EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers

By Dagmar E. Ehrnhoefer, J. Bieschke, A. Boeddrich, M. Herbst, L. Masino, R. Lurz, S. Engemann, A. Pastore, Erich E. Wanker. Nature Structural &Molecular Biology, 2008

1,398 citations recorded by the source corpus.

Subfields: Complementary and alternative medicine, Neurology, Physiology

View Paper: https://www.semanticscholar.org/paper/4fcd27b38b8fafbc7f722fd95091d4bb34d24abe

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

1. J. Bieschke
2. Jenny Russ
3. R. Friedrich
4. Heike J Wobst
5. K. Neugebauer
6. Erich E. Wanker
7. Dagmar E. Ehrnhoefer
8. L. Breydo

Citations in the corpus

• EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity (2010, methodology): “The membrane was then stained with NBT, a substance that specifically detects EGCG-bound polypeptide chains (6).”