Structural studies and cytotoxicity assays of "aggregation-prone" IAPP(8-16) and its non-amyloidogenic variants suggest its important role in fibrillogenesis and cytotoxicity of human amylin.
about
A common 'aggregation-prone' interface possibly participates in the self-assembly of human zona pellucida proteins.Mining databases for protein aggregation: a review.From Peptide Fragments to Whole Protein: Copper(II) Load and Coordination Features of IAPP.Exploring Amyloidogenicity of Clusterin: A Structural and Bioinformatics Analysis.Identification of an amyloid fibril forming segment of human Pmel17 repeat domain (RPT domain).
P2860
Structural studies and cytotoxicity assays of "aggregation-prone" IAPP(8-16) and its non-amyloidogenic variants suggest its important role in fibrillogenesis and cytotoxicity of human amylin.
description
2015 nî lūn-bûn
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2015年の論文
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2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
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2015年论文
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2015年论文
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name
Structural studies and cytotox ...... cytotoxicity of human amylin.
@en
type
label
Structural studies and cytotox ...... cytotoxicity of human amylin.
@en
prefLabel
Structural studies and cytotox ...... cytotoxicity of human amylin.
@en
P2093
P2860
P50
P356
P1433
P1476
Structural studies and cytotox ...... cytotoxicity of human amylin.
@en
P2093
Christina Cheimonidou
Eleni V Pappa
George Pairas
Ioannis P Trougakos
Paul Cordopatis
Stavros J Hamodrakas
Vassiliki A Iconomidou
Vassiliki Magafa
P2860
P304
P356
10.1002/BIP.22650
P577
2015-05-01T00:00:00Z