The complete atomic structure of the large ribosomal subunit at 2.4 A resolution.

By N. Ban, P. Nissen, Jeffrey Hansen, P. Moore, T. Steitz. Science, 2000

3,304 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/47845e9478b48fa61dbd73544596b9399f1d9078

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Citations in the corpus

Versatility of Aminoglycosides and Prospects for Their Future (2003, neutral): “and hygromycin B have been solved (12, 27, 45, 117, 257, 306, 315).”
Studies on the structure-function relationship of the bacterial ribosome (2004, methodology): “…2001), two independently constructed ~3 Å resolution models of the T. thermophilus 30S subunit (Wimberly et al. 2000, Schluenzen et al. 2000), a 2.4 Å model of the Haloarcula marismortui 50S subunit (Ban et al. 2000) and a 3.1 Å model of the Deinococcus radiodurans 50S subunit (Harms et al. 2001).”
Molecular Simulations of Cotranslational Protein Folding: Fragment Stabilities, Folding Cooperativity, and Trapping in the Ribosome (2006, positive): “sufficiently wide to allow complete folding to occur, but it does allow significant partial structure formation (Q ; 0.5), and since there is a constriction at the tunnel’s exit [ 53 ], the partially folded protein is prevented from diffusing out into solution to continue folding (e.g., see Figure 8”
Intrinsic protein disorder in complete genomes. (2000, background): “An especially interested feature of the ribosomal proteins is that they typically have small globular regions and long, extended tails that idiosyncratically meander among the RNA strands, probably acting as a glue for the various subregions of the RNA [4].”
Understanding the adaptation of Halobacterium species NRC-1 to its extreme environment through computational analysis of its genome sequence. (2001, neutral): “Recent success in solving the structure of the large ribosomal subunit from a related halophile, Haloarcula marismortui (Ban et al. 2000), genomic and genetic dissection of the archaeal regulon for purple membrane synthesis in Halobacterium NRC-1 (Baliga et al. 2001), and reverse genetic analysis…”
Macromolecular crystal twinning, lattice disorders and multiple crystals (2008, methodology): “2mm using a reverse extraction procedure for crystal growth that also increased crystal strength and singularity (73).”
More than the sum of their parts: On the evolution of proteins from peptides (2003, neutral): “(67) ‘At present, there are no serious alternatives to an RNA world being one essential intermediate stage in the origin of life’.”
Molecular dynamics applied to X-ray structure refinement. (2002, neutral): “( 8 ) FIGURE 1. Schematic explanation of molecular dynamics based simulated annealing.”
Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin. (2001, background): “These proteins all, however, do adopt complex structures as they assemble into complete ribosomes ( 16 ).”
Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics (2019, background): “IDPs/IDPRs can act as molecular glue or mortar [29] by filling the gaps and cracks between the structural elements of a binding partner [136].”