| scholarly article | Q13442814 |
| P356 | DOI | 10.1074/JBC.M108057200 |
| P698 | PubMed publication ID | 11560938 |
| P2093 | author name string | Jui-Yoa Chang | |
| P2860 | cites work | Polymer principles and protein folding | Q24672635 |
| Understanding protein folding via free-energy surfaces from theory and experiment | Q28139374 | ||
| Pathways for protein disulphide bond formation | Q28141294 | ||
| alpha-Lactalbumin: structure and function | Q28144778 | ||
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| From Levinthal to pathways to funnels | Q28300934 | ||
| Rapid formation of a molten globule intermediate in refolding of alpha-lactalbumin | Q28306450 | ||
| Folding of newly translated proteins in vivo: the role of molecular chaperones | Q29619368 | ||
| Reexamination of the folding of BPTI: predominance of native intermediates. | Q30358776 | ||
| The disulfide folding pathway of tick anticoagulant peptide (TAP), a Kunitz-type inhibitor structurally homologous to BPTI | Q71506653 | ||
| The disulfide folding pathway of human epidermal growth factor | Q72167777 | ||
| Bipartite structure of the alpha-lactalbumin molten globule | Q72347294 | ||
| Secondary structure of globular proteins at the early and the final stages in protein folding | Q72615791 | ||
| Kinetic role of a meta-stable native-like two-disulphide species in the folding transition of bovine pancreatic trypsin inhibitor | Q72753383 | ||
| Disulfide-rearranged molten globule state of alpha-lactalbumin | Q72782916 | ||
| Structure and heterogeneity of the one- and two-disulfide folding intermediates of tick anticoagulant peptide | Q73107554 | ||
| Probing the folding pathways of long R(3) insulin-like growth factor-I (LR(3)IGF-I) and IGF-I via capture and identification of disulfide intermediates by cyanylation methodology and mass spectrometry | Q73297494 | ||
| Illuminating folding intermediates | Q73333912 | ||
| Transient non-native secondary structures during the refolding of alpha-lactalbumin detected by infrared spectroscopy | Q73333946 | ||
| A stabilized molten globule protein | Q73378128 | ||
| Folding consensus? | Q73435431 | ||
| Denatured states of tick anticoagulant peptide. Compositional analysis of unfolded scrambled isomers | Q77732828 | ||
| The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. | Q30385457 | ||
| Theory of protein folding: the energy landscape perspective | Q30428743 | ||
| A major kinetic trap for the oxidative folding of human epidermal growth factor | Q30967084 | ||
| Mechanisms of protein folding | Q31944289 | ||
| Trapping of intermediates during the refolding of recombinant human epidermal growth factor (hEGF) by cyanylation, and subsequent structural elucidation by mass spectrometry | Q32065532 | ||
| Is protein folding hierarchic? I. Local structure and peptide folding | Q33543968 | ||
| Folding funnels, binding funnels, and protein function | Q33674287 | ||
| Autonomous protein folding units | Q33883803 | ||
| Role of the molten globule state in protein folding. | Q33883824 | ||
| Disulfide bonds and protein folding. | Q33887218 | ||
| Protein folding intermediates and pathways studied by hydrogen exchange | Q34001354 | ||
| Topology, stability, sequence, and length: defining the determinants of two-state protein folding kinetics | Q34031904 | ||
| Native disulfide bond formation in proteins | Q34046362 | ||
| Protein folding: progress made and promises ahead | Q34104532 | ||
| Biomedical implications of protein folding and misfolding | Q34136797 | ||
| Protein folding theory: from lattice to all-atom models | Q34243263 | ||
| Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human alpha-lactalbumin | Q34288348 | ||
| The 28-111 disulfide bond constrains the alpha-lactalbumin molten globule and weakens its cooperativity of folding | Q35646586 | ||
| A Ca(2+)-binding chimera of human lysozyme and bovine alpha-lactalbumin that can form a molten globule | Q38295610 | ||
| Multiple pathways for regenerating ribonuclease A. | Q40204307 | ||
