The protofilament structure of insulin amyloid fibrils
By J. L. Jimenez, E. J. Nettleton, Mario Bouchard, Carol V. Robinson, Christopher M. Dobson, H. Saibil. Proceedings of the National Academy of Sciences of the United States of America, 2002
837 citations recorded by the source corpus.
Subfields: Molecular Biology, Physiology, Rheumatology
View Paper: https://www.semanticscholar.org/paper/60bf3e5ddac94662c1cec6484c549e7f74b756de
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
- Christopher M. Dobson
- S. Marciniak
- R. Tycko
- A. Paravastu
- Richard Leapman
- Wai-Ming Yau
- D. Ron
- M. Krebs
In Physiology
- Christopher M. Dobson
- R. Tycko
- Wai-Ming Yau
- A. Paravastu
- Richard Leapman
- Fabrizio Chiti
- Michele Vendruscolo
Citations in the corpus
- Endoplasmic reticulum stress signaling in disease. (2006, background): “In contrast, amyloid can be formed through polymerization of a number of otherwise unrelated proteins, each causing a distinct disease (79, 148, 207).”
- AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides (2007, neutral): “Insulin 1–38 12–19 1/3 [66]”
- FTIR reveals structural differences between native β‐sheet proteins and amyloid fibrils (2004, background): “It is of note that the latter conclusion is supported independently by cryo-electron microscopy, which also has suggested that amyloid fibrils have smaller twist angles compared with native proteins (Jimenez et al. 2002).”
- Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils. (2006, background): “As represented in recent models for amyloid structures (7, 10, 14, 29, 36, 42, 44, 51-59) and supported by recent x-ray crystal structures of short amyloid-forming peptides (60), the core of an amyloid fibril contains two or more layers of β-sheets.”
- Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils (2008, methodology): “Here, we describe an experimentally-based structural model for fibrils formed by the 40-residue Alzheimer’s -amyloid peptide (A 1–40) that applies specifically to fibrils with a characteristic periodically-twisted morphology in transmission electron microscopy (TEM) images, sometimes described as a ”
- Principles of protein folding, misfolding and aggregation. (2004, background): “[61] Jiménez JL, Nettleton EJ, Bouchard M, Robinson CV, Dobson CM, Saibil HR.”