Genetic analysis of staphylococcal nuclease: identification of three intragenic "global" suppressors of nuclease-minus mutations.
about
In the light of directed evolution: pathways of adaptive protein evolutionThermodynamic prediction of protein neutralitySearching sequence space by definably random mutagenesis: improving the catalytic potency of an enzymeMechanisms for the Evolution of a Derived Function in the Ancestral Glucocorticoid ReceptorEnhanced protein thermostability from site-directed mutations that decrease the entropy of unfoldingThermodynamics of neutral protein evolutionPrevalence of epistasis in the evolution of influenza A surface proteinsA computational-experimental approach identifies mutations that enhance surface expression of an oseltamivir-resistant influenza neuraminidase.Software for the analysis and visualization of deep mutational scanning data.Probing the contribution of internal cavities to the volume change of protein unfolding under pressureInferring stabilizing mutations from protein phylogenies: application to influenza hemagglutinin.Dramatic thermostabilization of yeast iso-1-cytochrome c by an asparagine----isoleucine replacement at position 57.Electrostatic interactions between transmembrane segments mediate folding of Shaker K+ channel subunitsGenetic analysis of bacteriophage P22 lysozyme structure.Intragenic suppressors of folding defects in the P22 tailspike protein.Genetic analysis of the gyrase A-like domain of DNA topoisomerase II of Saccharomyces cerevisiaeIntragenic dominant suppressors of glp-1, a gene essential for cell-signaling in Caenorhabditis elegans, support a role for cdc10/SWI6/ankyrin motifs in GLP-1 function.Pressure-jump small-angle x-ray scattering detected kinetics of staphylococcal nuclease foldingPredicting the tolerance of proteins to random amino acid substitution.Evolutionary biochemistry: revealing the historical and physical causes of protein properties.Multiple global suppressors of protein stability defects facilitate the evolution of extended-spectrum TEM β-lactamases.Mutational studies on resurrected ancestral proteins reveal conservation of site-specific amino acid preferences throughout evolutionary history.Identification of destabilizing and stabilizing mutations of Ste2p, a G protein-coupled receptor in Saccharomyces cerevisiae.Essential role of a sodium dodecyl sulfate-resistant protein IV multimer in assembly-export of filamentous phageChemical chaperone rescue of mutant human cystathionine beta-synthaseIsocitrate dehydrogenase kinase/phosphatase: identification of mutations which selectively inhibit phosphatase activity.Characterization of the global stabilizing substitution A77V and its role in the evolution of CTX-M β-lactamases.A phoA structural gene mutation that conditionally affects formation of the enzyme bacterial alkaline phosphatase.Cyclic AMP-induced conformational change of cyclic AMP receptor protein (CRP): intragenic suppressors of cyclic AMP-independent CRP mutationsAlteration of T4 lysozyme structure by second-site reversion of deleterious mutations.Refolding rate of stability-enhanced cytochrome c is independent of thermodynamic driving force.The kinetic basis for the stabilization of staphylococcal nuclease by xylose.A natural polymorphism in beta-lactamase is a global suppressor.A global suppressor motif for p53 cancer mutants.Protein engineering. The design, synthesis and characterization of factitious proteins.Further stabilization of 3-isopropylmalate dehydrogenase of an extreme thermophile, Thermus thermophilus, by a suppressor mutation method.Genetic analysis of bacteriophage T4 lysozyme structure and function.Misincorporation by AMV reverse transcriptase shows strong dependence on the combination of template and substrate nucleotidesSuppression of mutations in the core of the Tetrahymena ribozyme by spermidine, ethanol and by substrate stabilizationGenetic selection of intragenic suppressor mutations that reverse the effect of common p53 cancer mutations.
P2860
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P2860
Genetic analysis of staphylococcal nuclease: identification of three intragenic "global" suppressors of nuclease-minus mutations.
description
1985 nî lūn-bûn
@nan
1985 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1985 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1985年の論文
@ja
1985年論文
@yue
1985年論文
@zh-hant
1985年論文
@zh-hk
1985年論文
@zh-mo
1985年論文
@zh-tw
1985年论文
@wuu
name
Genetic analysis of staphyloco ...... s of nuclease-minus mutations.
@ast
Genetic analysis of staphyloco ...... s of nuclease-minus mutations.
@en
type
label
Genetic analysis of staphyloco ...... s of nuclease-minus mutations.
@ast
Genetic analysis of staphyloco ...... s of nuclease-minus mutations.
@en
prefLabel
Genetic analysis of staphyloco ...... s of nuclease-minus mutations.
@ast
Genetic analysis of staphyloco ...... s of nuclease-minus mutations.
@en
P2860
P1433
P1476
Genetic analysis of staphyloco ...... s of nuclease-minus mutations.
@en
P2860
P304
P407
P577
1985-08-01T00:00:00Z