| Conformational comparison between alpha-lactalbumin and lysozyme | Q40502199 | ||
| Navigating the folding routes | Q40610371 | ||
| Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment | Q40869927 | ||
| How important is the molten globule for correct protein folding? | Q41341086 | ||
| Oxidative refolding of insulin-like growth factor 1 yields two products of similar thermodynamic stability: a bifurcating protein-folding pathway | Q42622478 | ||
| Electrostatic interactions in the acid denaturation of alpha-lactalbumin determined by NMR. | Q42846773 | ||
| The structure of denatured alpha-lactalbumin elucidated by the technique of disulfide scrambling: fractionation of conformational isomers of alpha-lactalbumin | Q43512154 | ||
| A specific hydrophobic core in the alpha-lactalbumin molten globule | Q47885497 | ||
| Alpha-lactalbumin forms a compact molten globule in the absence of disulfide bonds. | Q54077167 | ||
| Protein Folding: A Perspective from Theory and Experiment. | Q54308010 | ||
| Local structural preferences in the alpha-lactalbumin molten globule. | Q54615586 | ||
| How do small single-domain proteins fold? | Q55067789 | ||
| Rapid collapse and slow structural reorganisation during the refolding of bovine α-lactalbumin 1 1Edited by P. E. Wright | Q57889918 | ||
| Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A | Q60091267 | ||
| Protein folding | Q68539600 | ||
| Characterization of the critical state in protein folding. Effects of guanidine hydrochloride and specific Ca2+ binding on the folding kinetics of alpha-lactalbumin | Q69601709 | ||
| Folding intermediates studied by circular dichroism | Q69647534 | ||
| Amide proton exchange as a probe of protein folding pathways | Q69647537 | ||
| Disulfide bonds as probes of protein folding pathways | Q69647577 | ||
| Calcium regulates folding and disulfide-bond formation in alpha-lactalbumin | Q69734622 | ||
| Pathway of disulfide-coupled unfolding and refolding of bovine alpha-lactalbumin | Q70644814 | ||
| Disulfide determinants of calcium-induced packing in alpha-lactalbumin | Q70862469 | ||
| P433 | issue | 1 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 120-126 | |
| P577 | publication date | 2001-09-17 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | The folding pathway of alpha-lactalbumin elucidated by the technique of disulfide scrambling. Isolation of on-pathway and off-pathway intermediates | |
| P478 | volume | 277 |
| Q33716473 | Buffed energy landscapes: another solution to the kinetic paradoxes of protein folding |
| Q53393870 | Characterization of an alternative low energy fold for bovine α-lactalbumin formed by disulfide bond shuffling. |
| Q57956897 | Characterizing the Tick Carboxypeptidase Inhibitor |
| Q83275101 | Conformational isomers of denatured and unfolded proteins: methods of production and applications |
| Q34852456 | Denaturation and unfolding of human anaphylatoxin C3a: an unusually low covalent stability of its native disulfide bonds |
| Q37787263 | Distinct Folding Pathways of Two Homologous Disulfide Proteins: Bovine Pancreatic Trypsin Inhibitor and Tick Anticoagulant Peptide |
| Q41660385 | Effects of Metal Ions, Temperature, and a Denaturant on the Oxidative Folding Pathways of Bovine α-Lactalbumin. |
| Q84325236 | Fast and slow tracks in lysozyme folding elucidated by the technique of disulfide scrambling |
| Q51766347 | Non-Native Conformational Isomers of the Catalytic Domain of PCSK9 Induce an Immune Response, Reduce Lipids and Increase LDL Receptor Levels. |
| Q30336354 | Oxidative folding of Amaranthus alpha-amylase inhibitor: disulfide bond formation and conformational folding. |
| Q47265654 | Role of kinetic intermediates in the folding of leech carboxypeptidase inhibitor |
| Q44871285 | Two-state folding of lysozyme versus multiple-state folding of alpha-lactalbumin illustrated by the technique of disulfide scrambling |
| Q46576961 | Unfolding and breakdown of insulin in the presence of endogenous thiols |
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