Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine.
By C. Scheufler, A. Brinker, G. Bourenkov, S. Pegoraro, L. Moroder, H. Bartunik, F. Hartl, I. Moarefi. Cell, 2000
1,225 citations recorded by the source corpus.
Subfields: Molecular Biology, Physical and Theoretical Chemistry
View Paper: https://www.semanticscholar.org/paper/3533018eaf86c29a24e9faeb9087ab67375b471f
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
- Andrei N. Lupas
- Johannes Söding
- Jérôme Tubiana
- Manjunatha R. Karpenahalli
- Nevan J. Krogan
- Rémi Monasson
- T. Cavalier‐Smith
- Jack Greenblatt
Citations in the corpus
- The phagotrophic origin of eukaryotes and phylogenetic classification of Protozoa. (2002, background): “An evolutionarily chimaeric origin for centrosomes is possible, since Hsp90 and Hsp70 and γ-tubulin are key structural constituents (Lange et al., 2000; Scheufler et al., 2000).”
- Learning protein constitutive motifs from sequence data (2018, background): “SA, one of the 103, 406 distinct structures that a 27-mer can adopt on the cubic lattice Shakhnovich and Gutin (1990). Circled sites are related to the features shown in panel 6C.”
- Hsp90: a specialized but essential protein-folding tool. (2001, background): “Hydrophobic interactions with the divergent NH 2 termini of the peptides account for the specificity of binding (Scheufler et al., 2000).”
- Cargo of Kinesin Identified as Jip Scaffolding Proteins and Associated Signaling Molecules (2001, background): “In analogy to other TPR domain–containing proteins (Terlecky et al., 1995; Das et al., 1998; Groves and Barford, 1999; Scheufler et al., 2000), it is likely that three or more TPR motifs of KLC generate an extended surface groove that provides the docking site for the linear JIP-1 (and presumably…”
- Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. (2005, methodology): “It is proposed that the N-terminal domain of Hop binds to the C-terminal EEVD motif of Hsp70, while the two C-terminal TPR domains bind the C-terminal EEVD motif of Hsp90 (Scheufler et al., 2000; Brinker et al., 2002).”
- TPRpred: a tool for prediction of TPR-, PPR- and SEL1-like repeats from protein sequences (2007, background): “tein folding, by virtue of their tendency to bind target proteins [5,7,8].”