Ribosomal protein structures: insights into the architecture, machinery and evolution of the ribosome
V Ramakrishnan, SW White - Trends in Biochemical Sciences, 1998 - cell.com
Abstract Models of the bacterial ribosome based on recent structural analyses are beginning
to provide new insights into the protein synthetic machinery. Central to evolving models are …
to provide new insights into the protein synthetic machinery. Central to evolving models are …
The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
The large ribosomal subunit catalyzes peptide bond formation and binds initiation,
termination, and elongation factors. We have determined the crystal structure of the large …
termination, and elongation factors. We have determined the crystal structure of the large …
Overview of protein structural and functional folds
PD Sun, CE Foster, JC Boyington - Current protocols in protein …, 2004 - Wiley Online Library
This overview provides an illustrated, comprehensive survey of some commonly observed
protein‐fold families and structural motifs, chosen for their functional significance. It opens …
protein‐fold families and structural motifs, chosen for their functional significance. It opens …
Influence of Heavy Metals (Ni, Cu, and Zn) on Nitro-Oxidative Stress Responses, Proteome Regulation and Allergen Production in Basil (Ocimum basilicum L.) Plants
EC Georgiadou, E Kowalska, K Patla… - Frontiers in Plant …, 2018 - frontiersin.org
One of the most significant biosphere contamination problems worldwide is derived from
heavy metals. Heavy metals can be highly reactive and toxic according to their oxidation …
heavy metals. Heavy metals can be highly reactive and toxic according to their oxidation …
[HTML][HTML] High resolution structure of the large ribosomal subunit from a mesophilic eubacterium
We describe the high resolution structure of the large ribosomal subunit from Deinococcus
radiodurans (D50S), a gram-positive mesophile suitable for binding of antibiotics and …
radiodurans (D50S), a gram-positive mesophile suitable for binding of antibiotics and …
The roles of ribosomal proteins in the structure assembly, and evolution of the large ribosomal subunit
The structures of ribosomal proteins and their interactions with RNA have been examined in
the refined crystal structure of the Haloarcula marismortui large ribosomal subunit. The …
the refined crystal structure of the Haloarcula marismortui large ribosomal subunit. The …
Placement of protein and RNA structures into a 5 Å-resolution map of the 50S ribosomal subunit
We have calculated at 5.0 Å resolution an electron-density map of the large 50S ribosomal
subunit from the bacterium Haloarcula marismortui by using phases derived from four heavy …
subunit from the bacterium Haloarcula marismortui by using phases derived from four heavy …
The p43 component of the mammalian multi-synthetase complex is likely to be the precursor of the endothelial monocyte-activating polypeptide II cytokine
S Quevillon, F Agou, JC Robinson… - Journal of Biological …, 1997 - ASBMB
p43 is one of the three auxiliary components invariably associated with nine aminoacyl-
tRNA synthetases as a multienzyme complex ubiquitous to all eukaryotic cells from flies to …
tRNA synthetases as a multienzyme complex ubiquitous to all eukaryotic cells from flies to …
Computationally-guided design and selection of high performing ribosomal active site mutants
Understanding how modifications to the ribosome affect function has implications for
studying ribosome biogenesis, building minimal cells, and repurposing ribosomes for …
studying ribosome biogenesis, building minimal cells, and repurposing ribosomes for …
RNA binding strategies of ribosomal proteins
DE Draper, LP Reynaldo - Nucleic acids research, 1999 - academic.oup.com
Structures of a number of ribosomal proteins have now been determined by crystallography
and NMR, though the complete structure of a ribosomal protein-rRNA complex has yet to be …
and NMR, though the complete structure of a ribosomal protein-rRNA complex has yet to be …