Amyloidose - Versionsgeschichte

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2011-07-19T00:02:14Z

who

Frankhard61 am 14. März 2011 um 13:49 Uhr

2011-03-14T13:49:11Z

Frankhard61 am 14. März 2011 um 13:46 Uhr

2011-03-14T13:46:44Z

Ossip Groth am 21. Februar 2010 um 06:51 Uhr

2010-02-21T06:51:48Z

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2010-01-20T16:54:51Z

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| align="left" width="800" |<ref name="PMID12135474">Amyloid-fibril formation. Proposed mechanisms and relevance to conformational disease. Eur J Biochem 269(14):3362-71 (2002) PMID 12135474 </ref><ref name="PMID16302962">Mechanisms of amyloid fibril self-assembly and inhibition. Model short peptides as a key research tool. FEBS J 272(23):5971-8 (2005) PMID 16302962 </ref><ref name="PMID16302961">The Yin and Yang of protein folding. FEBS J 272(23):5962-70 (2005) PMID 16302961 </ref><ref name="PMID16302960">Structures for amyloid fibrils. FEBS J 272(23):5950-61 (2005) PMID 16302960 </ref><ref name="PMID16302959">Aspects on human amyloid forms and their fibril polypeptides. FEBS J 272(23):5942-9 (2005) PMID 16302959 </ref><ref name="PMID19433089">Glimpses of the molecular mechanisms of beta2-microglobulin fibril formation in vitro: aggregation on a complex energy landscape. FEBS Lett 583(16):2623-9 (2009) PMID 19433089 </ref><ref name="PMID18723507">Structural classification of toxic amyloid oligomers. J Biol Chem 283(44):29639-43 (2008) PMID 18723507 </ref><ref name="PMID18723506">The AbetaCs of Abeta-cleaving proteases. J Biol Chem 283(44):29645-9 (2008) PMID 18723506 </ref><ref name="PMID18650431">The role of amyloid precursor protein processing by BACE1, the beta-secretase, in Alzheimer disease pathophysiology. J Biol Chem 283(44):29621-5 (2008) PMID 18650431 </ref><ref name="PMID18650430">Amyloid precursor protein trafficking, processing, and function. J Biol Chem 283(44):29615-9 (2008) PMID 18650430 </ref><ref name="PMID19597329">Structural polymorphism of Alzheimer Abeta and other amyloid fibrils. Prion 3(2):89-93 (2009) PMID 19597329 </ref><ref name="PMID19270506">The multiple mechanisms of amyloid deposition: the role of parkin. Prion 3(1):5-11 (2009) PMID 19270506 </ref><ref name="PMID19158505">Amyloid fibrils: abnormal protein assembly. Prion 2(3):112-7 (2008) PMID 19158505 </ref><ref name="PMID19164927">Computational simulations of the early steps of protein aggregation. Prion 1(1):3-8 (2007) PMID 19164927 </ref><ref name="PMID19164912">Hacking the code of amyloid formation: the amyloid stretch hypothesis. Prion 1(1):9-14 (2007) PMID 19164912 </ref><ref name="PMID15070716">Unzipping the mysteries of amyloid fiber formation. Proc Natl Acad Sci U S A 101(13):4335-6 (2004) PMID 15070716 </ref><ref name="PMID15610843">Polychlorinated biphenyls inhibit amyloid fibril formation. Chem Biol 11(12):1604-6 (2004) PMID 15610843 </ref><ref name="PMID11412857">Transthyretin amyloidosis: a tale of weak interactions. FEBS Lett 498(2-3):201-3 (2001) PMID 11412857 </ref><ref name="PMID12176381">Ideas of order for amyloid fibril structure. Structure 10(8):1031-6 (2002) PMID 12176381 </ref><ref name="PMID9195890">Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases. Structure 5(5):595-600 (1997) PMID 9195890 </ref>
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| bgcolor="#dfdfdf" | '''Medline Suchterm/ Synonyme'''
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| bgcolor="#00dfdf" | '''Was ist das'''
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| bgcolor="#dfdfdf" | '''Struktur'''
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| bgcolor="#dfdfdf" | '''Physiologie'''
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| bgcolor="#dfdfdf" | '''Knockout'''
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| bgcolor="#dfdfdf" | '''Transgen'''
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| bgcolor="#dfdfdf" | '''Mutation'''
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| bgcolor="#dfdfdf" | '''Polymorphismus'''
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| bgcolor="#dfdfdf" | '''Genexpression'''
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| bgcolor="#dfdfdf" | '''Inhibitoren'''
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| bgcolor="#dfdfdf" | '''Agonisten'''
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== Bibliographie ==
<references />