scholarly article | Q13442814 |
P2093 | author name string | Saurav Mallik | |
Hiroshi Akashi | |||
Sudip Kundu | |||
P2860 | cites work | Ribosomal Mutation Database | Q24174718 |
The crystal structure of ribosomal protein S4 reveals a two-domain molecule with an extensive RNA-binding surface: one domain shows structural homology to the ETS DNA-binding motif | Q24533285 | ||
Phylogenetic structure of the prokaryotic domain: The primary kingdoms | Q24564821 | ||
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Ribosome biogenesis and the translation process in Escherichia coli | Q28246227 | ||
Protein complexes are under evolutionary selection to assemble via ordered pathways | Q28288859 | ||
Assortative mixing in Protein Contact Networks and protein folding kinetics | Q28303457 | ||
Prediction of protein-RNA residue-base contacts using two-dimensional conditional random field with the lasso | Q28661071 | ||
Molecular signatures of ribosomal evolution | Q28757251 | ||
Separation of phylogenetic and functional associations in biological sequences by using the parametric bootstrap | Q29544639 | ||
Regulation of actin filament assembly by Arp2/3 complex and formins | Q29615161 | ||
Correction for phylogeny, small number of observations and data redundancy improves the identification of coevolving amino acid pairs using mutual information. | Q30375462 | ||
Sequence coevolution between RNA and protein characterized by mutual information between residue triplets | Q30412218 | ||
Deleterious mutations in small subunit ribosomal RNA identify functional sites and potential targets for antibiotics | Q30476365 | ||
An assembly landscape for the 30S ribosomal subunit | Q33228236 | ||
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Kinetic cooperativity in Escherichia coli 30S ribosomal subunit reconstitution reveals additional complexity in the assembly landscape | Q33777643 | ||
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Molecular basis of co-operativity in protein folding. | Q52435156 | ||
Crystal structure of the 30 s ribosomal subunit from Thermus thermophilus: structure of the proteins and their interactions with 16 s RNA | Q56396627 | ||
Structural preordering in the N-terminal region of ribosomal protein S4 revealed by heteronuclear NMR spectroscopy | Q73153247 | ||
Modeling a minimal ribosome based on comparative sequence analysis | Q74529126 | ||
RNA tertiary structure and cooperative assembly of a large ribonucleoprotein complex | Q80950943 | ||
Coevolution of protein and RNA structures within a highly conserved ribosomal domain | Q81447903 | ||
Assembly mapping of 30 S ribosomal proteins from Escherichia coli. Further studies. | Q34214234 | ||
Effects of polyvalent cations on the folding of an rRNA three-way junction and binding of ribosomal protein S15 | Q34361485 | ||
A novel method for detecting intramolecular coevolution: adding a further dimension to selective constraints analyses. | Q34611485 | ||
Expanded versions of the 16S and 23S ribosomal RNA mutation databases (16SMDBexp and 23SMDBexp) | Q34648173 | ||
Distinguishing specific and nonspecific interdomain interactions in multidomain proteins | Q34692183 | ||
Allostery and cooperativity revisited | Q34786984 | ||
Assembly reflects evolution of protein complexes | Q34787237 | ||
Independent in vitro assembly of a ribonucleoprotein particle containing the 3' domain of 16S rRNA. | Q35670384 | ||
Structure and function of E. coli ribosomes. V. Reconstitution of functionally active 30S ribosomal particles from RNA and proteins | Q36468269 | ||
Stochastic dynamics of macromolecular-assembly networks. | Q36494123 | ||
Detecting overlapping protein complexes in protein-protein interaction networks | Q36528169 | ||
Coevolution at protein complex interfaces can be detected by the complementarity trace with important impact for predictive docking | Q36693877 | ||
Concurrent nucleation of 16S folding and induced fit in 30S ribosome assembly | Q37289162 | ||
Protein-guided RNA dynamics during early ribosome assembly. | Q37669372 | ||
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Emerging methods in protein co-evolution | Q38086348 | ||
Slow formation of stable complexes during coincubation of minimal rRNA and ribosomal protein S4 | Q38322055 | ||
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Ribosome dynamics and tRNA movement by time-resolved electron cryomicroscopy | Q41618424 | ||
Global stabilization of rRNA structure by ribosomal proteins S4, S17, and S20. | Q41878089 | ||
Finding coevolving amino acid residues using row and column weighting of mutual information and multi-dimensional amino acid representation | Q41953697 | ||
The archaeal origins of the eukaryotic translational system | Q43123450 | ||
The 16S rRNA binding site of Thermus thermophilus ribosomal protein S15: comparison with Escherichia coli S15, minimum site and structure | Q43205974 | ||
Influence of conservation on calculations of amino acid covariance in multiple sequence alignments | Q46449574 | ||
Cooperativity in macromolecular assembly | Q46725345 | ||
An evolutionarily conserved network of amino acids mediates gating in voltage-dependent potassium channels | Q47333767 | ||
Ribosomal protein structures: insights into the architecture, machinery and evolution of the ribosome | Q47757349 | ||
Mutual information without the influence of phylogeny or entropy dramatically improves residue contact prediction | Q48372137 | ||
Using information theory to search for co-evolving residues in proteins | Q48475034 | ||
Using multiple interdependency to separate functional from phylogenetic correlations in protein alignments | Q48598890 | ||
P275 | copyright license | Creative Commons Attribution-NonCommercial 4.0 International | Q34179348 |
P6216 | copyright status | copyrighted | Q50423863 |
P433 | issue | 11 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | co-evolution | Q208841 |
P304 | page(s) | 5352-5363 | |
P577 | publication date | 2015-05-08 | |
P1433 | published in | Nucleic Acids Research | Q135122 |
P1476 | title | Assembly constraints drive co-evolution among ribosomal constituents | |
P478 | volume | 43 |
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Q92730841 | Exploring allosteric communication in multiple states of the bacterial ribosome using residue network analysis |
Q33553759 | Modular Organization of Residue-Level Contacts Shapes the Selection Pressure on Individual Amino Acid Sites of Ribosomal Proteins |
Q51645839 | Predicting protein folding rate change upon point mutation using residue-level coevolutionary information. |
Q26766142 | Sequence co-evolutionary information is a natural partner to minimally-frustrated models of biomolecular dynamics |
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