol.55 , pp. 11-21
    • Nowak, M.1
  • 73
    • 79952005272 scopus 로고    scopus 로고
    • Transplantation vs. conventional-dose therapy for amyloidosis
    • Palladini G, Merlini G. Transplantation vs. conventional-dose therapy for amyloidosis. Curr Opin Oncol 23: 214-220, 2011.
    • (2011) Curr Opin Oncol , vol.23 , pp. 214-220
    • Palladini, G.1    Merlini, G.2
  • 74
    • 33646586054 scopus 로고    scopus 로고
    • Hereditary cystatin C amyloid angiopathy: Genetic, clinical, and pathological aspects
    • Palsdottir A, Snorradottir AO, Thorsteinsson L. Hereditary cystatin C amyloid angiopathy: genetic, clinical, and pathological aspects. Brain Pathol 16: 55-59, 2006.
    • (2006) Brain Pathol , vol.16 , pp. 55-59
    • Palsdottir, A.1    Snorradottir, A.O.2    Thorsteinsson, L.3
  • 77
    • 77952604860 scopus 로고    scopus 로고
    • A single mutation promotes amyloidogenicity through a highly promiscuous dimer interface
    • Peterson FC, Baden EM, Owen BA, Volkman BF, Ramirez-Alvarado M. A single mutation promotes amyloidogenicity through a highly promiscuous dimer interface. Structure 18: 563-570, 2010.
    • (2010) Structure , vol.18 , pp. 563-570
    • Peterson, F.C.1    Baden, E.M.2    Owen, B.A.3    Volkman, B.F.4    Ramirez-Alvarado, M.5
  • 79
    • 65249180061 scopus 로고    scopus 로고
    • Mutations in specific structural regions of im-munoglobulin light chains are associated with free light chain levels in patients with AL amyloidosis
    • Poshusta TL, Sikkink LA, Leung N, Clark RJ, Dispenzieri A, Ramirez-Alvarado M. Mutations in specific structural regions of im-munoglobulin light chains are associated with free light chain levels in patients with AL amyloidosis. PLoS One 4: e5169, 2009.
    • (2009) PLoS One , vol.4
    • Poshusta, T.L.1    Sikkink, L.A.2    Leung, N.3    Clark, R.J.4    Dispenzieri, A.5    Ramirez-Alvarado, M.6
  • 81
    • 0037144424 scopus 로고    scopus 로고
    • Amyloid fibril formation by pentapeptide and tetrapeptide fragments of human calcitonin
    • Reches M, Porat Y, Gazit E. Amyloid fibril formation by pentapeptide and tetrapeptide fragments of human calcitonin. J Biol Chem 277: 35475-35480, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 35475-35480
    • Reches, M.1    Porat, Y.2    Gazit, E.3
  • 84
    • 0036176146 scopus 로고    scopus 로고
    • Pathology, diagnosis and pathogenesis of AA amyloidosis
    • Rocken C, Shakespeare A. Pathology, diagnosis and pathogenesis of AA amyloidosis. Virchows Arch 440: 111-122, 2002.
    • (2002) Virchows Arch , vol.440 , pp. 111-122
    • Rocken, C.1    Shakespeare, A.2
  • 86
    • 79551530731 scopus 로고    scopus 로고
    • Oligonucleotide therapeutic approaches for Hun-tington disease
    • Sah DW, Aronin N. Oligonucleotide therapeutic approaches for Hun-tington disease. J Clin Invest 121: 500-507, 2011.
    • (2011) J Clin Invest , vol.121 , pp. 500-507
    • Sah, D.W.1    Aronin, N.2
  • 87
    • 34548564578 scopus 로고    scopus 로고
    • Light-chain (AL) amyloidosis: Diagnosis and treatment
    • Sanchorawala V. Light-chain (AL) amyloidosis: diagnosis and treatment. Clin J Am Soc Nephrol 1: 1331-1341, 2006.
    • (2006) Clin J Am Soc Nephrol , vol.1 , pp. 1331-1341
    • Sanchorawala, V.1
  • 88
    • 30944433400 scopus 로고    scopus 로고
    • Serum free light-chain responses after high-dose intravenous melphalan and autologous stem cell transplantation for AL (primary) amyloidosis
    • Sanchorawala V, Seldin DC, Magnani B, Skinner M, Wright DG. Serum free light-chain responses after high-dose intravenous melphalan and autologous stem cell transplantation for AL (primary) amyloidosis. Bone Marrow Transplant 36: 597-600, 2005.
