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|a pubmed24n0502.xml
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|a (DE-627)NLM150538243
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|a (NLM)15379486
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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100 |
1 |
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|a Li, Changqing
|e verfasserin
|4 aut
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1 |
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|a Amyloid-like formation by self-assembly of peptidolipids in two dimensions
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|c 2004
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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|a Band
|b nc
|2 rdacarrier
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|a Date Completed 21.08.2006
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|a Date Revised 18.11.2010
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|a published: Print
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|a Citation Status MEDLINE
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|a The accumulation of beta-amyloid peptide (Abeta) in the human brain is known to be the major cause that drives Alzheimer's disease pathogenesis. Abeta, a 39-42 amino acid peptide, is the cleavage product of amyloid precursor protein in the hydrophobic transmembrane region. The present study employs a two-dimensional (2D) approach. Two synthetic peptidolipids, C18-IIGLM-OH and C18-IIGLM-NH2, are selected based on the fragment 31-35 of Abeta which is recognized as one of the determining segments that induces formation of amyloid fibril plaques. The aliphatic hydrocarbon chain C18 is attached to the N-terminal of the fragment 31-35 to facilitate the 2D study at the air-water interface. The aggregation process is observed by two measurements: (1) surface pressure-area and surface dipole moment-area isotherms and (2) epifluorescence microscopy of the Langmuir films to investigate the topography of the amyloid-like formation
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Amyloid
|2 NLM
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|a Amyloid beta-Peptides
|2 NLM
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|a Lipids
|2 NLM
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|a Peptide Fragments
|2 NLM
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|a amyloid beta-protein (31-35)
|2 NLM
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|a Orbulescu, Jhony
|e verfasserin
|4 aut
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1 |
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|a Sui, Guodong
|e verfasserin
|4 aut
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1 |
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|a Leblanc, Roger M
|e verfasserin
|4 aut
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773 |
0 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 20(2004), 20 vom: 28. Sept., Seite 8641-5
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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|g volume:20
|g year:2004
|g number:20
|g day:28
|g month:09
|g pages:8641-5
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|a AR
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|d 20
|j 2004
|e 20
|b 28
|c 09
|h 8641-5
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