Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations.
about
Merging molecular mechanism and evolution: theory and computation at the interface of biophysics and evolutionary population geneticsThe interface of protein structure, protein biophysics, and molecular evolutionSystematic detection of internal symmetry in proteins using CE-SymmWeakly stable regions and protein-protein interactions in beta-barrel membrane proteinsProtein biophysics explains why highly abundant proteins evolve slowlyMolecular Determinants of Mutant Phenotypes, Inferred from Saturation Mutagenesis DataEnzyme Efficiency but Not Thermostability Drives Cefotaxime Resistance Evolution in TEM-1 β-Lactamase.A prion-like mechanism for the propagated misfolding of SOD1 from in silico modeling of solvated near-native conformersA comprehensive, high-resolution map of a gene's fitness landscapeProtein flexibility facilitates quaternary structure assembly and evolution.Reconstructed Ancestral Enzymes Impose a Fitness Cost upon Modern Bacteria Despite Exhibiting Favourable Biochemical Properties.Evolutionary capacitance and control of protein stability in protein-protein interaction networks.Evolutionary, physicochemical, and functional mechanisms of protein homooligomerization.A simulated intermediate state for folding and aggregation provides insights into ΔN6 β2-microglobulin amyloidogenic behavior.Thermal stabilization of dihydrofolate reductase using monte carlo unfolding simulations and its functional consequences.The βγ-crystallins: native state stability and pathways to aggregation.Protein Homeostasis Imposes a Barrier on Functional Integration of Horizontally Transferred Genes in BacteriaDelayed commitment to evolutionary fate in antibiotic resistance fitness landscapes.Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness.Biophysical principles predict fitness landscapes of drug resistance.Cellular strategies for regulating functional and nonfunctional protein aggregation.Evolutionary diversification of the multimeric states of proteins.Population size dependence of fitness effect distribution and substitution rate probed by biophysical model of protein thermostability.Transient protein-protein interactions perturb E. coli metabolome and cause gene dosage toxicity.Evolutionary selection for protein aggregation.Modulating protein stability - directed evolution strategies for improved protein function.Quantifying and understanding the fitness effects of protein mutations: Laboratory versus natureBridging the physical scales in evolutionary biology: from protein sequence space to fitness of organisms and populations.Mutation effects predicted from sequence co-variation.SpyTag/SpyCatcher cyclization confers resilience to boiling on a mesophilic enzymeAntigenic diversification is correlated with increased thermostability in a mammalian virus.Systems-level response to point mutations in a core metabolic enzyme modulates genotype-phenotype relationship.Lean forward: Genetic analysis of temperature-sensitive mutants unfolds the secrets of oligomeric protein complex assembly.A Simple Model of Protein Domain Swapping in Crowded Cellular Environments.Highly expressed genes evolve under strong epistasis from a proteome-wide scan in E. coli.Adaptive Mutations in RNA Polymerase and the Transcriptional Terminator Rho Have Similar Effects on Escherichia coli Gene Expression.Thermosensitivity of growth is determined by chaperone-mediated proteome reallocation.Fitness costs of minimal sequence alterations causing protein instability and toxicity.An in silico study of the effect of SOD1 electrostatic loop dynamics on amyloid‑like filament formation.Optimization of lag phase shapes the evolution of a bacterial enzyme.
P2860
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P2860
Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations.
@ast
Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations.
@en
type
label
Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations.
@ast
Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations.
@en
prefLabel
Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations.
@ast
Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations.
@en
P2860
P356
P1476
Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations.
@en
P2093
Shimon Bershtein
Wanmeng Mu
P2860
P304
P356
10.1073/PNAS.1118157109
P407
P577
2012-03-12T00:00:00Z