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Volumn 298, Issue 5599, 2002, Pages 1785-1788

Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; CONFORMATIONS; DISEASES;

EID: 0037195617     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1073619     Document Type: Article
Times cited : (274)

References (30)
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    • Unglycosylated proteins are more likely to misfold in the ER and be subject to retrograde transport; in addition, glycosylated species that are retrogradely transported are subject to cytoplasmic deglycosidases.
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    • Stronger proteasome-inhibiting activity is exhibited by 50 μM MG132 than by 10 μM lactacystin.
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    • There are two possible reasons for this phenomenon: (i) The nucleus is formed from a subset of specific conformers, all of which must come together at the same time, or (ii) the nucleus is formed from still molten conformers that must be free to associate with each other and cannot be constrained by other interactions (e.g., bound to chaperones).
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    • note
    • Factors that may influence the conversion of PrP include the unfolded state that is associated with transport from ER to the cytosol, interactions with cytosolic chaperones, the reducing environment of the cytosol, the unglycosylated state of the transported protein, the local concentration of cytosolic PrP, the efficiency of the proteasome, and the effect of specific mutations on folding.
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    • published online 17 October (10.1126/science.1073725)
    • J. Ma, S. Lindquist, Science 298, 1785; published online 17 October 2002 (10.1126/science.1073725).
    • (2002) Science , vol.298 , pp. 1785
    • Ma, J.1    Lindquist, S.2
  • 30
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    • note
    • We thank R. Kopito, B. Caughey, S. Priola, and P. Thomas for various reagents, and members of the Lindquist lab for critical reading of the manuscript. Supported by NIH grant GMS 25874 and by HHMI.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.