    • (2005) Bone Marrow Transplant , vol.36 , pp. 597-600
    • Sanchorawala, V.1    Seldin, D.C.2    Magnani, B.3    Skinner, M.4    Wright, D.G.5
  • 89
    • 59649105575 scopus 로고    scopus 로고
    • Pathogenesis of and therapeutic strategies to ameliorate the transthyretin amyloidoses
    • Sekijima Y, Kelly JW, Ikeda S. Pathogenesis of and therapeutic strategies to ameliorate the transthyretin amyloidoses. Curr Pharm Des 14: 3219-3230, 2008.
    • (2008) Curr Pharm Des , vol.14 , pp. 3219-3230
    • Sekijima, Y.1    Kelly, J.W.2    Ikeda, S.3
  • 91
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe DJ. Folding proteins in fatal ways. Nature 426: 900-904, 2003.
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 92
    • 33749037743 scopus 로고    scopus 로고
    • Amyloidosis and the heart: A comprehensive review
    • Shah KB, Inoue Y, Mehra MR. Amyloidosis and the heart: a comprehensive review. Arch Intern Med 166: 1805-1813, 2006.
    • (2006) Arch Intern Med , vol.166 , pp. 1805-1813
    • Shah, K.B.1    Inoue, Y.2    Mehra, M.R.3
  • 94
    • 79958709932 scopus 로고    scopus 로고
    • Cytotoxicity of amyloidogenic immunoglobulin light chains in cell culture
    • Sikkink LA, Ramirez-Alvarado M. Cytotoxicity of amyloidogenic immunoglobulin light chains in cell culture. Cell Death Dis 1: e98, 2010.
    • (2010) Cell Death Dis , vol.e98 , pp. 1
    • Sikkink, L.A.1    Ramirez-Alvarado, M.2
  • 96
    • 78649315112 scopus 로고    scopus 로고
    • Amyloid fibril protein nomenclature: 2010 recommendations from the nomenclature committee of the International Society of Amyloidosis
    • Sipe JD, Benson MD, Buxbaum JN, Ikeda S, Merlini G, Saraiva MJ, Westermark P. Amyloid fibril protein nomenclature: 2010 recommendations from the nomenclature committee of the International Society of Amyloidosis. Amyloid 17: 101-104, 2011.
    • (2011) Amyloid , vol.17 , pp. 101-104
    • Sipe, J.D.1    Benson, M.D.2    Buxbaum, J.N.3    Ikeda, S.4    Merlini, G.5    Saraiva, M.J.6    Westermark, P.7
  • 97
    • 0033849738 scopus 로고    scopus 로고
    • Review: History of the amyloid fibril
    • Sipe JD, Cohen AS. Review: history of the amyloid fibril. J Struct Biol 130: 88-98, 2000.
    • (2000) J Struct Biol , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 98
    • 36348934009 scopus 로고    scopus 로고
    • Bortezomib in the treatment of AL amyloidosis: Targeted therapy?
    • Sitia R, Palladini G, Merlini G. Bortezomib in the treatment of AL amyloidosis: targeted therapy? Haematologica 92: 1302-1307, 2007.
    • (2007) Haematologica , vol.92 , pp. 1302-1307
    • Sitia, R.1    Palladini, G.2    Merlini, G.3
  • 99
    • 0018717327 scopus 로고
    • Serum amyloid P-component levels in amyloidosis, connective tissue diseases, infection, and malignancy as compared to normal serum
    • Skinner M, Vaitukaitis JL, Cohen AS, Benson MD. Serum amyloid P-component levels in amyloidosis, connective tissue diseases, infection, and malignancy as compared to normal serum. J Lab Clin Med 94: 633-638, 1979.
    • (1979) J Lab Clin Med , vol.94 , pp. 633-638
    • Skinner, M.1    Vaitukaitis, J.L.2    Cohen, A.S.3    Benson, M.D.4
  • 101
    • 0033807726 scopus 로고    scopus 로고
    • Four structural risk factors identify most fibril-forming kappa light chains
    • Stevens FJ. Four structural risk factors identify most fibril-forming kappa light chains. Amyloid 7: 200-211, 2000.
    • (2000) Amyloid , vol.7 , pp. 200-211
    • Stevens, F.J.1
  • 102
    • 0034126224 scopus 로고    scopus 로고
    • Liver transplantation for hereditary transthyretin amyloidosis
    • Suhr OB, Herlenius G, Friman S, Ericzon BG. Liver transplantation for hereditary transthyretin amyloidosis. Liver Transpl 6: 263-276, 2000.
