| scholarly article | Q13442814 |
| P50 | author | Sebastian Bittrich | Q59676928 |
| P2093 | author name string | Michael Schroeder | |
| Dirk Labudde | |||
| P2860 | cites work | Implications of thermodynamics of protein folding for evolution of primary sequences | Q59093418 |
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| A surprising simplicity to protein folding. | Q30326802 | ||
| Rupture of the hydrogen bond linking two Omega-loops induces the molten globule state at neutral pH in cytochrome c. | Q30332982 | ||
| Automated procedure for contact-map-based protein structure reconstruction. | Q30360793 | ||
| Fidelity of the protein structure reconstruction from inter-residue proximity constraints. | Q30362065 | ||
| Accurate De Novo Prediction of Protein Contact Map by Ultra-Deep Learning Model | Q30364844 | ||
| The pros and cons of predicting protein contact maps. | Q30366465 | ||
| CONFOLD: Residue-residue contact-guided ab initio protein folding. | Q30374675 | ||
| Assessment of the utility of contact-based restraints in accelerating the prediction of protein structure using molecular dynamics simulations. | Q30377837 | ||
| Optimal contact definition for reconstruction of contact maps | Q30389746 | ||
| ConEVA: a toolbox for comprehensive assessment of protein contacts | Q30396077 | ||
| Blurring contact maps of thousands of proteins: what we can learn by reconstructing 3D structure | Q30398542 | ||
| Applications of contact predictions to structural biology | Q30402065 | ||
| Comparative modeling: the state of the art and protein drug target structure prediction | Q30402152 | ||
| Principles of protein folding--a perspective from simple exact models. | Q30417429 | ||
| Conservation and prediction of solvent accessibility in protein families | Q30419557 | ||
| Defining an essence of structure determining residue contacts in proteins | Q30972736 | ||
| The RCSB protein data bank: integrative view of protein, gene and 3D structural information | Q31139806 | ||
| How protein stability and new functions trade off | Q33332450 | ||
| The hydrogen exchange core and protein folding. | Q33714720 | ||
| Protein folding: the stepwise assembly of foldon units | Q33935275 | ||
| PLIP: fully automated protein-ligand interaction profiler | Q35601315 | ||
| Hydrogen exchange methods to study protein folding | Q35850714 | ||
| Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR. | Q36199183 | ||
| Protein folding dynamics: the diffusion-collision model and experimental data | Q36278710 | ||
| Foldons, protein structural modules, and exons | Q37708079 | ||
| The role of key residues in structure, function, and stability of cytochrome-c. | Q38101468 | ||
| Early Folding Events, Local Interactions, and Conservation of Protein Backbone Rigidity | Q38273110 | ||
| Universally conserved positions in protein folds: reading evolutionary signals about stability, folding kinetics and function | Q38321925 | ||
| Improved protein structure reconstruction using secondary structures, contacts at higher distance thresholds, and non-contacts | Q38603470 | ||
| Exploring the Sequence-based Prediction of Folding Initiation Sites in Proteins | Q38617959 | ||
| Co-evolution techniques are reshaping the way we do structural bioinformatics | Q41150914 | ||
| The case for defined protein folding pathways. | Q41293309 | ||
| Origins of coevolution between residues distant in protein 3D structures. | Q41561983 | ||
| Protein folding intermediates: native-state hydrogen exchange | Q42322493 | ||
| From protein sequence to dynamics and disorder with DynaMine | Q44486815 | ||
| Quantitative evaluation of experimental NMR restraints. | Q44593564 | ||
| Assessment of contact predictions in CASP12: co-evolution and deep learning coming of age. | Q45944467 | ||
| Assessment of hard target modeling in CASP12 reveals an emerging role of alignment-based contact prediction methods. | Q46130527 | ||
| Critical assessment of methods of protein structure prediction (CASP)-Round XII. | Q46348067 | ||
| Studies on protein folding, unfolding and fluctuations by computer simulation. I. The effect of specific amino acid sequence represented by specific inter-unit interactions | Q46518756 | ||
| Forecasting residue-residue contact prediction accuracy | Q47313672 | ||
| Visualization and analysis of non-covalent contacts using the Protein Contacts Atlas. | Q47563134 | ||
| Network scaling invariants help to elucidate basic topological principles of proteins. | Q51906167 | ||
| The single helix in protein L is largely disrupted at the rate-limiting step in folding. | Q52532694 | ||
| CMView: interactive contact map visualization and analysis. | Q52896524 | ||
| Local perturbations by ligand binding of hydrogen deuterium exchange kinetics in a four-helix bundle protein, acyl coenzyme A binding protein (ACBP). | Q54005293 | ||
| Characterizing the relation of functional and Early Folding Residues in protein structures using the example of aminoacyl-tRNA synthetases | Q58098472 | ||
| P433 | issue | 1 | |
| P304 | page(s) | 18517 | |
| P577 | publication date | 2019-12-06 | |
| P1433 | published in | Scientific Reports | Q2261792 |
| P1476 | title | StructureDistiller: Structural relevance scoring identifies the most informative entries of a contact map | |
| P478 | volume | 9 |
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