FTIR reveals structural differences between native β‐sheet proteins and amyloid fibrils

By G. Zandomeneghi, M. Krebs, Margaret G. McCammon, M. Fändrich. Protein Science, 2004

665 citations recorded by the source corpus.

Subfields: Molecular Biology, Physiology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/951dfd4bc4e697e7d4980eaa9aa4ca2a29bb97b3

How researchers see this paper

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

In Molecular Biology

1. Fabrizio Chiti
2. Christopher M. Dobson
3. Michele Vendruscolo
4. Tuomas P. J. Knowles
5. F. Hartl
6. M. Hayer-Hartl
7. D. Selkoe
8. E. K. Kim

In Physiology

1. Christopher M. Dobson
2. Fabrizio Chiti
3. Michele Vendruscolo
4. Tuomas P. J. Knowles
5. F. Hartl
6. E. K. Kim
7. E. Choi

In Spectroscopy

1. Christopher M. Dobson
2. Fabrizio Chiti

Citations in the corpus

• The RIP1/RIP3 Necrosome Forms a Functional Amyloid Signaling Complex Required for Programmed Necrosis (2012, neutral): “Fourier transform infrared spectroscopy (FTIR) has been well established to distinguish cross-b amyloid fibrils from native b sheet proteins in that the former shows amide I0 maxima between 1,610 cm 1 and 1,630 cm 1 in wavenumbers, which is smaller than native b sheet proteins (Zandomeneghi et al., ”
• Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, methodology): “The fibrils possess a cross-β structure, in which β-strands are oriented perpendicularly to the fibril axis and are assembled into β-sheets that run the length of the fibrils, as initially detected using X-ray fiber diffraction (74), with recent support from Fourier transform infrared spectroscopy, ”