The Dependence of Amyloid‐β Dynamics on Protein Force Fields and Water Models

Publisher： John Wiley & Sons Inc

E-ISSN： 1439-7641|16|15|3278-3289

ISSN： 1439-4235

Source： CHEMPHYSCHEM, Vol.16, Iss.15, 2015-10, pp. : 3278-3289

Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.

Previous Menu Next

Abstract

Related content

Single‐Molecule Imaging Reveals that Small Amyloid‐β1–42 Oligomers Interact with the Cellular Prion Protein (PrPC)

By  

CHEMBIOCHEM, Vol. 15, Iss. 17, 2014-11 ,pp. : 2515-2521

John Wiley & Sons Inc

Access to resources Recommend Favorite

Polarizable force fields for molecular dynamics simulations of biomolecules

By  

WILEY INTERDISCIPLINARY REVIEWS: COMPUTATIONAL MOLECULAR SCIENCE (ELECTRONIC), Vol. 5, Iss. 2, 2015-03 ,pp. : 241-254

John Wiley & Sons Inc

Access to resources Recommend Favorite

Confined Water in Amyloid‐Competent Oligomers of the Prion Protein

By  

CHEMPHYSCHEM, Vol. 17, Iss. 18, 2016-09 ,pp. : 2804-2807

John Wiley & Sons Inc

Access to resources Recommend Favorite

Targeted Magnetic Nanoparticles for Remote Magnetothermal Disruption of Amyloid‐β Aggregates

By  

ADVANCED HEALTHCARE MATERIALS (ELECTRONIC), Vol. 4, Iss. 14, 2015-10 ,pp. : 2100-2109

John Wiley & Sons Inc

Access to resources Recommend Favorite

Targeted Magnetic Nanoparticles for Remote Magnetothermal Disruption of Amyloid‐β Aggregates

By  

ADVANCED HEALTHCARE MATERIALS (ELECTRONIC), Vol. 2192-2640, Iss. 14, 2015-10 ,pp. : 2100-2109

John Wiley & Sons Inc

Access to resources Recommend Favorite