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Volumn 22, Issue 2, 2006, Pages 605-608

Predicting solvent and aggregation effects of peptides using group contribution calculations

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; BIOTECHNOLOGY; OLIGOMERS; PROTEINS; SOLVENTS; TISSUE;

EID: 33646049045     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp050407d     Document Type: Article
Times cited : (9)

References (15)
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    • Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies
    • Kirkitadze, M. D.; Bitan, G.; Teplow, D. B. Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies. J. Neurosci. Res. 2002, 69, 567-577.
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  • 4
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    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R.; Head, E.; Thompson, J. L.; McIntire, T. M.; Milton, S. C.; Cotman, C. W.; Glabe, C. C. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003, 300, 486-489.
    • (2003) Science , vol.300 , pp. 486-489
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    • Structure-function relationships for inhibitors of beta-amyloid toxicity containing the recognition sequence KLVFF
    • Lowe, T. L.; Strzelec, A.; Kiessling, L. L.; Murphy, R. M. Structure-function relationships for inhibitors of beta-amyloid toxicity containing the recognition sequence KLVFF. Biochemistry 2001, 40, 7882-7889.
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  • 7
    • 0142103473 scopus 로고    scopus 로고
    • Targeted control of kinetics of beta-amyloid self-association by surface tension-modifying peptides
    • Kim, J. R.; Gibson, T. J.; Murphy, R. M. Targeted control of kinetics of beta-amyloid self-association by surface tension-modifying peptides. J. Biol. Chem. 2003, 278, 40730-40735.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40730-40735
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  • 8
    • 20544440379 scopus 로고    scopus 로고
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    • Gibson, T.J.1    Murphy, R.M.2
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.