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A review of enzyme design in catalytic stability by artificial intelligence
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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/aic.16847openalex-snapshot
From directed evolution to computational enzyme engineering—A review
inferredcites →https://doi.org/10.1002/biot.201500153openalex-snapshot
Incorporating unnatural amino acids to engineer biocatalysts for industrial bioprocess applications
inferredcites →https://doi.org/10.1002/cbic.201700613openalex-snapshot
2D Enzyme Cascade Network with Efficient Substrate Channeling by Swinging Arms
inferredcites →https://doi.org/10.1002/humu.22204openalex-snapshot
VariBench: A Benchmark Database for Variations
inferredcites →https://doi.org/10.1002/jcc.21334openalex-snapshot
AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
inferredcites →https://doi.org/10.1002/pro.3585openalex-snapshot
ProtaBank: A repository for protein design and engineering data
inferredcites →https://doi.org/10.1002/pro.3757openalex-snapshot
A computational method for design of connected catalytic networks in proteins
inferredcites →https://doi.org/10.1002/pro.3901openalex-snapshot
A mechanistic view of enzyme evolution
inferredcites →https://doi.org/10.1002/pro.4467openalex-snapshot
BayeStab : Predicting effects of mutations on protein stability with uncertainty quantification
inferredcites →https://doi.org/10.1002/pro.5560041020openalex-snapshot
Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
inferredcites →https://doi.org/10.1002/prot.20810openalex-snapshot
Prediction of protein stability changes for single‐site mutations using support vector machines
inferredcites →https://doi.org/10.1002/prot.25599openalex-snapshot
TKSA‐MC: A web server for rational mutation through the optimization of protein charge interactions
inferredcites →https://doi.org/10.1006/jmbi.1996.0531openalex-snapshot
The Crystal Structure of Indole-3-glycerol Phosphate Synthase from the Hyperthermophilic ArchaeonSulfolobus solfataricusin Three Different Crystal Forms: Effects of Ionic Strength
inferredcites →https://doi.org/10.1006/jtbi.2001.2497openalex-snapshot
Design Issues for the Michaelis–Menten Model
inferredcites →https://doi.org/10.1007/978-3-031-01587-8openalex-snapshot
Introduction to Graph Neural Networks
inferredcites →https://doi.org/10.1007/s00894-007-0197-4openalex-snapshot
Sequence analysis and rule development of predicting protein stability change upon mutation using decision tree model
inferredcites →https://doi.org/10.1007/s10462-011-9272-4openalex-snapshot
Decision trees: a recent overview
inferredcites →https://doi.org/10.1007/s11274-019-2642-9openalex-snapshot
Unnatural amino acids: production and biotechnological potential
inferredcites →https://doi.org/10.1016/b978-0-12-095461-2.00006-0openalex-snapshot
Enzymes and Enzyme Regulation
inferredcites →https://doi.org/10.1016/b978-0-12-815739-8.00007-9openalex-snapshot
Support vector regression
inferredcites →https://doi.org/10.1016/b978-044453079-0/50013-4openalex-snapshot
THERMODYNAMICS AND BIOLOGICAL SYSTEMS
inferredcites →https://doi.org/10.1016/j.abb.2007.08.004openalex-snapshot
Electrostatic interactions in the denatured state ensemble: Their effect upon protein folding and protein stability
inferredcites →https://doi.org/10.1016/j.bpj.2017.11.012openalex-snapshot
Effects of pH and Salt Concentration on Stability of a Protein G Variant Using Coarse-Grained Models
inferredcites →https://doi.org/10.1016/j.bpj.2021.03.036openalex-snapshot
Electrostatic interaction optimization improves catalytic rates and thermotolerance on xylanases
inferredcites →https://doi.org/10.1016/j.compbiolchem.2006.06.004openalex-snapshot
Knowledge acquisition and development of accurate rules for predicting protein stability changes
inferredcites →https://doi.org/10.1016/j.foodchem.2020.127670openalex-snapshot
Influence of amino acids on thermal stability and heat-set gelation of bovine serum albumin
inferredcites →https://doi.org/10.1016/j.jmb.2007.12.013openalex-snapshot
Modulating Catalytic Activity by Unnatural Amino Acid Residues in a GSH-Binding Loop of GST P1-1
inferredcites →https://doi.org/10.1016/j.jmb.2016.01.012openalex-snapshot
EASE-MM: Sequence-Based Prediction of Mutation-Induced Stability Changes with Feature-Based Multiple Models
inferredcites →https://doi.org/10.1016/j.sbi.2013.06.009openalex-snapshot
Protein engineering with unnatural amino acids
