메뉴 건너뛰기




Volumn 110, Issue 9, 2002, Pages 1219-1220

The cellular response to aggregated proteins associated with human disease

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTITRYPSIN; AMYLOID PRECURSOR PROTEIN; GENE PRODUCT; MUTANT PROTEIN; SERINE PROTEINASE INHIBITOR; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 0036840193     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI200216780     Document Type: Short Survey
Times cited : (23)

References (15)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C.B. 1973. Principles that govern the folding of protein chains. Science. 181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 0036841958 scopus 로고    scopus 로고
    • Protein aggregation in disease: A role of folding intermediates forming specific multimeric interactions
    • doi: 10.1172/JCI200216781
    • Horwich, A. 2002. Protein aggregation in disease: A role of folding intermediates forming specific multimeric interactions. J. Clin. Invest. 110:1221-1232. doi: 10.1172/JCI200216781.
    • (2002) J. Clin. Invest. , vol.110 , pp. 1221-1232
    • Horwich, A.1
  • 3
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini, M., et al. 2002. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature. 416:507-511.
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1
  • 4
    • 0036855661 scopus 로고    scopus 로고
    • Deciphering the genesis and fate of amyloid-β protein yields novel therapies for Alzheimer disease
    • In press
    • Selkoe, D.J. 2002. Deciphering the genesis and fate of amyloid-β protein yields novel therapies for Alzheimer disease. J. Clin. Invest. In press.
    • (2002) J. Clin. Invest.
    • Selkoe, D.J.1
  • 5
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid? Protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D.M., et al. 2002. Naturally secreted oligomers of amyloid? Protein potently inhibit hippocampal long-term potentiation in vivo. Nature. 416:535-539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1
  • 7
    • 0032526433 scopus 로고    scopus 로고
    • Role of the proteosome in membrane extraction of a shortlived ER-transmembrane protein
    • Mayer, T., Braun, T., and Jentsch, S. 1998. Role of the proteosome in membrane extraction of a shortlived ER-transmembrane protein. EMBO J. 17:3251-3257.
    • (1998) EMBO J. , vol.17 , pp. 3251-3257
    • Mayer, T.1    Braun, T.2    Jentsch, S.3
  • 8
    • 0036853914 scopus 로고    scopus 로고
    • Orchestrating the unfolded protein response in health and disease
    • In press
    • Kaufman, R. 2002. Orchestrating the unfolded protein response in health and disease. J. Clin. Invest. In press.
    • (2002) J. Clin. Invest.
    • Kaufman, R.1
  • 9
    • 0036856008 scopus 로고    scopus 로고
    • Translational control in the endoplasmic reticulum stress response
    • In press
    • Ron, D. 2002. Translational control in the endoplasmic reticulum stress response. J. Clin. Invest. In press.
    • (2002) J. Clin. Invest.
    • Ron, D.1
  • 10
    • 0036175128 scopus 로고    scopus 로고
    • Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes
    • doi:10.1172/JCI200214550
    • Oyadomari, S., et al. 2002. Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes. J. Clin. Invest. 109:525-532. doi:10.1172/JCI200214550.
    • (2002) J. Clin. Invest. , vol.109 , pp. 525-532
    • Oyadomari, S.1
  • 11
    • 0036896021 scopus 로고    scopus 로고
    • Rescuing protein conformation: Prospects for pharmacological therapy in cystic fibrosis
    • In press
    • Gelman, M.S., and Kopito, R.R. 2002. Rescuing protein conformation: Prospects for pharmacological therapy in cystic fibrosis. J. Clin. Invest. In press.
    • (2002) J. Clin. Invest.
    • Gelman, M.S.1    Kopito, R.R.2
  • 12
    • 85047684827 scopus 로고    scopus 로고
    • α1-antitrypsin polymerization and the serpinopath: Pathobiology and prospects for therapy
    • In press
    • Lomas, D.A., and Mahadeva, R. 2002. α1-antitrypsin polymerization and the serpinopath: Pathobiology and prospects for therapy. J. Clin. Invest. In press.
    • (2002) J. Clin. Invest.
    • Lomas, D.A.1    Mahadeva, R.2
  • 13
    • 0033598346 scopus 로고    scopus 로고
    • Familial dementia caused by polymerization of mutant neuroserpin
    • Davis, R.L., et al. 1999. Familial dementia caused by polymerization of mutant neuroserpin. Nature. 401:376-379.
    • (1999) Nature , vol.401 , pp. 376-379
    • Davis, R.L.1
  • 14
    • 85060564827 scopus 로고    scopus 로고
    • Liver injury in α1-antitrypsin deficiency: Role of autophagy and mitochondrial injury in response to aggregated protein in the endoplasmic reticulum
    • In press
    • Perlmutter, D.H. 2002. Liver injury in α1-antitrypsin deficiency: Role of autophagy and mitochondrial injury in response to aggregated protein in the endoplasmic reticulum. J. Clin. Invest. In press.
    • (2002) J. Clin. Invest.
    • Perlmutter, D.H.1
  • 15
    • 0037162451 scopus 로고    scopus 로고
    • Association ofcalnexin with mutant peripheral myelin protein-22 ex vivo: A basis for "gain-of-function" ER diseases
    • Dickson, K.M., et al. 2002. Association ofcalnexin with mutant peripheral myelin protein-22 ex vivo: A basis for "gain-of-function" ER diseases. Proc. Natl. Acad. Sci. USA. 99:9852-9857.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9852-9857
    • Dickson, K.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.