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Volumn 127, Issue , 2016, Pages 44-49

Familial mutations in fibrinogen Aα (FGA) chain identified in renal amyloidosis increase in vitro amyloidogenicity of FGA fragment

Author keywords

Amyloid; Atomic force microscopy; Dynamic light scattering; Fibrinogen alpha chain; Fibrinogen amyloidosis; Renal amyloidosis

Indexed keywords

AMYLOID; FIBRINOGEN; FIBRINOGEN AALPHA; UNCLASSIFIED DRUG; PEPTIDE FRAGMENT;

EID: 84966312394     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2016.04.020     Document Type: Article
Times cited : (21)

References (39)
  • 1
    • 32944457929 scopus 로고    scopus 로고
    • Amyloidosis
    • M.B. Pepys Amyloidosis Annu. Rev. Med. 57 2006 223 241
    • (2006) Annu. Rev. Med. , vol.57 , pp. 223-241
    • Pepys, M.B.1
  • 2
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 0042709605 scopus 로고    scopus 로고
    • Molecular mechanisms of amyloidosis
    • G. Merlini, and V. Bellotti Molecular mechanisms of amyloidosis N. Engl. J. Med. 349 2003 583 596
    • (2003) N. Engl. J. Med. , vol.349 , pp. 583-596
    • Merlini, G.1    Bellotti, V.2
  • 4
    • 0033059283 scopus 로고    scopus 로고
    • The hereditary renal amyloidoses
    • S. Tan The hereditary renal amyloidoses, Clin. Exp. Nephrol. 3 1999 1 8
    • (1999) Clin. Exp. Nephrol. , vol.3 , pp. 1-8
    • Tan, S.1
  • 5
    • 0027465319 scopus 로고
    • Hereditary renal amyloidosis associated with a mutant fibrinogen alpha-chain
    • M.D. Benson, J. Liepnieks, T. Uemichi, G. Wheeler, and R. Correa Hereditary renal amyloidosis associated with a mutant fibrinogen alpha-chain Nat. Genet. 3 1993 252 255
    • (1993) Nat. Genet. , vol.3 , pp. 252-255
    • Benson, M.D.1    Liepnieks, J.2    Uemichi, T.3    Wheeler, G.4    Correa, R.5
  • 6
    • 0028211154 scopus 로고
    • Hereditary renal amyloidosis with a novel variant fibrinogen
    • T. Uemichi, J.J. Liepnieks, and M.D. Benson Hereditary renal amyloidosis with a novel variant fibrinogen J. Clin. Investig. 93 1994 731 736
    • (1994) J. Clin. Investig. , vol.93 , pp. 731-736
    • Uemichi, T.1    Liepnieks, J.J.2    Benson, M.D.3
  • 7
    • 0029916231 scopus 로고    scopus 로고
    • A frame shift mutation in the fibrinogen A alpha chain gene in a kindred with renal amyloidosis
    • T. Uemichi, J.J. Liepnieks, T. Yamada, M.A. Gertz, N. Bang, and M.D. Benson A frame shift mutation in the fibrinogen A alpha chain gene in a kindred with renal amyloidosis Blood 87 1996 4197 4203
    • (1996) Blood , vol.87 , pp. 4197-4203
    • Uemichi, T.1    Liepnieks, J.J.2    Yamada, T.3    Gertz, M.A.4    Bang, N.5    Benson, M.D.6
  • 9
    • 0032153493 scopus 로고    scopus 로고
    • Fibrinogen A alpha chain Leu 554: An African-American kindred with late onset renal amyloidosis
    • T. Uemichi, J.J. Liepnieks, M.A. Gertz, and M.D. Benson Fibrinogen A alpha chain Leu 554: an African-American kindred with late onset renal amyloidosis Amyloid 5 1998 188 192
    • (1998) Amyloid , vol.5 , pp. 188-192
    • Uemichi, T.1    Liepnieks, J.J.2    Gertz, M.A.3    Benson, M.D.4
  • 12
    • 30944438482 scopus 로고    scopus 로고
    • Hereditary amyloidosis in early childhood associated with a novel insertion-deletion (indel) in the fibrinogen Aalpha chain gene
    • H.G. Kang, A. Bybee, I.S. Ha, M.S. Park, J.A. Gilbertson, H.I. Cheong, Y. Choi, and P.N. Hawkins Hereditary amyloidosis in early childhood associated with a novel insertion-deletion (indel) in the fibrinogen Aalpha chain gene Kidney Int. 68 2005 1994 1998
    • (2005) Kidney Int. , vol.68 , pp. 1994-1998
    • Kang, H.G.1    Bybee, A.2    Ha, I.S.3    Park, M.S.4    Gilbertson, J.A.5    Cheong, H.I.6    Choi, Y.7    Hawkins, P.N.8
  • 15
    • 58149100172 scopus 로고    scopus 로고
    • Cardiac amyloidosis with the E526V mutation of the fibrinogen A alpha-chain
    • G. Mourad, J.P. Delabre, and V. Garrigue Cardiac amyloidosis with the E526V mutation of the fibrinogen A alpha-chain N. Engl. J. Med. 359 2008 2847 2848
    • (2008) N. Engl. J. Med. , vol.359 , pp. 2847-2848
    • Mourad, G.1    Delabre, J.P.2    Garrigue, V.3
  • 20
    • 0034975060 scopus 로고    scopus 로고
    • A database for human fibrinogen variants
