Synapse
⌘+K
Synapse
PulseExploreClubsResearchersJournals
Instagram
HomeClubsExplore
August 28, 2001Biochemistry

Effect of Familial Parkinson's Disease Point Mutations A30P and A53T on the Structural Properties, Aggregation, and Fibrillation of Human α-Synuclein

View Full Paper
Ask AI
Bookmark
Share

Authors

JLJie LiUniversity of South CarolinaVUVladimir N. UverskyUniversity of California, RiversideAFAnthony L. FinkUniversity of California, Riverside

Discussion

Loading...

Member takes

Overview

Key Points

Key points are not available for this paper at this time.

Cite This Study

Li et al. (2001) studied this question.

synapsesocial.com/papers/69e13edb73d2bbd124b96f27https://doi.org/10.1021/bi010616g
View Full Paper
Ask AI
Bookmark
Share

Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Synthetic filaments assembled from C‐terminally truncated α‐synuclein1998 · 424 citations
  2. 2PHASE AND ELECTRON MICROSCOPIC OBSERVATIONS OF LEWY BODIES AND MELANIN GRANULES IN THE SUBSTANTIA NIGRA AND LOCUS CAERULEUS IN PARKINSONʼS DISEASE1965 · 350 citations
  3. 3Fibrils Formed in Vitro from α-Synuclein and Two Mutant Forms Linked to Parkinson's Disease are Typical Amyloid2000 · 795 citations
  4. 4Mutant and Wild Type Human α-Synucleins Assemble into Elongated Filaments with Distinct Morphologies in Vitro1999 · 512 citations