Crossref
journal-article
Elsevier BV
Journal of Molecular Biology (78)
References
63
Referenced
59
10.1016/S1359-0278(96)00041-7
/ Folding Des. / Rapid formation of a molten globule intermediate in refolding of α-lactalbumin by Arai (1996)10.1016/0959-440X(93)90206-Z
/ Curr. Opin. Struct. Biol. / Pulsed H/D exchange studies of folding intermediates by Baldwin (1993)10.1016/S1359-0278(96)00003-X
/ Folding Des. / On-pathway versus off-pathway folding intermediates by Baldwin (1996)10.1016/S0021-9258(19)63827-5
/ J. Biol. Chem / The complete amino acid sequence of bovine α-lactalbumin by Brew (1970){'key': '10.1006/jmbi.1998.2100_BIB5', 'first-page': '225', 'article-title': 'Equine whey proteins', 'volume': '68B', 'author': 'Bell', 'year': '1981', 'journal-title': 'Comp. Biochem. Physiol.'}
/ Comp. Biochem. Physiol. / Equine whey proteins by Bell (1981)10.1038/nsb1296-1019
/ Nature Struct. Biol. / Kinetic intermediates in the formation of the cytochrome c molten globule by Colón (1996)10.1021/bi960052u
/ Biochemistry / Side-chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding by Colón (1996)10.1021/bi9611671
/ Biochemistry / Structure of the acid state of Escherichia coli ribonuclease HI by Dabora (1996)10.1038/nsb0197-10
/ Nature Struct. Biol. / From Levinthal to pathways to funnels by Dill (1997)10.1002/pro.5560040401
/ Protein Sci. / Principles of protein folding by Dill (1995)10.1021/bi00145a003
/ Biochemistry / Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy by Elöve (1992)10.1016/0022-2836(88)90525-6
/ J. Mol. Biol. / Thermodynamic study of the apomyoglobin structure by Griko (1988)10.1021/bi00173a036
/ Biochemistry / Energetics of the α-lactalbumin states by Griko (1994)10.1006/jmbi.1995.0510
/ J. Mol. Biol. / The unfolding thermodynamics of c-type lysozymes by Griko (1995)10.1021/bi00370a034
/ Biochemistry / Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate by Ikeguchi (1986)10.1093/oxfordjournals.jbchem.a135582
/ J. Biochem. / Ca2+-induced alteration in the unfolding behavior of α-lactalbumin by Ikeguchi (1986)10.1002/pro.5560070710
/ Protein Sci. / Transition state in the folding of α-lactalbumin probed by the 6–120 disulfide bond by Ikeguchi (1998)10.1021/bi00107a010
/ Biochemistry / Folding of chymotrypsin inhibitor 2. 1. evidence for a two-state transition by Jackson (1991)10.1126/science.8235610
/ Science / Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin by Jennings (1993)10.1021/bi00020a026
/ Biochemistry / Protein stability as a function of denaturant concentration by Johnson (1995)10.1038/nsb0596-439
/ Nature Struct. Biol. / Packing interactions in the apomyglobin folding intermediate by Kay (1996)10.1038/nsb0296-193
/ Nature Struct. Biol. / Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues by Khorasanizadeh (1996){'key': '10.1006/jmbi.1998.2100_BIB23', 'first-page': '313', 'article-title': 'Protein folding kinetics', 'volume': '40', 'author': 'Kiefhaber', 'year': '1995'}
/ Protein folding kinetics by Kiefhaber (1995)10.1073/pnas.92.20.9029
/ Proc. Natl Acad. Sci. USA / Kinetic traps in lysozyme folding by Kiefhaber (1995)10.1146/annurev.bi.59.070190.003215
/ Annu. Rev. Biochem. / Intermediates in the folding reactions of small proteins by Kim (1990)10.1002/prot.340060202
/ Proteins: Struct. Funct. Genet. / The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure by Kuwajima (1989)10.1096/fasebj.10.1.8566530
/ FASEB J / The molten globule state of α-lactalbumin by Kuwajima (1996){'key': '10.1006/jmbi.1998.2100_BIB28', 'series-title': 'Circular Dichroism and the Conformational Analysis of Biomolecules', 'first-page': '159', 'article-title': 'Stopped-flow circular dichroism', 'author': 'Kuwajima', 'year': '1996'}
/ Circular Dichroism and the Conformational Analysis of Biomolecules / Stopped-flow circular dichroism by Kuwajima (1996)10.1016/0022-2836(76)90091-7
/ J. Mol. Biol. / Three-state denaturation of α-lactalbumin by guanidine hydrochloride by Kuwajima (1976)10.1021/bi00325a010
/ Biochemistry / Comparison of the transient folding intermediates in lysozyme and α-lactalbumin by Kuwajima (1985)10.1016/0014-5793(87)80363-0
/ FEBS Letters / Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism by Kuwajima (1987)10.1016/0022-2836(89)90500-7
/ J. Mol. Biol. / Characterization of the critical state in protein folding. Effects of guanidine hydrochloride and specific Ca2+-binding on the folding kinetics of α-lactalbumin by Kuwajima (1989)10.1038/nsb0794-447
/ Nature Struct. Biol. / Molten globular characteristics of the native state of apomyoglobin by Lin (1994)10.1021/bi00010a002
/ Biochemistry / A native tertiary interaction stabilizes the A state of cytochrome c by Marmorino (1995)10.1006/jmbi.1997.1450