inferredcites →https://doi.org/10.1016/j.tibtech.2011.04.003openalex-snapshot
Deep mutational scanning: assessing protein function on a massive scale
inferredcites →https://doi.org/10.1016/s0076-6879(00)x0216-9openalex-snapshot
Numerical Computer Methods
inferredcites →https://doi.org/10.1016/s1095-6433(00)00359-7openalex-snapshot
Review: Protein function at thermal extremes: balancing stability and flexibility
inferredcites →https://doi.org/10.1016/s1095-6433(98)10002-8openalex-snapshot
The thermodynamics and evolution of complexity in biological systems
inferredcites →https://doi.org/10.1021/acs.biochem.7b00942openalex-snapshot
Biological Roles of Protein Kinetic Stability
inferredcites →https://doi.org/10.1021/acs.biochem.8b01004openalex-snapshot
A Biophysical Perspective on Enzyme Catalysis
inferredcites →https://doi.org/10.1021/acs.biochem.9b00405openalex-snapshot
Stability and Conformational Resilience of Protein Disulfide Isomerase
inferredcites →https://doi.org/10.1021/acs.jcim.0c00489openalex-snapshot
Improving Enzyme Optimum Temperature Prediction with Resampling Strategies and Ensemble Learning
inferredcites →https://doi.org/10.1021/acs.jcim.8b00839openalex-snapshot
GuacaMol: Benchmarking Models for de Novo Molecular Design
inferredcites →https://doi.org/10.1021/acs.jcim.9b00911openalex-snapshot
Rational Design of Chymotrypsin Inhibitor 2 by Optimizing Non-Native Interactions
inferredcites →https://doi.org/10.1021/acs.jmedchem.6b00319openalex-snapshot
Unusual Amino Acids in Medicinal Chemistry
inferredcites →https://doi.org/10.1021/acs.jpcb.1c01253openalex-snapshot
Improving the Thermostability of Xylanase A from Bacillus subtilis by Combining Bioinformatics and Electrostatic Interactions Optimization
inferredcites →https://doi.org/10.1021/bi00592a028openalex-snapshot
Thermal stability and protein structure
inferredcites →https://doi.org/10.1038/nmeth.3027openalex-snapshot
Deep mutational scanning: a new style of protein science
inferredcites →https://doi.org/10.1038/nmeth0607-466openalex-snapshot
Eris: an automated estimator of protein stability
inferredcites →https://doi.org/10.1038/s41580-020-00294-xopenalex-snapshot
Global view of human protein glycosylation pathways and functions
inferredcites →https://doi.org/10.1038/s41586-021-03828-1openalex-snapshot
Highly accurate protein structure prediction for the human proteome
inferredcites →https://doi.org/10.1038/s41587-022-01618-2openalex-snapshot
Large language models generate functional protein sequences across diverse families
inferredcites →https://doi.org/10.1038/s41592-021-01205-4openalex-snapshot
DOME: recommendations for supervised machine learning validation in biology
inferredcites →https://doi.org/10.1038/s41929-022-00798-zopenalex-snapshot
Deep learning-based kcat prediction enables improved enzyme-constrained model reconstruction
inferredcites →https://doi.org/10.1038/s42256-021-00310-5openalex-snapshot
Expanding functional protein sequence spaces using generative adversarial networks
inferredcites →https://doi.org/10.1038/srep28285openalex-snapshot
Towards a structural biology of the hydrophobic effect in protein folding
inferredcites →https://doi.org/10.1039/b909200popenalex-snapshot
Incorporation of unnatural amino acids for synthetic biology
inferredcites →https://doi.org/10.1039/c7ra06544bopenalex-snapshot
The effects of macromolecular crowding and surface charge on the properties of an immobilized enzyme: activity, thermal stability, catalytic efficiency and reusability
inferredcites →https://doi.org/10.1074/jbc.m113.485953openalex-snapshot
Engineering the Pattern of Protein Glycosylation Modulates the Thermostability of a GH11 Xylanase
inferredcites →https://doi.org/10.1080/07388551.2019.1682963openalex-snapshot
Recent advances in the improvement of enzyme thermostability by structure modification
inferredcites →https://doi.org/10.1093/bib/bbaa337openalex-snapshot
FireProtASR: A Web Server for Fully Automated Ancestral Sequence Reconstruction
inferredcites →https://doi.org/10.1093/bib/bby088openalex-snapshot
Control principles for complex biological networks
inferredcites →https://doi.org/10.1093/bib/bbz071openalex-snapshot
A critical review of five machine learning-based algorithms for predicting protein stability changes upon mutation
inferredcites →https://doi.org/10.1093/bib/bbz168openalex-snapshot
On the critical review of five machine learning-based algorithms for predicting protein stability changes upon mutation
