Assembly constraints drive co-evolution among ribosomal constituents

scientific article published on 8 May 2015

Assembly constraints drive co-evolution among ribosomal constituents is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1093/NAR/GKV448
P932PMC publication ID4477670
P698PubMed publication ID25956649
P5875ResearchGate publication ID275970231

P2093author name stringSaurav Mallik
Hiroshi Akashi
Sudip Kundu
P2860cites workRibosomal Mutation DatabaseQ24174718
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Molecular signatures of ribosomal evolutionQ28757251
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Detecting coevolution in and among protein domainsQ33305006
Kinetic cooperativity in Escherichia coli 30S ribosomal subunit reconstitution reveals additional complexity in the assembly landscapeQ33777643
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Exploring the paths of (virus) assemblyQ34099024
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The roles of stability and contact order in determining protein folding rates.Q52069638
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 RNAQ56396627
Structural preordering in the N-terminal region of ribosomal protein S4 revealed by heteronuclear NMR spectroscopyQ73153247
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Expanded versions of the 16S and 23S ribosomal RNA mutation databases (16SMDBexp and 23SMDBexp)Q34648173
Distinguishing specific and nonspecific interdomain interactions in multidomain proteinsQ34692183
Allostery and cooperativity revisitedQ34786984
Assembly reflects evolution of protein complexesQ34787237
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 proteinsQ36468269
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Detecting overlapping protein complexes in protein-protein interaction networksQ36528169
Coevolution at protein complex interfaces can be detected by the complementarity trace with important impact for predictive dockingQ36693877
Concurrent nucleation of 16S folding and induced fit in 30S ribosome assemblyQ37289162
Protein-guided RNA dynamics during early ribosome assembly.Q37669372
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Global stabilization of rRNA structure by ribosomal proteins S4, S17, and S20.Q41878089
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An evolutionarily conserved network of amino acids mediates gating in voltage-dependent potassium channelsQ47333767
Ribosomal protein structures: insights into the architecture, machinery and evolution of the ribosomeQ47757349
Mutual information without the influence of phylogeny or entropy dramatically improves residue contact predictionQ48372137
Using information theory to search for co-evolving residues in proteinsQ48475034
Using multiple interdependency to separate functional from phylogenetic correlations in protein alignmentsQ48598890
P275copyright licenseCreative Commons Attribution-NonCommercial 4.0 InternationalQ34179348
P6216copyright statuscopyrightedQ50423863
P433issue11
P407language of work or nameEnglishQ1860
P921main subjectco-evolutionQ208841
P304page(s)5352-5363
P577publication date2015-05-08
P1433published inNucleic Acids ResearchQ135122
P1476titleAssembly constraints drive co-evolution among ribosomal constituents
P478volume43

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cites work (P2860)
Q50884788Co-evolutionary constraints of globular proteins correlate with their folding rates
Q38876977Coevolutionary constraints in the sequence-space of macromolecular complexes reflect their self-assembly pathways
Q35761232Deciphering Cis-Regulatory Element Mediated Combinatorial Regulation in Rice under Blast Infected Condition
Q92730841Exploring allosteric communication in multiple states of the bacterial ribosome using residue network analysis
Q33553759Modular Organization of Residue-Level Contacts Shapes the Selection Pressure on Individual Amino Acid Sites of Ribosomal Proteins
Q51645839Predicting protein folding rate change upon point mutation using residue-level coevolutionary information.
Q26766142Sequence co-evolutionary information is a natural partner to minimally-frustrated models of biomolecular dynamics

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