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Effect of Protein Backbone Folding on the Stability of Protein−Ligand Complexes
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Outgoing claims: the papers this work cites, builds on, or argues with.
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Molecular docking using surface complementarity
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The effect of inhibitor binding on the structural stability and cooperativity of the HIV-1 protease
inferredcites →https://doi.org/10.1002/(sici)1097-461x(1999)75:6<1017::aid-qua6>3.0.co;2-copenalex-snapshot
On a characterization of the folding of proteins
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Predicting binding energetics from structure: Looking beyond ?G�
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Prediction of the binding energy for small molecules, peptides and proteins
inferredcites →https://doi.org/10.1002/1097-461x(2000)80:4/5<848::aid-qua34>3.0.co;2-dopenalex-snapshot
Relative measure of geometrical entanglement to study folding-unfolding transitions. Application to analysis of molecular dynamics trajectories of proteinsin vacuo
inferredcites →https://doi.org/10.1002/anie.200200565openalex-snapshot
Binding Affinities of Host–Guest, Protein–Ligand, and Protein–Transition‐State Complexes
inferredcites →https://doi.org/10.1002/jmr.300080603openalex-snapshot
Occluded molecular surface: Analysis of protein packing
inferredcites →https://doi.org/10.1002/prot.10609openalex-snapshot
Characterization of the amino acid contribution to the folding degree of proteins
inferredcites →https://doi.org/10.1006/jmbi.1998.2090openalex-snapshot
The structural stability of the HIV-1 protease 1 1Edited by P. E. Wright
inferredcites →https://doi.org/10.1007/s001090000084openalex-snapshot
Recent developments in structure-based drug design
inferredcites →https://doi.org/10.1016/j.compbiolchem.2005.06.005openalex-snapshot
Folding degrees of azurins and pseudoazurins
inferredcites →https://doi.org/10.1016/s0009-2614(00)00158-5openalex-snapshot
Characterization of 3D molecular structure
inferredcites →https://doi.org/10.1016/s0009-2614(97)00447-8openalex-snapshot
Characterization of 3-D sequences of proteins
inferredcites →https://doi.org/10.1016/s0065-3233(08)60377-0openalex-snapshot
Stability of Protein Structure and Hydrophobic Interaction
inferredcites →https://doi.org/10.1016/s0076-6879(98)95038-8openalex-snapshot
[7] Molecular crowding: Analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion
inferredcites →https://doi.org/10.1016/s0076-6879(98)95045-5openalex-snapshot
[14] Prediction of binding energetics from structure using empirical parameterization
inferredcites →https://doi.org/10.1016/s0958-1669(02)00010-1openalex-snapshot
Chemical proteomics and its application to drug discovery
inferredcites →https://doi.org/10.1016/s0969-2126(99)80097-5openalex-snapshot
Residue depth: a novel parameter for the analysis of protein structure and stability
inferredcites →https://doi.org/10.1016/s1476-9271(02)00078-6openalex-snapshot
Application of a novel graph-theoretic folding degree index to the study of steroid–DB3 antibody binding affinity
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Thermodynamic and Structural Studies of Cavity Formation in Proteins Suggest That Loss of Packing Interactions Rather Than the Hydrophobic Effect Dominates the Observed Energetics ,
inferredcites →https://doi.org/10.1021/bi00154a023openalex-snapshot
Use of protein unfolding studies to determine the conformational and dimeric stabilities of HIV-1 and SIV proteases
inferredcites →https://doi.org/10.1021/bi00483a001openalex-snapshot
Dominant forces in protein folding
inferredcites →https://doi.org/10.1021/bi00781a013openalex-snapshot
Thermodynamics of the binding of S-peptide to S-protein to form ribonuclease S'
inferredcites →https://doi.org/10.1021/bi00781a014openalex-snapshot
Binding of cations to caseins. Site binding, Donnan binding, and system characteristics
inferredcites →https://doi.org/10.1021/bi050001+openalex-snapshot
Attempts to Delineate the Relative Contributions of Changes in Hydrophobicity and Packing to Changes in Stability of Ribonuclease S Mutants
inferredcites →https://doi.org/10.1021/bi9701742openalex-snapshot
Structure-Based Thermodynamic Analysis of HIV-1 Protease Inhibitors
inferredcites →https://doi.org/10.1021/ci034278xopenalex-snapshot
A Protein Folding Degree Measure and Its Dependence on Crystal Packing, Protein Size, Secondary Structure, and Domain Structural Class
inferredcites →https://doi.org/10.1021/ci990323iopenalex-snapshot
Characterization of Fold Diversity among Proteins with the Same Number of Amino Acid Residues
inferredcites →https://doi.org/10.1021/ja993810nopenalex-snapshot
Quantitative Symmetry in Structure−Activity Correlations: The Near C2 Symmetry of Inhibitor/HIV Protease Complexes
inferredcites →https://doi.org/10.1038/342299a0openalex-snapshot
X-ray analysis of HIV-1 proteinase at 2.7 Å resolution confirms structural homology among retroviral enzymes
inferredcites →https://doi.org/10.1039/b405153jopenalex-snapshot
Quantitative characterization of protein structure: application to a novel α/β fold
inferredcites →https://doi.org/10.1081/rrs-120037896openalex-snapshot
Thermodynamics of Protein–Ligand Interactions: History, Presence, and Future Aspects
inferredcites →https://doi.org/10.1093/bioinformatics/18.5.697openalex-snapshot
Characterization of the folding degree of proteins
inferredcites →https://doi.org/10.1177/135965350200600401openalex-snapshot
Combination of Protease Inhibitors for the Treatment of HIV-1-Infected Patients: A Review of Pharmacokinetics and Clinical Experience
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Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Alignment-free Prediction of Ribonucleases using a Computational Chemistry approach: Comparison with HMM model and Isolation from Schizosaccharomyces pombe, Prediction, and Experimental assay of a new sequence
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