inferredcites →https://doi.org/10.1093/bioinformatics/btac090openalex-snapshot
HIV-1 drug resistance profiling using amino acid sequence space cartography
inferredcites →https://doi.org/10.1093/bioinformatics/bth928openalex-snapshot
A neural-network-based method for predicting protein stability changes upon single point mutations
inferredcites →https://doi.org/10.1093/bioinformatics/btm100openalex-snapshot
iPTREE-STAB: interpretable decision tree based method for predicting protein stability changes upon mutations
inferredcites →https://doi.org/10.1093/bioinformatics/btr576openalex-snapshot
Protein stability: a single recorded mutation aids in predicting the effects of other mutations in the same amino acid site
inferredcites →https://doi.org/10.1093/bioinformatics/btt691openalex-snapshot
mCSM: predicting the effects of mutations in proteins using graph-based signatures
inferredcites →https://doi.org/10.1093/bioinformatics/btv291openalex-snapshot
INPS: predicting the impact of non-synonymous variations on protein stability from sequence
inferredcites →https://doi.org/10.1093/bioinformatics/btw192openalex-snapshot
INPS-MD: a web server to predict stability of protein variants from sequence and structure
inferredcites →https://doi.org/10.1093/bioinformatics/btz184openalex-snapshot
FoldX 5.0: working with RNA, small molecules and a new graphical interface
inferredcites →https://doi.org/10.1093/bioinformatics/btz682openalex-snapshot
BioBERT: a pre-trained biomedical language representation model for biomedical text mining
inferredcites →https://doi.org/10.1093/database/baaa065openalex-snapshot
EnzyMine: a comprehensive database for enzyme function annotation with enzymatic reaction chemical feature
inferredcites →https://doi.org/10.1093/database/bas028openalex-snapshot
MuteinDB: the mutein database linking substrates, products and enzymatic reactions directly with genetic variants of enzymes
inferredcites →https://doi.org/10.1093/molbev/msy244openalex-snapshot
Beyond Stability Constraints: A Biophysical Model of Enzyme Evolution with Selection on Stability and Activity
inferredcites →https://doi.org/10.1093/nar/gkaa981openalex-snapshot
FireProtDB: database of manually curated protein stability data
inferredcites →https://doi.org/10.1093/nar/gkab1061openalex-snapshot
AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models
inferredcites →https://doi.org/10.1093/nar/gkac351openalex-snapshot
iFeatureOmega: an integrative platform for engineering, visualization and analysis of features from molecular sequences, structural and ligand data sets
inferredcites →https://doi.org/10.1093/nar/gki375openalex-snapshot
I-Mutant2.0: predicting stability changes upon mutation from the protein sequence or structure
inferredcites →https://doi.org/10.1093/nar/gkj103openalex-snapshot
ProTherm and ProNIT: thermodynamic databases for proteins and protein-nucleic acid interactions
inferredcites →https://doi.org/10.1093/nar/gkl190openalex-snapshot
CUPSAT: prediction of protein stability upon point mutations
inferredcites →https://doi.org/10.1093/nar/gkm998openalex-snapshot
AAindex: amino acid index database, progress report 2008
inferredcites →https://doi.org/10.1093/nar/gkt1178openalex-snapshot
The carbohydrate-active enzymes database (CAZy) in 2013
inferredcites →https://doi.org/10.1093/nar/gku411openalex-snapshot
DUET: a server for predicting effects of mutations on protein stability using an integrated computational approach
inferredcites →https://doi.org/10.1093/nar/gku946openalex-snapshot
EzCatDB: the enzyme reaction database, 2015 update
inferredcites →https://doi.org/10.1093/nar/gkw1092openalex-snapshot
KEGG: new perspectives on genomes, pathways, diseases and drugs
inferredcites →https://doi.org/10.1093/nar/gkx1012openalex-snapshot
Mechanism and Catalytic Site Atlas (M-CSA): a database of enzyme reaction mechanisms and active sites
inferredcites →https://doi.org/10.1093/nar/gky1004openalex-snapshot
RCSB Protein Data Bank: biological macromolecular structures enabling research and education in fundamental biology, biomedicine, biotechnology and energy
inferredcites →https://doi.org/10.1093/nar/gky1048openalex-snapshot
BRENDA in 2019: a European ELIXIR core data resource
inferredcites →https://doi.org/10.1093/nar/gky1049openalex-snapshot
UniProt: a worldwide hub of protein knowledge
inferredcites →https://doi.org/10.1093/nar/gky1100openalex-snapshot
