Crystal Structure of the Ribosome at 5.5 Å Resolution

By M. Yusupov, G. Yusupova, A. Baucom, K. Lieberman, T. Earnest, J. Cate, H. Noller. Science, 2001

1,966 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/de448d80f1020bd553aba6659215caa10254c101

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

In Molecular Biology

Citations in the corpus

Identification of conserved regions in the plastid genome: implications for DNA barcoding and biological function (2006, background): “These highly conserved regions, which can be used as priming sites for PCR amplification, represent two segments of the internal loop in the center of the plastid 23S rDNA domain V (Yusupov et al. 2001), and are thus named p23SrV_f (5’-TGGACAGAAAGACCCTATGAAGCTT-3’) and p23SrV_r (5’- ATAAAAGTTACTCTAG”
The antiquity of RNA-based evolution (2002, background): “Although there may never be direct physical evidence of an RNA-based organism, because the RNA world is likely to have been extinct for almost four billion years, molecular archaeologists have uncovered artefacts of this ancestral era, none more pronounced than the recently reported crystal structur”
Studies on the role of helix 69 of 23S rRNA in the factor-dependent stages of translation initiation, elongation, and termination (2011, methodology): “While the RNA-RNA bridges tend to be centrally located, the protein bridges are in the periphery of the interface (Cate et al. 1999; Yusupov et al. 2001), particularly in the “head” region of the small subunit that is known to undergo large 35 movements during translocation (Zhang et al. 2009; Gao…”
Principles of protein folding, misfolding and aggregation. (2004, background): “Recently, a combination of electron microscopy and X-ray crystallography has revealed detailed structures of these complex “molecular machines” [31], no mean feat given that they contain more than 50 different proteins and three large RNA molecules.”
Initiation factor 2 stabilizes the ribosome in a semirotated conformation (2015, background): “Proc Natl Acad Sci USA 110(39):15656–15661.”
Natively unfolded proteins: A point where biology waits for physics (2002, background): “…the 50S ribosomal proteins L2, L3, L14, L23, L24, and L32, as well as the 30S ribosomal proteins S12 and S18 were native premolten globules in their free forms (Venyaminov et al. 1981), but adopted rigid well-folded conformations during the formation of a functional ribosome (Yusupov et al. 2001).”
Inference of direct residue contacts in two-component signaling. (2010, background): “One of the great success stories in X-ray crystallography was the resolution of the entire ribosome (Ramakrishnan, 2008; Yusupov et al., 2001).”