/ J. Mol. Biol. / Native tertiary structure in an A-state by Marmorino (1998)10.1093/protein/7.9.1089
/ Protein Eng. / Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions by Matouschek (1994)10.1038/nsb1095-871
/ Nature Struct. Biol. / Structural basis of the stability of a lysozyme molten globule by Morozova (1995)10.1006/jmbi.1997.0996
/ J. Mol. Biol. / Structural characterization and comparison of the native and A-states of equine lysozyme by Morozova-Roche (1997)10.1111/j.1432-1033.1989.tb14806.x
/ Eur. J. Biochem. / The evolution of lysozyme and α-lactalbumin by Nitta (1989)10.1016/0021-9673(91)85073-O
/ J. Chromatog. / Determination of calcium ions tightly bound to proteins by Nitta (1991)10.1016/0014-5793(87)80328-9
/ FEBS Letters / The calcium-binding property of equine lysozyme by Nitta (1987)10.1111/j.1399-3011.1993.tb00121.x
/ Int. J. Pept. Protein Res. / Comparative study of the stability of the folding intermediates of the calcium-binding lysozymes by Nitta (1993)10.1016/0014-5793(83)80010-6
/ FEBS Letters / ‘Molten-globule state’ by Ohgushi (1983)10.1016/0076-6879(86)31045-0
/ Methods Enzymol. / Determination and analysis of urea and guanidine hydrochloride denaturation curves by Pace (1986)10.1002/(SICI)1097-0134(19980101)30:1<43::AID-PROT4>3.0.CO;2-L
/ Proteins: Struct. Funct. Genet. / Is the molten globule a third thermodynamic state of protein? The example of α-lactalbumin by Pfeil (1998)10.1016/S0065-3233(08)60546-X
/ Advan. Protein Chem. / Molten globule and protein folding by Ptitsyn (1995)10.1038/308377a0
/ Nature / Similarity of the nucleotide sequences of rat α-lactalbumin and chicken lysozyme genes by Qasba (1984)10.1038/nsb0497-298
/ Nature Struct. Biol. / The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions by Raschke (1997)10.1038/335700a0
/ Nature / Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR by Roder (1988)10.1146/annurev.bb.16.060187.000555
/ Annu. Rev. Biophys. Biophys. Chem. / The thermodynamic stability of proteins by Schellman (1987)10.1038/nsb0895-663
/ Nature Struct. Biol. / Extremely rapid protein folding in the absence of intermediates by Schindler (1995){'key': '10.1006/jmbi.1998.2100_BIB52', 'series-title': 'Protein Folding', 'first-page': '197', 'article-title': 'Kinetics of unfolding and refolding of single-domain proteins', 'author': 'Schmid', 'year': '1992'}
/ Protein Folding / Kinetics of unfolding and refolding of single-domain proteins by Schmid (1992)10.1006/jmbi.1995.0579
/ J. Mol. Biol. / Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human α-lactalbumin by Schulman (1995)10.1016/S0959-440X(97)80005-X
/ Curr. Opin. Struct. Biol. / Theoretical studies of protein-folding thermodynamics and kinetics by Shakhnovich (1997)10.1006/jmbi.1998.1826
/ J. Mol. Biol. / Contribution of individual residues to formation of the native-like tertiary topology in the α-lactalbumin molten globule by Song (1998)10.1016/S0065-3233(08)60241-7
/ Advan. Protein Chem. / Protein denaturation by Tanford (1970)10.1093/oxfordjournals.jbchem.a123727
/ J. Biochem. / Crystallographic studies of a calcium binding lysozyme from equine milk at 2.5 Å resolution by Tsuge (1992)10.1021/bi00095a018
/ Biochemistry / Partially folded states of equine lysozyme by Van Dael (1993)10.1006/jmbi.1997.1030
/ J. Mol. Biol. / Three-state model for lysozyme folding by Wildegger (1997)10.1073/pnas.94.26.14314
/ Proc. Natl Acad. Sci. USA / Hydrophobic sequence minimization of the α-lactalbumin molten globule by Wu (1997)10.1006/jmbi.1998.1825
/ J. Mol. Biol. / A specific hydrophobic core in the α-lactalbumin molten globule by Wu (1998)10.1021/bi00051a003
/ Biochemistry / Folding pathway of Escherichia coli ribonuclease HI by Yamasaki (1995)10.1016/0022-2836(92)90824-4
/ J. Mol. Biol. / Absence of the thermal transition in apo-α-lactalbumin in the molten globule state by Yutani (1992)
Dates
Type | When |
---|---|
Created | 22 years, 10 months ago (Oct. 7, 2002, 7:22 a.m.) |
Deposited | 3 years, 1 month ago (June 23, 2022, 5:57 p.m.) |
Indexed | 1 month, 2 weeks ago (July 4, 2025, 7:47 a.m.) |
Issued | 26 years, 10 months ago (Oct. 1, 1998) |
Published | 26 years, 10 months ago (Oct. 1, 1998) |
Published Print | 26 years, 10 months ago (Oct. 1, 1998) |
Funders
1
Ministry of Education, Culture, Sports, Science and Technology
10.13039/501100001700
Region: Asia
gov (National government)
Labels
3
- Monbu-kagaku-shō
- 文部科学省
- MEXT
@article{Mizuguchi_1998, title={Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy}, volume={283}, ISSN={0022-2836}, url={http://dx.doi.org/10.1006/jmbi.1998.2100}, DOI={10.1006/jmbi.1998.2100}, number={1}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Mizuguchi, Mineyuki and Arai, Munehito and Ke, Yue and Nitta, Katsutoshi and Kuwajima, Kunihiro}, year={1998}, month=oct, pages={265–277} }