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References from Protposer: The web server that readily proposes protein stabilizing mutations with high PPV. Local targets link to admitted publications; unresolved targets remain external evidence.
10.1038/299756a0
10.1038/299756a0 · External reference
Oligonucleotide-directed mutagenesis as a general and powerful method for studies of protein function
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The challenge of enzyme cost in the production of lignocellulosic biofuels
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Protein-based nanomaterials and nanosystems for biomedical applications: A review
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10.1016/j.csbj.2018.01.002 · Admitted local publication
A Fuzzy Query Method Based on Human-Readable Rules for Predicting Protein Stability Changes
10.2174/18741991008020100143 · 2009 · External reference
mCSM: predicting the effects of mutations in proteins using graph-based signatures
10.1093/bioinformatics/btt691 · 2013 · External reference
ENCoM server: exploring protein conformational space and the effect of mutations on protein function and stability
10.1093/nar/gkv343 · 2015 · External reference
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I-Mutant2. 0: predicting stability changes upon mutation from the protein sequence or structure
10.1093/nar/gki375 · 2005 · External reference
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10.1093/protein/gzp030 · External reference
10.1093/bioinformatics/bty340
10.1093/bioinformatics/bty340 · External reference
Artificial intelligence challenges for predicting the impact of mutations on protein stability
10.1016/j.sbi.2021.11.001 · 2021 · External reference
Predicting changes in protein thermodynamic stability upon point mutation with deep 3D convolutional neural networks
10.1371/journal.pcbi.1008291 · 2020 · External reference
10.1021/acs.jcim.1c00201
10.1021/acs.jcim.1c00201 · External reference
A study in Rashomon curves and volumes: A new perspective on generalization and model simplicity in machine learning
2019 · External reference
10.1093/bioinformatics/btp445
10.1093/bioinformatics/btp445 · External reference
PoPMuSiC 2.1: a web server for the estimation of protein stability changes upon mutation and sequence optimality
10.1186/1471-2105-12-151 · 2011 · External reference
10.1016/j.jbiotec.2012.06.020
10.1016/j.jbiotec.2012.06.020 · External reference
Alpha-Helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces
1992 · External reference
Elucidating the Folding Problem of Helical Peptides Using Empirical Parameters
10.1038/nsb0694-399 · 1994 · External reference
Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides
10.1006/jmbi.1994.0023 · 1995 · External reference
Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence
10.1006/jmbi.1994.0024 · 1995 · External reference
10.1016/s0014-5793(98)00569-9
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10.1110/ps.062274906
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10.1016/j.jmb.2006.02.060
10.1016/j.jmb.2006.02.060 · External reference
Predicting stabilizing mutations in proteins using Poisson-Boltzmann based models: study of unfolded state ensemble models and development of a successful binary classifier based on residue interaction energies
10.1039/c5cp04348d · 2015 · External reference
Mutation of exposed hydrophobic amino acids to arginine to increase protein stability
10.1186/1471-2091-5-9 · 2004 · External reference
10.1093/protein/gzq072
10.1093/protein/gzq072 · External reference
Stabilization of apoflavodoxin by replacing hydrogen-bonded charged Asp or Glu residues by the neutral isosteric Asn or Gln
10.1093/protein/14.3.173 · 2001 · External reference
Consensus sequence design as a general strategy to create hyperstable, biologically active proteins
10.1073/pnas.1816707116 · 2019 · External reference
Ancestral protein reconstruction: Techniques and applications
10.1515/hsz-2015-0158 · 2016 · External reference
Rational stabilization of complex proteins: a divide and combine approach
10.1038/srep09129 · 2015 · External reference
10.1093/nar/gkx285
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10.1038/nsb1203-980
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The worldwide Protein Data Bank (wwPDB): ensuring a single, uniform archive of PDB data
10.1093/nar/gkl971 · 2006 · External reference
Unresolved reference
External reference
Quantification of biases in predictions of protein stability changes upon mutations
10.1101/308239 · 2018 · External reference
A critical review of five machine learning-based algorithms for predicting protein stability changes upon mutation
2019 · External reference
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10.1002/prot.22488 · External reference
Applications of network BLAST server
10.1016/s0076-6879(96)66011-x · 1996 · External reference
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2013 · External reference
The SWISS-PROT protein sequence data bank and its supplement TrEMBL
10.1093/nar/25.1.31 · 1997 · External reference
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10.1093/nar/gkg040 · 2003 · External reference
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PAML: a program package for phylogenetic analysis by maximum likelihood
10.1093/bioinformatics/13.5.555 · 1997 · External reference
The rapid generation of mutation data matrices from protein sequences
1992 · External reference
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10.1186/1471-2105-5-113 · External reference
