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Mechanisms of amyloid fibril formation - focus on domain-swapping

  • Published:2011-05-31 Issue:13 Volume:278 Page:2263-2282
  • ISSN:1742-464X
  • Container-title:FEBS Journal
  • language:en
  • Short-container-title:

Author:

Žerovnik Eva,Stoka Veronika,Mirtič Andreja,Gunčar Gregor,Grdadolnik Jože,Staniforth Rosemary A.,Turk Dušan,Turk Vito

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Cited by 61 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Key charged residues influence the amyloidogenic propensity of the helix-1 region of serum amyloid A;Biochimica et Biophysica Acta (BBA) - General Subjects;2024-11

2. Why is Dimeric 3D Domain Swapping in Antibody Light Chains Missing from the Solution? Atomistic Insights Mechanisms;The Journal of Physical Chemistry B;2024-09-13

3. Structural determinants of odorant-binding proteins affecting their ability to form amyloid fibrils;International Journal of Biological Macromolecules;2024-04

4. MFG-E8, A Novel Biomarker for Alzheimer’s Disease and Its Amyloidotic Feature;The Global Burden of Disease and Risk Factors - Understanding and Management;2024-02-01

5. Pathways of amyloid fibril formation and protein aggregation;Progress in Molecular Biology and Translational Science;2024
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