| scholarly article | Q13442814 |
| P2093 | author name string | Patrizia Polverino de Laureto | |
| Angelo Fontana | |||
| Erica Frare | |||
| Rossella Gottardo | |||
| Herman Van Dael | |||
| P2860 | cites work | Structure and thermodynamics of the extraordinarily stable molten globule state of canine milk lysozyme | Q27621804 |
| Crystal structures of apo- and holo-bovine alpha-lactalbumin at 2. 2-A resolution reveal an effect of calcium on inter-lobe interactions | Q27625381 | ||
| Crystal structures of guinea-pig, goat and bovine alpha-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase | Q27733380 | ||
| Effect of the extra n-terminal methionine residue on the stability and folding of recombinant alpha-lactalbumin expressed in Escherichia coli | Q27766482 | ||
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| Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa | Q27861105 | ||
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| From Levinthal to pathways to funnels | Q28300934 | ||
| Comparison of the structural and dynamical properties of holo and apo bovine alpha-lactalbumin by NMR spectroscopy. | Q30328039 | ||
| The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. | Q30385457 | ||
| Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates | Q30423134 | ||
| Hydrogen exchange: the modern legacy of Linderstrøm-Lang | Q30427220 | ||
| Protein interactions leading to conformational changes monitored by limited proteolysis: apo form and fragments of horse cytochrome c. | Q30727543 | ||
| Role of the molten globule state in protein folding. | Q33883824 | ||
| Equilibrium and Kinetic Studies on Folding of the Authentic and Recombinant Forms of Human α-Lactalbumin by Circular Dichroism Spectroscopy† | Q58840872 | ||
| Calorimetric determination of the energetics of the molten globule intermediate in protein folding: apo-alpha-lactalbumin | Q68030513 | ||
| Evidence for a molten globule state as a general intermediate in protein folding | Q68738248 | ||
| Comparison of the binding of Ca2+ and Mn2+ to bovine alpha-lactalbumin and equine lysozyme | Q69408497 | ||
| Correlation between sites of limited proteolysis and segmental mobility in thermolysin | Q69506899 | ||
| Ca2+-induced alteration in the unfolding behavior of alpha-lactalbumin | Q69517122 | ||
| Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange | Q69792095 | ||
| Comparative study of the stability of the folding intermediates of the calcium-binding lysozymes | Q70624539 | ||
| Simple two-step procedure for the preparation of highly active pure equine milk lysozyme | Q70950157 | ||
| Alpha-Lactalbumin: compact state with fluctuating tertiary structure? | Q71064817 | ||
| Structural basis of the stability of a lysozyme molten globule | Q71726957 | ||
| The unfolding thermodynamics of c-type lysozymes: a calorimetric study of the heat denaturation of equine lysozyme | Q71751606 | ||
| A protein dissection study of a molten globule | Q72266488 | ||
| Bipartite structure of the alpha-lactalbumin molten globule | Q72347294 | ||
| Partially folded states of equine lysozyme. Structural characterization and significance for protein folding | Q72551818 | ||
| Protein folding. Solid evidence for molten globules | Q72787914 | ||
| The molten globule state of a chimera of human alpha-lactalbumin and equine lysozyme | Q73062186 | ||
| Kinetic role of early intermediates in protein folding | Q73070815 | ||
| Raman optical activity characterization of native and molten globule states of equine lysozyme: comparison with hen lysozyme and bovine alpha-lactalbumin | Q73911191 | ||
| Hydrogen exchange study of canine milk lysozyme: stabilization mechanism of the molten globule | Q74015797 | ||
| [How many molten globules states exist?] | Q77082683 | ||
| Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy | Q77373730 | ||
| Energetics of three-state unfolding of a protein: canine milk lysozyme | Q77542902 | ||
| Fine tuning the N-terminus of a calcium binding protein: alpha-lactalbumin | Q78140818 | ||
| Amino acid sequence around the cysteine residues of pigeon egg-white lysozyme: comparative study with other type c lysozymes | Q93683100 | ||
| Comparison of equilibrium and kinetic approaches for determining protein folding mechanisms | Q33883828 | ||
| Protein folding intermediates and pathways studied by hydrogen exchange | Q34001354 | ||
| ‘Molten‐globule state’: a compact form of globular proteins with mobile side‐chains | Q34255230 | ||
| THE AMINO ACID SEQUENCE OF EGG WHITE LYSOZYME | Q34255405 | ||
| Protein aggregation: folding aggregates, inclusion bodies and amyloid | Q34460420 | ||
| The evolution of lysozyme and alpha-lactalbumin | Q34531208 | ||
| Limited proteolysis of bovine alpha-lactalbumin: isolation and characterization of protein domains | Q36281337 | ||
| Equilibrium and kinetic folding of pigeon lysozyme | Q38336916 | ||
| Metal-ion binding and the molecular conformational properties of alpha lactalbumin | Q38749005 | ||
| Three-state denaturation of α-lactalbumin by guanidine hydrochloride | Q39118524 | ||
| Equilibrium and kinetics of the thermal unfolding of α-lactalbumin. The relation to its folding mechanism | Q39207434 | ||
| Aromatic Contributions To Circular Dichroism Spectra Of Protein | Q39936788 | ||
| Compact Intermediate States in Protein Folding | Q40476020 | ||
| Pathways of protein folding | Q40835296 | ||
| Molten globule and protein folding | Q40944932 | ||
| The molten globule state of alpha-lactalbumin. | Q40949095 | ||
| Intermediate states in protein folding | Q40990251 | ||
| Time-resolved biophysical methods in the study of protein folding | Q41206751 | ||
| The application of circular dichroism to studies of protein folding and unfolding | Q41452511 | ||
| Probing the partly folded states of proteins by limited proteolysis | Q41458691 | ||
| Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of alpha-lactalbumin and lysozyme | Q41478567 | ||
| The structural aspects of limited proteolysis of native proteins | Q41738009 | ||
| Energetics of solvent and ligand-induced conformational changes in alpha-lactalbumin. | Q41877826 | ||
| Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering | Q42845790 | ||
| Calcium-binding and structural stability of echidna and canine milk lysozymes | Q42846123 | ||
| Molecular cloning and nucleotide sequence of a bovine alpha-lactalbumin cDNA. | Q43458214 | ||
| The amino acid sequence of equine milk lysozyme | Q43494039 | ||
| Stepwise proteolytic removal of the beta subdomain in alpha-lactalbumin. The protein remains folded and can form the molten globule in acid solution | Q43698087 | ||
| Absence of the thermal transition in apo-alpha-lactalbumin in the molten globule state. A study by differential scanning microcalorimetry | Q44533041 | ||
| The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions. | Q45952003 | ||
| Anion-induced folding of Staphylococcal nuclease: characterization of multiple equilibrium partially folded intermediates. | Q46010103 | ||
| Discrete intermediates versus molten globule models for protein folding: characterization of partially folded intermediates of apomyoglobin | Q46133803 | ||
| Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding | Q46559043 | ||
| Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin | Q46929622 | ||
| Sequences of two highly divergent canine type c lysozymes: implications for the evolutionary origins of the lysozyme/alpha-lactalbumin superfamily | Q47222856 | ||
| Molecular dynamics simulations of apocytochrome b562--the highly ordered limit of molten globules | Q47630366 | ||
| Structural characterisation and comparison of the native and A-states of equine lysozyme. | Q50528369 | ||
| Probing the conformational state of apomyoglobin by limited proteolysis. | Q52524166 | ||
| Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins. | Q52879960 | ||
| Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. | Q52900971 | ||
| Alpha-lactalbumin forms a compact molten globule in the absence of disulfide bonds. | Q54077167 | ||
| Probing the molten globule state of alpha-lactalbumin by limited proteolysis. | Q54160128 | ||
| Limited proteolysis of cytochrome c in trifluoroethanol. | Q54175197 | ||
| Local structural preferences in the alpha-lactalbumin molten globule. | Q54615586 | ||
| Rapid collapse and slow structural reorganisation during the refolding of bovine α-lactalbumin 1 1Edited by P. E. Wright | Q57889918 | ||
| A residue-specific NMR view of the non-cooperative unfolding of a molten globule | Q57889932 | ||
| Structural characterization of a highly–ordered ‘molten globule’ at low pH | Q57889953 | ||
| What is the molten globule? | Q58007405 | ||
| Cooperative thermal transitions of bovine and human apo-α-lactalbumins: evidence for a new intermediate state | Q58322027 | ||
| P433 | issue | 12 | |
| P921 | main subject | proteolysis | Q33123 |
| P304 | page(s) | 2932-2946 | |
| P577 | publication date | 2002-12-01 | |
| P1433 | published in | Protein Science | Q7251445 |
| P1476 | title | Partly folded states of members of the lysozyme/lactalbumin superfamily: a comparative study by circular dichroism spectroscopy and limited proteolysis | |
| P478 | volume | 11 |
| Q43057928 | A comparative study of the alpha-subdomains of bovine and human alpha-lactalbumin reveals key differences that correlate with molten globule stability |
| Q92932862 | A simple and rapid pipeline for identification of receptor-binding sites on the surface proteins of pathogens |
| Q53612710 | Acid-induced unfolding kinetics in simulated gastric digestion of proteins. |
| Q35881297 | Binding of lysozyme to phospholipid bilayers: evidence for protein aggregation upon membrane association |
| Q37916600 | Bioactivity of α-lactalbumin related to its interaction with fatty acids: a review. |
| Q41490934 | Differential stabilities of alternative exon-skipped rod motifs of dystrophin |
| Q38322697 | Egg proteins as allergens and the effects of the food matrix and processing |
| Q42000625 | Equilibrium and kinetic studies on folding of canine milk lysozyme |
| Q28480624 | Evidence for conserved function of γ-glutamyltranspeptidase in Helicobacter genus |
| Q43107662 | Exploring tryptophan dynamics in acid-induced molten globule state of bovine alpha-lactalbumin: a wavelength-selective fluorescence approach |
| Q35751822 | Förster resonance energy transfer evidence for lysozyme oligomerization in lipid environment |
| Q37626736 | Identification of in vitro autophosphorylation sites and effects of phosphorylation on the Arabidopsis CRINKLY4 (ACR4) receptor-like kinase intracellular domain: insights into conformation, oligomerization, and activity. |
| Q45947665 | Immunological behavior of in vitro digested egg-white lysozyme. |
| Q44701435 | Iron-sulfur cluster biosynthesis: biochemical characterization of the conformational dynamics of Thermotoga maritima IscU and the relevance for cellular cluster assembly |
| Q37397893 | Iron-sulfur cluster biosynthesis: characterization of a molten globule domain in human NFU. |
| Q91817045 | Life in Phases: Intra- and Inter- Molecular Phase Transitions in Protein Solutions |
| Q52624824 | Modulation of physiological and pathological activities of lysozyme by biological membranes. |
| Q39628392 | Role of low native state kinetic stability and interaction of partially unfolded states with molecular chaperones in the mitochondrial protein mistargeting associated with primary hyperoxaluria |
| Q43176751 | Synthetic "chaperones": nanoparticle-mediated refolding of thermally denatured proteins |
| Q43056019 | The effects of molecular crowding on the amyloid fibril formation of alpha-lactalbumin and the chaperone action of alpha-casein |
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