InterPro in 2019: improving coverage, classification and access to protein sequence annotations
inferredcites →https://doi.org/10.1093/nar/gky381openalex-snapshot
gRINN: a tool for calculation of residue interaction energies and protein energy network analysis of molecular dynamics simulations
inferredcites →https://doi.org/10.1093/nar/gkz740openalex-snapshot
BioSeq-Analysis2.0: an updated platform for analyzing DNA, RNA and protein sequences at sequence level and residue level based on machine learning approaches
inferredcites →https://doi.org/10.1093/protein/gzu027openalex-snapshot
Concommitant adaptation of a GH11 xylanase by directed evolution to create an alkali-tolerant/thermophilic enzyme
inferredcites →https://doi.org/10.1107/s2059798317015303openalex-snapshot
Hydrogen bonds are a primary driving force for de novo protein folding
inferredcites →https://doi.org/10.1111/j.1753-4887.1981.tb06752.xopenalex-snapshot
Proceedings of the National Academy of Sciences of the United States of America
inferredcites →https://doi.org/10.1126/science.364.6439.448-gopenalex-snapshot
Enzyme activity from machine learning
inferredcites →https://doi.org/10.1126/science.abj8754openalex-snapshot
Accurate prediction of protein structures and interactions using a three-track neural network
inferredcites →https://doi.org/10.1126/science.add2187openalex-snapshot
Robust deep learning–based protein sequence design using ProteinMPNN
inferredcites →https://doi.org/10.1126/science.ade2574openalex-snapshot
Evolutionary-scale prediction of atomic-level protein structure with a language model
inferredcites →https://doi.org/10.1186/1471-2091-12-42openalex-snapshot
BKM-react, an integrated biochemical reaction database
inferredcites →https://doi.org/10.1186/1471-2105-11-370openalex-snapshot
Predicting changes in protein thermostability brought about by single- or multi-site mutations
inferredcites →https://doi.org/10.1186/1471-2105-12-151openalex-snapshot
PoPMuSiC 2.1: a web server for the estimation of protein stability changes upon mutation and sequence optimality
inferredcites →https://doi.org/10.1186/1471-2105-13-44openalex-snapshot
Grading amino acid properties increased accuracies of single point mutation on protein stability prediction
inferredcites →https://doi.org/10.1186/1471-2105-14-s2-s5openalex-snapshot
iStable: off-the-shelf predictor integration for predicting protein stability changes
inferredcites →https://doi.org/10.1186/1471-2164-11-s2-s5openalex-snapshot
Sequence feature-based prediction of protein stability changes upon amino acid substitutions
inferredcites →https://doi.org/10.1186/1471-2164-15-s1-s4openalex-snapshot
Towards sequence-based prediction of mutation-induced stability changes in unseen non-homologous proteins
inferredcites →https://doi.org/10.1371/journal.pcbi.1004556openalex-snapshot
FireProt: Energy- and Evolution-Based Computational Design of Thermostable Multiple-Point Mutants
inferredcites →https://doi.org/10.1371/journal.pone.0047247openalex-snapshot
PROTS-RF: A Robust Model for Predicting Mutation-Induced Protein Stability Changes
inferredcites →https://doi.org/10.2174/0929867324666170623092503openalex-snapshot
Supervised Machine Learning Methods Applied to Predict Ligand- Binding Affinity
inferredcites →https://doi.org/10.2174/092986732838211207154549openalex-snapshot
Application of Machine Learning Techniques for Drug Discovery
inferredcites →https://doi.org/10.2174/1389203716666150923105312openalex-snapshot
Amino acid network for prediction of catalytic residues in enzymes: a comparison survey
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Converting Enzymes into Tools of Industrial Importance
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inferredcites →https://doi.org/10.4018/978-1-5225-7368-5openalex-snapshot
Advanced Methodologies and Technologies in Artificial Intelligence, Computer Simulation, and Human-Computer Interaction
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Neural Message Passing for Quantum Chemistry
inferredcites →https://doi.org/10.5281/zenodo.2539113openalex-snapshot
Enzymes from the BRENDA database annotated with organism growth temperatures and predicted Topt
inferredcites →https://doi.org/10.5281/zenodo.3578467openalex-snapshot
Enzymes from the BRENDA and CAZy databases annotated with organism growth temperatures and predicted Topt
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Incoming claims: where this work appears in other papers’ reference lists and arguments.
