Atomic structures of amyloid cross-β spines reveal varied steric zippers

By M. Sawaya, S. Sambashivan, R. Nelson, M. Ivanova, Stuart A. Sievers, M. Apostol, Michael J. Thompson, M. Balbirnie, J. Wiltzius, Heather T Mcfarlane and 3 more. Nature, 2007

2,061 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/9a64de45e99e743474bd5cda0de4dd4355a61fff

How researchers see this paper

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

In Materials Chemistry

1. Nigel W. Moriarty
2. Pavel V. Afonine
3. Min Zheng
4. Mark P. Waller
5. Jeffrey R. Reimers
6. Vladimir N Uversky
7. R. Tycko
8. A. Paravastu

In Molecular Biology

1. Zhijian J. Chen
2. Nigel W. Moriarty
3. Pavel V. Afonine
4. A. Paravastu
5. Richard Leapman
6. Oliver D. King
7. Lijun Sun
8. R. Tycko

In Physiology

1. A. Paravastu
2. Richard Leapman
3. Wai-Ming Yau
4. R. Tycko
5. Zhijian J. Chen
6. Jessica W. Wu
7. Vladimir N Uversky
8. L. Breydo

Citations in the corpus

• Stress granules as crucibles of ALS pathogenesis (2013, background): “Disease-linked mutations in the prion-like domain of hnRNPA1 and hnRNPA2/B1 introduce a potent steric zipper, which can form two self-complementary sheets that comprise the spine of an amyloid fibril (Sawaya et al., 2007).”
• Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils (2008, background): “In addition to creating a hydrophobic core, the parallel nature of the -sheets may permit ‘‘polar zipper’’ interactions among Q15 sidechains (31), which fit into a cavity created by G37 and G38 in a manner reminiscent of the ‘‘steric zippers’’ that have been observed in amyloid-like peptide crystal ”
• The RIP1/RIP3 Necrosome Forms a Functional Amyloid Signaling Complex Required for Programmed Necrosis (2012, positive): “This type of packing is remarkably similar to the structure of the VQIVYK sequence from tau (PDB 2ON9) (Sawaya et al., 2007), a microtubule-associated protein that plays an important role in stabilizing axonal microtubules.”
• Α-synuclein misfolding and Parkinson's disease. (2012, background): “These studies were later confirmed by X-ray diffraction ofmany short amyloid peptides, including a small segment from α-synuclein [64, 67].”
• The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease (2012, background): “…structures that are each capable of conformational self-replication via templating the conversion of other copies of the same protein (Alberti et al., 2009; Gendoo and Harrison, 2011; Goldschmidt et al., 2010; Halfmann et al., 2011; Sawaya et al., 2007; Toombs et al., 2010; Wiltzius et al., 2009).”