| P50 | author | Giampietro Ramponi | Q114439219 |
| | Kevin W Plaxco | Q40061619 |
| | Massimo Stefani | Q56635756 |
| | Giulia Calloni | Q56990035 |
| | Niccolo Taddei | Q57476604 |
| P2093 | author name string | Fabrizio Chiti | |
| P2860 | cites work | Development of Enzymatic Activity during Protein Folding | Q57957851 |
| | Acceleration of the folding of acylphosphatase by stabilization of local secondary structure | Q58291230 |
| | Folding studies of immunoglobulin-like β-sandwich proteins suggest that they share a common folding pathway | Q60162505 |
| | Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding | Q68030484 |
| | Hydrophilicity of polar amino acid side-chains is markedly reduced by flanking peptide bonds | Q68453330 |
| | The sequence-specific assignment of the 1H-NMR spectrum of an enzyme, horse-muscle acylphosphatase | Q69350462 |
| | Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues | Q70907210 |
| | Folding and unfolding kinetics of the proline-to-alanine mutants of bovine pancreatic ribonuclease A | Q71087379 |
| | Partially folded states of equine lysozyme. Structural characterization and significance for protein folding | Q72551818 |
| | Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2 | Q73174178 |
| | High-energy channeling in protein folding | Q73456086 |
| | Multiple roles of prolyl residues in structure and folding | Q74247254 |
| | Molecular Biology of Hydrogen Utilization in Aerobic Chemolithotrophs | Q22255626 |
| | From snapshot to movie: phi analysis of protein folding transition states taken one step further | Q24657640 |
| | Structural changes in the transition state of protein folding: alternative interpretations of curved chevron plots | Q27618392 |
| | Unspecific hydrophobic stabilization of folding transition states | Q27638872 |
| | Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain | Q27639566 |
| | Crystal structure of common type acylphosphatase from bovine testis | Q27734684 |
| | Folding kinetics of the protein pectate lyase C reveal fast-forming intermediates and slow proline isomerization | Q28211923 |
| | Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding | Q28218085 |
| | Insights into acylphosphatase structure and catalytic mechanism | Q28235991 |
| | Principles that govern the folding of protein chains | Q28236872 |
| | Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain | Q28364514 |
| | Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases | Q29616535 |
| | Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants | Q29617228 |
| | Hydrophobic core packing in the SH3 domain folding transition state | Q30167681 |
| | Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9. | Q30312660 |
| | Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates | Q30423134 |
| | Mechanisms of protein folding | Q31944289 |
| | Slow folding of muscle acylphosphatase in the absence of intermediates. | Q31990320 |
| | Slow cooperative folding of a small globular protein HPr. | Q32152487 |
| | Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts | Q33608244 |
| | Enzymes that catalyse the restructuring of proteins | Q33840728 |
| | Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. | Q33878446 |
| | Mapping the folding pathway of an immunoglobulin domain: structural detail from Phi value analysis and movement of the transition state | Q33948562 |
| | Topology, stability, sequence, and length: defining the determinants of two-state protein folding kinetics | Q34031904 |
| | Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe | Q34104675 |
| | Kinetic partitioning of protein folding and aggregation. | Q34110167 |
| | Keeping it in the family: folding studies of related proteins | Q34141529 |
| | Protein design based on folding models | Q34141538 |
| | Transient folding intermediates characterized by protein engineering | Q34351283 |
| | Contact order, transition state placement and the refolding rates of single domain proteins. | Q34464266 |
| | Prolyl isomerases | Q34545614 |
| | Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition | Q34968585 |
| | The topomer search model: A simple, quantitative theory of two-state protein folding kinetics | Q35031306 |
| | Salt-induced detour through compact regions of the protein folding landscape | Q35708354 |
| | Transient aggregates in protein folding are easily mistaken for folding intermediates | Q36178839 |
| | Designing conditions for in vitro formation of amyloid protofilaments and fibrils | Q36445068 |
| | The rate of interconversion between the two unfolded forms of ribonuclease A does not depend on guanidinium chloride concentration | Q40289731 |
| | Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues | Q40346399 |
| | Mutational analysis of the propensity for amyloid formation by a globular protein | Q40410762 |
| | On-pathway versus off-pathway folding intermediates | Q41394280 |
| | Folding of beta-sandwich proteins: three-state transition of a fibronectin type III module | Q41764385 |
| | Cis proline mutants of ribonuclease A. II. Elimination of the slow‐folding forms by mutation | Q42009152 |
| | Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins | Q43025218 |
| | Comparison of the folding processes of T. thermophilus and E. coli ribonucleases H. | Q43029909 |
| | Folding of intracellular retinol and retinoic acid binding proteins | Q43565756 |
| | Protein conformational changes induced by 1,1'-bis(4-anilino-5-naphthalenesulfonic acid): preferential binding to the molten globule of DnaK. | Q46583355 |
| | Residues participating in the protein folding nucleus do not exhibit preferential evolutionary conservation. | Q52046281 |
| | Thermodynamics and kinetics of folding of common-type acylphosphatase: comparison to the highly homologous muscle isoenzyme. | Q53129242 |
| | Protein Folding: A Perspective from Theory and Experiment. | Q54308010 |
| | How do small single-domain proteins fold? | Q55067789 |
| | Cytochrome c 553 , a small heme protein that lacks misligation in its unfolded state, folds with rapid two-state kinetics 1 1Edited by C. R. Matthews | Q57822008 |
| | Folding of circular permutants with decreased contact order: general trend balanced by protein stability 1 1Edited by A. R. Fersht | Q57823297 |
| | Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain | Q57957112 |
| P433 | issue | 3 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | protein folding | Q847556 |
| | Acylphosphatase | Q24722433 |
| | hydrophobicity | Q41854968 |
| P304 | page(s) | 577-591 | |
| P577 | publication date | 2003-07-01 | |
| P1433 | published in | Journal of Molecular Biology | Q925779 |
| P1476 | title | Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding | |
| P478 | volume | 330 | |