Crystal structure and assembly of a eukaryotic small heat shock protein
By R. Montfort, E. Basha, K. Friedrich, C. Slingsby, E. Vierling. Nature Structural Biology, 2001
737 citations recorded by the source corpus.
Subfields: Materials Chemistry, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/5ad10ac48aa5a238c2a20c67cc3293669026e36b
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In Molecular Biology
Citations in the corpus
- Crystal structure of truncated human βB1‐crystallin (2003, background): “…with A3 (Werten et al. 1999) indicate that they might play a crucial role in higher oligomer assembly in ways that echo the function of N- and C-terminal extensions in higher oligomer assembly of the small heat shock protein family of which -crystallin is a member (van Montfort et al. 2001).”
- Complexity of the heat stress response in plants. (2007, neutral): “9 from wheat [19].”
- A critical motif for oligomerization and chaperone activity of bacterial α‐heat shock proteins (2002, background): “The functional, substrate-binding entitymight actually be an a-Hsp dimer rather than the fully oligomerized particle, which is regarded as a transient storage form of the chaperone [34,44].”
- Ageing and vision: structure, stability and function of lens crystallins. (2004, background): “…protein evokes the heat shock response, while unfolding endoplasmic reticulum protein evokes the unfolded protein response (for review, see Morimoto and Santoro, 1998; van den IJssel et al., 1999; Patil and Walter, 2001; van Montfort et al., 2001; Arrigo and M .uller, 2002; Sonna et al., 2002).”
- The human genome encodes 10 α-crystallin–related small heat shock proteins: HspB1–10 (2003, background): “Correspondence to: Wilfried W. de Jong, Tel: 31-24-3616848; Fax: 31-24- 3540525; E-mail: w.dejong@ncmls.kun.nl. structures are only known for an archaebacterial (Kim et al 1998) and a plant sHsp (van Montfort et al 2001).”