    • M. Hanss, and F. Biot A database for human fibrinogen variants Ann. N. Y. Acad. Sci. 936 2001 89 90
    • (2001) Ann. N. Y. Acad. Sci. , vol.936 , pp. 89-90
    • Hanss, M.1    Biot, F.2
  • 22
    • 45749102914 scopus 로고    scopus 로고
    • The Zyggregator method for predicting protein aggregation propensities
    • G.G. Tartaglia, and M. Vendruscolo The Zyggregator method for predicting protein aggregation propensities Chem. Soc. Rev. 37 2008 1395 1401
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 1395-1401
    • Tartaglia, G.G.1    Vendruscolo, M.2
  • 24
    • 33845605514 scopus 로고    scopus 로고
    • "prion-proof" for [PIN+]: Infection with in vitro-made amyloid aggregates of Rnq1p-(132-405) induces [PIN+]
    • B.K. Patel, and S.W. Liebman "Prion-proof" for [PIN+]: infection with in vitro-made amyloid aggregates of Rnq1p-(132-405) induces [PIN+] J. Mol. Biol. 365 2007 773 782
    • (2007) J. Mol. Biol. , vol.365 , pp. 773-782
    • Patel, B.K.1    Liebman, S.W.2
  • 25
    • 84953729964 scopus 로고    scopus 로고
    • Recombinant Human Semenogelin-1 (Sg1) and Sg1 (1-159) form Detergent Stable Amyloid like Aggregates in vitro
    • N. Sharma, V. Sivalingam, and B.K. Patel Recombinant Human Semenogelin-1 (Sg1) and Sg1 (1-159) form Detergent Stable Amyloid like Aggregates in vitro Protein Pept. Lett. 23 2015 87 96
    • (2015) Protein Pept. Lett. , vol.23 , pp. 87-96
    • Sharma, N.1    Sivalingam, V.2    Patel, B.K.3
  • 28
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: Detection of amyloid aggregation in solution
    • H. LeVine 3rd Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution Protein Sci. 2 1993 404 410
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • LeVine, H.1
  • 29
    • 79956311051 scopus 로고    scopus 로고
    • A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions
    • Y. Furukawa, K. Kaneko, S. Watanabe, K. Yamanaka, and N. Nukina A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions J. Biol. Chem. 286 2011 18664 18672
    • (2011) J. Biol. Chem. , vol.286 , pp. 18664-18672
    • Furukawa, Y.1    Kaneko, K.2    Watanabe, S.3    Yamanaka, K.4    Nukina, N.5
  • 30
    • 0024352110 scopus 로고
    • Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation
    • W.E. Klunk, J.W. Pettegrew, and D.J. Abraham Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation J. Histochem Cytochem 37 1989 1273 1281
    • (1989) J. Histochem Cytochem , vol.37 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 32
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • N. Sreerama, and R.W. Woody A self-consistent method for the analysis of protein secondary structure from circular dichroism Anal. Biochem. 209 1993 32 44
    • (1993) Anal. Biochem. , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 33
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • L. Whitmore, and B.A. Wallace DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data Nucleic Acids Res. 32 2004 W668 W673
    • (2004) Nucleic Acids Res. , vol.32 , pp. W668-W673
    • Whitmore, L.1    Wallace, B.A.2
  • 36
    • 58149400915 scopus 로고    scopus 로고
    • Conformational conversion may precede or follow aggregate elongation on alternative pathways of amyloid protofibril formation
    • S. Kumar, and J.B. Udgaonkar Conformational conversion may precede or follow aggregate elongation on alternative pathways of amyloid protofibril formation J. Mol. Biol. 385 2009 1266 1276
    • (2009) J. Mol. Biol. , vol.385 , pp. 1266-1276
    • Kumar, S.1    Udgaonkar, J.B.2
  • 38
    • 84959524549 scopus 로고    scopus 로고
    • New insights into in vitro amyloidogenic properties of human serum albumin suggest considerations for therapeutic precautions
    • N. Sharma, V. Sivalingam, S. Maurya, A. Prasad, P. Khandelwal, S.C. Yadav, and B.K. Patel New insights into in vitro amyloidogenic properties of human serum albumin suggest considerations for therapeutic precautions FEBS Lett. 589 2015 4033 4038
    • (2015) FEBS Lett. , vol.589 , pp. 4033-4038
    • Sharma, N.1    Sivalingam, V.2    Maurya, S.3    Prasad, A.4    Khandelwal, P.5    Yadav, S.C.6    Patel, B.K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.