10.1093/bioinformatics/btp163
10.1093/bioinformatics/btp163 · External reference
10.1002/bip.360221211
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10.1006/jmbi.1994.1334
10.1006/jmbi.1994.1334 · External reference
ProtSA: a web application for calculating sequence specific protein solvent accessibilities in the unfolded ensemble
10.1186/1471-2105-10-104 · 2009 · External reference
10.1529/biophysj.106.087528
10.1529/biophysj.106.087528 · External reference
Voronoia: analyzing packing in protein structures
10.1093/nar/gkn769 · 2009 · External reference
10.1007/978-1-4939-7231-9_4
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10.1006/jmbi.1993.1626
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10.1110/ps.9.9.1753
10.1110/ps.9.9.1753 · External reference
10.1006/jmbi.1998.2401
10.1006/jmbi.1998.2401 · External reference
DelPhi: a comprehensive suite for DelPhi software and associated resources
2012 · External reference
GROMACS 3.0: a package for molecular simulation and trajectory analysis
10.1007/s008940100045 · 2001 · External reference
10.1016/j.softx.2015.06.001 · Admitted local publication
ProTherm, version 4.0: Thermodynamic database for proteins and mutants
2004 · External reference
ProTherm and ProNIT: thermodynamic databases for proteins and protein–nucleic acid interactions
10.1093/nar/gkj103 · 2006 · External reference
Systematic investigation of the data set dependency of protein stability predictors
10.1021/acs.jcim.0c00591 · 2020 · External reference
10.1016/s0969-2126(97)00260-8
10.1016/s0969-2126(97)00260-8 · External reference
ThermoMutDB: a thermodynamic database for missense mutations
10.1093/nar/gkaa925 · 2021 · External reference
Protein stability engineering insights revealed by domain-wide comprehensive mutagenesis
10.1073/pnas.1903888116 · 2019 · External reference
Energetics of a hydrogen bond (charged and neutral) and of a cation-π interaction in apoflavodoxin
10.1006/jmbi.1999.2863 · 1999 · External reference
10.1006/jmbi.2001.4436
10.1006/jmbi.2001.4436 · External reference
10.1002/prot.21041
10.1002/prot.21041 · External reference
FtsH cleavage of non-native conformations of proteins
10.1016/j.jsb.2010.05.001 · 2010 · External reference
Do Proteins with Similar Folds Have Similar Transition State Structures? A Diffuse Transition State of the 169 Residue Apoflavodoxin
10.1016/j.jmb.2006.03.067 · 2006 · External reference
Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation
10.1016/j.jmb.2004.09.047 · 2004 · External reference
Structure of stable protein folding intermediates by equilibrium φ-analysis: The apoflavodoxin thermal intermediate
10.1016/j.jmb.2004.08.081 · 2004 · External reference
10.1529/biophysj.104.050203
10.1529/biophysj.104.050203 · External reference
10.3390/ijms19041009
10.3390/ijms19041009 · External reference
A three-state prediction of single point mutations on protein stability changes
10.1186/1471-2105-9-s2-s6 · 2008 · External reference
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10.1021/acs.jcim.1c00160 · External reference
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10.1002/jcc.26810
10.1002/jcc.26810 · External reference
Unresolved reference
2019 · External reference
10.1093/bib/bbz146
10.1093/bib/bbz146 · External reference
Four-State Equilibrium Unfolding of an scFv Antibody Fragment†
10.1021/bi025742e · 2002 · External reference
10.1016/j.cplett.2005.02.029
10.1016/j.cplett.2005.02.029 · External reference
Length variations amongst protein domain superfamilies and consequences on structure and function
10.1371/journal.pone.0004981 · 2009 · External reference
10.1038/nrg3927
10.1038/nrg3927 · External reference
10.1038/nmeth.3027
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Identification of stabilizing point mutations through mutagenesis of destabilized protein libraries
10.1016/j.jbc.2022.101785 · 2022 · External reference
10.1016/j.cbpa.2014.09.013
10.1016/j.cbpa.2014.09.013 · External reference
Predicting the effects of coding non-synonymous variants on protein function using the SIFT algorithm
10.1038/nprot.2009.86 · 2009 · External reference
10.1101/gr.176601
10.1101/gr.176601 · External reference
10.1093/nar/gkg509
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Unresolved reference
2006 · External reference
10.1093/bioinformatics/btv195
10.1093/bioinformatics/btv195 · External reference
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Predicting the functional effect of amino acid substitutions and indels
10.1371/journal.pone.0046688 · 2012 · External reference
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Mutational landscape of K-Ras substitutions at 12th position-a systematic molecular dynamics approach
10.1080/07391102.2020.1830177 · 2022 · External reference
Accurate calculation of barnase and SNase folding energetics using short molecular dynamics simulations and an atomistic model of the unfolded ensemble: evaluation of force fields and water models
10.1021/acs.jcim.9b00430 · 2019 · External reference
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10.1039/c3cs60137d · External reference
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10.1016/j.jbiotec.2004.03.026 · External reference
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The ‘relevant’ stability of proteins with equilibrium intermediates
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Protein dynamics governed by interfaces of high polarity and low packing density
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