    • (2000) Liver Transpl , vol.6 , pp. 263-276
    • Suhr, O.B.1    Herlenius, G.2    Friman, S.3    Ericzon, B.G.4
  • 103
    • 69149103558 scopus 로고    scopus 로고
    • Intrinsic disorder in proteins associated with neurodegen-erative diseases
    • Uversky VN. Intrinsic disorder in proteins associated with neurodegen-erative diseases. Front Biosci 14: 5188-5238, 2009.
    • (2009) Front Biosci , vol.14 , pp. 5188-5238
    • Uversky, V.N.1
  • 104
    • 48249097986 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in human diseases: Introducing the D2 concept
    • Uversky VN, Oldfield CJ, Dunker AK. Intrinsically disordered proteins in human diseases: introducing the D2 concept. Annu Rev Biophys 37: 215-246, 2008.
    • (2008) Annu Rev Biophys , vol.37 , pp. 215-246
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 105
    • 73949091104 scopus 로고    scopus 로고
    • Classification of amyloidosis by laser microdissection and mass spectrometry-based proteomic analysis in clinical biopsy specimens
    • Vrana JA, Gamez JD, Madden BJ, Theis JD, Bergen HR, Dogan A. Classification of amyloidosis by laser microdissection and mass spectrometry-based proteomic analysis in clinical biopsy specimens. Blood 114: 4957-4959, 2009.
    • (2009) Blood , vol.114 , pp. 4957-4959
    • Vrana, J.A.1    Gamez, J.D.2    Madden, B.J.3    Theis, J.D.4    Bergen, H.R.5    Dogan, A.6
  • 106
    • 0345426278 scopus 로고    scopus 로고
    • Thermodynamic instability of human lambda 6 light chains: Correlation with fibrillogenicity
    • Wall J, Schell M, Murphy C, Hrncic R, Stevens FJ, Solomon A. Thermodynamic instability of human lambda 6 light chains: correlation with fibrillogenicity. Biochemistry 38: 14101-14108, 1999.
    • (1999) Biochemistry , vol.38 , pp. 14101-14108
    • Wall, J.1    Schell, M.2    Murphy, C.3    Hrncic, R.4    Stevens, F.J.5    Solomon, A.6
  • 107
    • 3142641190 scopus 로고    scopus 로고
    • Structural basis of light chain amyloidogenicity: Comparison of the thermodynamic properties, fibril-logenic potential and tertiary structural features of four Vlambda6 proteins
    • Wall JS, Gupta V, Wilkerson M, Schell M, Loris R, Adams P, Solomon A, Stevens F, Dealwis C. Structural basis of light chain amyloidogenicity: comparison of the thermodynamic properties, fibril-logenic potential and tertiary structural features of four Vlambda6 proteins. J Mol Recognit 17: 323-331, 2004.
    • (2004) J Mol Recognit , vol.17 , pp. 323-331
    • Wall, J.S.1    Gupta, V.2    Wilkerson, M.3    Schell, M.4    Loris, R.5    Adams, P.6    Solomon, A.7    Stevens, F.8    Dealwis, C.9
  • 109
    • 33846263334 scopus 로고    scopus 로고
    • Safety and efficacy of risk-adapted cyclophosph-amide, thalidomide, and dexamethasone in systemic AL amyloidosis
    • Wechalekar AD, Goodman HJ, Lachmann HJ, Offer M, Hawkins PN, Gillmore JD. Safety and efficacy of risk-adapted cyclophosph-amide, thalidomide, and dexamethasone in systemic AL amyloidosis. Blood 109: 457-464, 2007.
    • (2007) Blood , vol.109 , pp. 457-464
    • Wechalekar, A.D.1    Goodman, H.J.2    Lachmann, H.J.3    Offer, M.4    Hawkins, P.N.5    Gillmore, J.D.6
  • 110
    • 33646384419 scopus 로고    scopus 로고
    • Immunology and immunotherapy of Alzheimer's disease
    • Weiner HL, Frenkel D. Immunology and immunotherapy of Alzheimer's disease. Nat Rev Immunol 6: 404-416, 2006.
    • (2006) Nat Rev Immunol , vol.6 , pp. 404-416
    • Weiner, H.L.1    Frenkel, D.2
  • 112
    • 67549142772 scopus 로고    scopus 로고
    • Localized insulin-derived amyloidosis in patients with diabetes mellitus: A case report
    • Yumlu S, Barany R, Eriksson M, Rocken C. Localized insulin-derived amyloidosis in patients with diabetes mellitus: a case report. Hum Pathol 40: 1655-1660, 2009.
    • (2009) Hum Pathol , vol.40 , pp. 1655-1660
    • Yumlu, S.1    Barany, R.2    Eriksson, M.3    Rocken, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.