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Revolutionising the design and analysis of protein engineering experiments using fractional factorial design

https://doi.org/10.1101/298273
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/0471142727.mb0803s51openalex-snapshot
Random Mutagenesis by PCR
inferredcites →https://doi.org/10.1016/j.bpj.2015.07.026openalex-snapshot
Rapid Bioinformatic Identification of Thermostabilizing Mutations
inferredcites →https://doi.org/10.1016/j.bpj.2015.08.020openalex-snapshot
Identifying Thermostabilizing Mutations in Membrane Proteins by Bioinformatics
inferredcites →https://doi.org/10.1016/j.jsb.2008.12.007openalex-snapshot
AcrB et al.: Obstinate contaminants in a picogram scale. One more bottleneck in the membrane protein structure pipeline
inferredcites →https://doi.org/10.1016/j.jsb.2011.09.005openalex-snapshot
AcrB contamination in 2-D crystallization of membrane proteins: Lessons from a sodium channel and a putative monovalent cation/proton antiporter
inferredcites →https://doi.org/10.1016/j.pep.2013.10.016openalex-snapshot
Statistical approaches to maximize recombinant protein expression in Escherichia coli: A general review
inferredcites →https://doi.org/10.1016/s0021-9258(19)86452-9openalex-snapshot
Protein crystallization using incomplete factorial experiments.
inferredcites →https://doi.org/10.1021/acs.jpcb.6b01405openalex-snapshot
Identification of Thermostabilizing Mutations for Membrane Proteins: Rapid Method Based on Statistical Thermodynamics
inferredcites →https://doi.org/10.1021/ct500616vopenalex-snapshot
Rapid Computational Prediction of Thermostabilizing Mutations for G Protein-Coupled Receptors
inferredcites →https://doi.org/10.1038/nature17983openalex-snapshot
No observable conformational changes in PSII
inferredcites →https://doi.org/10.1038/nature17995openalex-snapshot
Local fitness landscape of the green fluorescent protein
inferredcites →https://doi.org/10.1038/nmeth.2019openalex-snapshot
Fiji: an open-source platform for biological-image analysis
inferredcites →https://doi.org/10.1038/nprot.2007.448openalex-snapshot
Selection of human antibody fragments by phage display
inferredcites →https://doi.org/10.1038/nprot.2016.088openalex-snapshot
A mutagenesis and screening strategy to generate optimally thermostabilized membrane proteins for structural studies
inferredcites →https://doi.org/10.1038/srep21294openalex-snapshot
A generic selection system for improved expression and thermostability of G protein-coupled receptors by directed evolution
inferredcites →https://doi.org/10.1073/pnas.0804396105openalex-snapshot
Co-evolving stability and conformational homogeneity of the human adenosine A 2a receptor
inferredcites →https://doi.org/10.1073/pnas.1114944109openalex-snapshot
Transport of drugs by the multidrug transporter AcrB involves an access and a deep binding pocket that are separated by a switch-loop
inferredcites →https://doi.org/10.1073/pnas.80.8.2189openalex-snapshot
Mutator strains of Escherichia coli, mutD and dnaQ, with defective exonucleolytic editing by DNA polymerase III holoenzyme.
inferredcites →https://doi.org/10.1093/nar/17.16.6545openalex-snapshot
A simple method for site-directed mutagenesis using the polymerase chain reaction
inferredcites →https://doi.org/10.1107/s0021889891004430openalex-snapshot
Sparse matrix sampling: a screening method for crystallization of proteins
inferredcites →https://doi.org/10.1107/s1744309108028248openalex-snapshot
There is a baby in the bath water: AcrB contamination is a major problem in membrane-protein crystallization
inferredcites →https://doi.org/10.1111/j.1472-765x.2004.01595.xopenalex-snapshot
Response surface methodology for optimizing the fermentation medium of Clostridium butyricum
inferredcites →https://doi.org/10.1126/science.2471267openalex-snapshot
High-Resolution Epitope Mapping of hGH-Receptor Interactions by Alanine-Scanning Mutagenesis
inferredcites →https://doi.org/10.1128/aac.00715-09openalex-snapshot
Klebsiella pneumoniae AcrAB Efflux Pump Contributes to Antimicrobial Resistance and Virulence
inferredcites →https://doi.org/10.1128/aac.48.4.1145-1150.2004openalex-snapshot
Expression ofacrB,acrF,acrD,marA, andsoxSinSalmonella entericaSerovar Typhimurium: Role in Multiple Antibiotic Resistance
inferredcites →https://doi.org/10.1371/journal.pone.0114864openalex-snapshot
Stubborn Contaminants: Influence of Detergents on the Purity of the Multidrug ABC Transporter BmrA
inferredcites →https://doi.org/10.3389/fphar.2015.00058openalex-snapshot
New perspectives in signaling mediated by receptors coupled to stimulatory G protein: the emerging significance of cAMP efflux and extracellular cAMP-adenosine pathway
inferredcites →https://doi.org/10.3389/fphar.2015.00082openalex-snapshot
Stabilization of G protein-coupled receptors by point mutations

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1007/978-3-030-69514-9_40openalex-snapshot
Optimization of the Deposition Condition for Improving the Ti Film Resistance of DRAM Products
inferred← citeshttps://doi.org/10.1038/s41598-020-71744-xopenalex-snapshot
IMPROvER: the Integral Membrane Protein Stability Selector
inferred← citeshttps://doi.org/10.1109/tcpmt.2021.3082419openalex-snapshot
Reducing Thickness Deviation of W-Shaped Structures in Manufacturing DRAM Products Using RSM and ANN_GA
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