Novel methods for directed evolution of enzymes: quality, not quantity.
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Tuning the dials of Synthetic BiologyExploiting models of molecular evolution to efficiently direct protein engineeringDiscovery of active proteins directly from combinatorial randomized protein libraries without display, purification or sequencing: identification of novel zinc finger proteinsFluorescent proteins as tools to aid protein productionTriplet nucleotide removal at random positions in a target gene: the tolerance of TEM-1 beta-lactamase to an amino acid deletion.Expanding the Nucleotide and Sugar 1-Phosphate Promiscuity of Nucleotidyltransferase RmlA via Directed EvolutionThe crystal structure of an esterase from the hyperthermophilic microorganism Pyrobaculum calidifontis VA1 explains its enantioselectivityA Single Mutation in a Regulatory Protein Produces Evolvable Allosterically Regulated Catalyst of Nonnatural ReactionE Pluribus Unum: 50 Years of Research, Millions of Viruses, and One Goal--Tailored Acceleration of AAV EvolutionThe case for an early biological origin of DNADNA polymerases engineered by directed evolution to incorporate non-standard nucleotidesRational redesign of glucose oxidase for improved catalytic function and stabilityInvestigating protein structural plasticity by surveying the consequence of an amino acid deletion from TEM-1 beta-lactamase.Directed evolution strategies for enantiocomplementary haloalkane dehalogenases: from chemical waste to enantiopure building blocks.Multiplex-PCR-based recombination as a novel high-fidelity method for directed evolution.Laboratory-directed protein evolutionEngineering and rapid selection of a low-affinity glucose/galactose-binding protein for a glucose biosensorSteering directed protein evolution: strategies to manage combinatorial complexity of mutant libraries.Revealing biases inherent in recombination protocols.A semi-rational design strategy of directed evolution combined with chemical synthesis of DNA sequences.Expanded molecular diversity generation during directed evolution by trinucleotide exchange (TriNEx).Shedding light on the efficacy of laboratory evolution based on iterative saturation mutagenesis.Golden gate shuffling: a one-pot DNA shuffling method based on type IIs restriction enzymes.Engineering Kinases to Phosphorylate Nucleoside Analogs for Antiviral and Cancer Therapy.Replacing Mn(2+) with Co(2+) in human arginase i enhances cytotoxicity toward l-arginine auxotrophic cancer cell lines.Revisiting the lipase from Pseudomonas aeruginosa: directed evolution of substrate acceptance and enantioselectivity using iterative saturation mutagenesis.Manipulating the expression rate and enantioselectivity of an epoxide hydrolase by using directed evolution.Enzyme-coupled assay for beta-xylosidase hydrolysis of natural substratesEnhancing the thermal robustness of an enzyme by directed evolution: least favorable starting points and inferior mutants can map superior evolutionary pathways.Engineering of biocatalysts - from evolution to creation.Enhancing the efficiency of directed evolution in focused enzyme libraries by the adaptive substituent reordering algorithm.Many pathways in laboratory evolution can lead to improved enzymes: how to escape from local minima.Foundations for the design and implementation of synthetic genetic circuits.Biased clique shuffling reveals stabilizing mutations in cellulase Cel7A.Thermostable DNA ligase-mediated PCR production of circular plasmid (PPCP) and its application in directed evolution via in situ error-prone PCR.Directed evolution by using iterative saturation mutagenesis based on multiresidue sites.A high-throughput adrenaline test for the exploration of the catalytic potential of halohydrin dehalogenases in epoxide ring-opening reactions.A Practical System for High-Throughput Screening of Mutants of Bacillus fastidiosus Uricase.Development and Use of a Novel Random Mutagenesis Method: In Situ Error-Prone PCR (is-epPCR).The outlook for protein engineering in crop improvement.
P2860
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P2860
Novel methods for directed evolution of enzymes: quality, not quantity.
description
2004 nî lūn-bûn
@nan
2004 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Novel methods for directed evolution of enzymes: quality, not quantity.
@ast
Novel methods for directed evolution of enzymes: quality, not quantity.
@en
type
label
Novel methods for directed evolution of enzymes: quality, not quantity.
@ast
Novel methods for directed evolution of enzymes: quality, not quantity.
@en
prefLabel
Novel methods for directed evolution of enzymes: quality, not quantity.
@ast
Novel methods for directed evolution of enzymes: quality, not quantity.
@en
P1476
Novel methods for directed evolution of enzymes: quality, not quantity.
@en
P2093
Stefan Lutz
P304
P356
10.1016/J.COPBIO.2004.05.004
P577
2004-08-01T00:00:00Z