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inferred← citeshttps://doi.org/10.1002/ejoc.202301236openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/978-981-96-3311-1_9openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s12155-025-10876-2openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.abb.2024.110246openalex-snapshot
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inferred← citeshttps://doi.org/10.1101/2024.01.12.575432openalex-snapshot
TransMEP: Transfer learning on large protein language models to predict mutation effects of proteins from a small known dataset
inferred← citeshttps://doi.org/10.1101/2024.11.13.623507openalex-snapshot
Computational Design of Metallohydrolases
inferred← citeshttps://doi.org/10.1101/2025.03.28.645293openalex-snapshot
Generative Landscapes and Dynamics to Design Multidomain Artificial Transmembrane Transporters
inferred← citeshttps://doi.org/10.1101/2025.05.18.654422openalex-snapshot
Self-distillation and antisymmetric constraints enable accurate prediction of protein stability changes from single mutations
inferred← citeshttps://doi.org/10.1142/s2737416524400052openalex-snapshot
Investigating Enzyme Biochemistry by Deep Learning: A Computational Tool for a New Era
inferred← citeshttps://doi.org/10.1145/3664647.3680883openalex-snapshot
MetaEnzyme: Meta Pan-Enzyme Learning for Task-Adaptive Redesign
inferred← citeshttps://doi.org/10.1146/annurev-biochem-051424-071952openalex-snapshot
Unexpected Applications of AlphaFold in Molecular Sciences
inferred← citeshttps://doi.org/10.1186/s40643-024-00835-8openalex-snapshot
Mining versatile feruloyl esterases: phylogenetic classification, structural features, and deep learning model
inferred← citeshttps://doi.org/10.1360/csb-2026-0626openalex-snapshot
Computational chemistry-driven rational design of enzymes
inferred← citeshttps://doi.org/10.3390/biology14091268openalex-snapshot
The Role of AI-Driven De Novo Protein Design in the Exploration of the Protein Functional Universe
inferred← citeshttps://doi.org/10.3390/foods15020402openalex-snapshot
Current Progress and Future Directions of Enzyme Technology in Food Nutrition: A Comprehensive Review of Processing, Nutrition, and Functional Innovation
inferred← citeshttps://doi.org/10.3390/ijms26115097openalex-snapshot
Substrate Activation Efficiency in Active Sites of Hydrolases Determined by QM/MM Molecular Dynamics and Neural Networks
inferred← citeshttps://doi.org/10.3390/microorganisms12050933openalex-snapshot
Multiple Cofactor Engineering Strategies to Enhance Pyridoxine Production in Escherichia coli
inferred← citeshttps://doi.org/10.3390/molecules31010045openalex-snapshot
AI-Driven Enzyme Engineering: Emerging Models and Next-Generation Biotechnological Applications
inferred← citeshttps://doi.org/10.3390/molecules31132359openalex-snapshot
Bridging Algorithms and Biocatalysis: Perspectives on AI-Supported Enzyme Engineering
inferred← citeshttps://doi.org/10.5802/crchim.389openalex-snapshot
Shortest Path Map correlation-based tool for capturing functionally relevant allosteric networks and its application in enzyme design
inferred← citeshttps://doi.org/10.70675/bac5b968z5ac5z406czaa3az3ea700df1ec8openalex-snapshot
Machine learning to understand and engineer the structural kinome
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