Kinetic control of dimer structure formation in amyloid fibrillogenesis.

@article{Hwang2004KineticCO,
  title={Kinetic control of dimer structure formation in amyloid fibrillogenesis.},
  author={Wonmuk Hwang and Shuguang Zhang and Roger D. Kamm and Martin Karplus},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2004},
  volume={101 35},
  pages={
          12916-21
        }
}
Amyloid fibril formation involves nonfibrillar oligomeric intermediates, which are important as possible cytotoxic species in neurodegenerative diseases. However, their transient nature and polydispersity have made it difficult to identify their formation mechanism or structure. We have investigated the dimerization process, the first step in aggregate formation, by multiple molecular dynamics simulations of five beta-sheet-forming peptides. Contrary to the regular beta-sheet structure of the… CONTINUE READING

Citations

Publications citing this paper.
SHOWING 1-10 OF 72 CITATIONS, ESTIMATED 56% COVERAGE

Thermodynamic Selection of Steric Zipper Patterns in the Amyloid Cross-β Spine

  • PLoS Computational Biology
  • 2009
VIEW 5 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED

FILTER CITATIONS BY YEAR

2005
2019

CITATION STATISTICS

  • 3 Highly Influenced Citations

References

Publications referenced by this paper.

Similar Papers