-
1
-
-
0014730026
-
Analytical gel chromatography of proteins
-
Ackers G.L. Analytical gel chromatography of proteins. Advan. Protein Chem. 24:1970;343-446
-
(1970)
Advan. Protein Chem.
, vol.24
, pp. 343-446
-
-
Ackers, G.L.1
-
2
-
-
0015870378
-
Circular dichroism and optical rotatory dispersion of proteins and polypeptides
-
Adler A.J., Greenfield N.J., Fasman G.D. Circular dichroism and optical rotatory dispersion of proteins and polypeptides. Methods Enzymol. 27:1973;675-735
-
(1973)
Methods Enzymol
, vol.27
, pp. 675-735
-
-
Adler, A.J.1
Greenfield, N.J.2
Fasman, G.D.3
-
3
-
-
0029123975
-
Following protein folding in real time using NMR spectroscopy
-
Balbach J., Forge V., Van Nuland N.A., Winder S.L., Hore P.J., Dobson C.M. Following protein folding in real time using NMR spectroscopy. Nature Struct. Biol. 2:1995;865-870
-
(1995)
Nature Struct. Biol.
, vol.2
, pp. 865-870
-
-
Balbach, J.1
Forge, V.2
Van Nuland, N.A.3
Winder, S.L.4
Hore, P.J.5
Dobson, C.M.6
-
4
-
-
0000992692
-
Molten globule: Specific or nonspecific folding intermediates?
-
Baldwin R.L. Molten globule specific or nonspecific folding intermediates? Chemtracts-Biochem. Mol. Biol. 2:1991;379-389
-
(1991)
Chemtracts-Biochem. Mol. Biol.
, vol.2
, pp. 379-389
-
-
Baldwin, R.L.1
-
5
-
-
0029249945
-
The nature of protein folding pathways: The classical versus the new
-
Baldwin R.L. The nature of protein folding pathways The classical versus the new. J. Biomol. NMR. 5:1995;103-109
-
(1995)
J. Biomol. NMR
, vol.5
, pp. 103-109
-
-
Baldwin, R.L.1
-
6
-
-
0026534194
-
PH-induced folding/unfolding of staphylococcal nuclease: Determination of kinetic parameters by the sequential-jump method
-
Chen H.M., Markin V.S., Tsong T.Y. PH-induced folding/unfolding of staphylococcal nuclease determination of kinetic parameters by the sequential-jump method. Biochemistry. 31:1992;1483-1491
-
(1992)
Biochemistry
, vol.31
, pp. 1483-1491
-
-
Chen, H.M.1
Markin, V.S.2
Tsong, T.Y.3
-
7
-
-
0025982146
-
Molten globule intermediates and protein folding
-
Christensen H., Pain R.H. Molten globule intermediates and protein folding. Eur. Biophys. J. 19:1991;221-229
-
(1991)
Eur. Biophys. J.
, vol.19
, pp. 221-229
-
-
Christensen, H.1
Pain, R.H.2
-
8
-
-
0021759423
-
Use of high-speed size-exclusion chromatography for the study of protein folding and stability
-
Corbett R.J.T., Roche R.S. Use of high-speed size-exclusion chromatography for the study of protein folding and stability. Biochemistry. 23:1984;1888-1894
-
(1984)
Biochemistry
, vol.23
, pp. 1888-1894
-
-
Corbett, R.J.T.1
Roche, R.S.2
-
9
-
-
1842298212
-
From Levinthal to pathways to funnels
-
Dill K.A., Chan H.S. From Levinthal to pathways to funnels. Nature Struct. Biol. 4:1997;10-19
-
(1997)
Nature Struct. Biol.
, vol.4
, pp. 10-19
-
-
Dill, K.A.1
Chan, H.S.2
-
10
-
-
0001931668
-
Unfolded proteins, compact states and molten globules
-
Dobson C.M. Unfolded proteins, compact states and molten globules. Curr. Opin. Struct. Biol. 2:1992;6-12
-
(1992)
Curr. Opin. Struct. Biol.
, vol.2
, pp. 6-12
-
-
Dobson, C.M.1
-
11
-
-
0029562577
-
Partially folded states of proteins: Characterization by X-ray scattering
-
Doniach S., Bascle J., Garel T., Orland H. Partially folded states of proteins characterization by X-ray scattering. J. Mol. Biol. 254:1995;960-967
-
(1995)
J. Mol. Biol.
, vol.254
, pp. 960-967
-
-
Doniach, S.1
Bascle, J.2
Garel, T.3
Orland, H.4
-
12
-
-
0019593952
-
Fluorescence quenching studies with proteins
-
Eftink M.R., Ghiron C.A. Fluorescence quenching studies with proteins. Anal. Biochem. 114:1981;199-227
-
(1981)
Anal. Biochem.
, vol.114
, pp. 199-227
-
-
Eftink, M.R.1
Ghiron, C.A.2
-
13
-
-
0027301270
-
Evidence of an associative intermediate on the myoglobin refolding pathway
-
Eliezer D., Chiba K., Tsuruta H., Doniach S., Hodgson K.O., Kihara H. Evidence of an associative intermediate on the myoglobin refolding pathway. Biophys. J. 65:1993;912-917
-
(1993)
Biophys. J.
, vol.65
, pp. 912-917
-
-
Eliezer, D.1
Chiba, K.2
Tsuruta, H.3
Doniach, S.4
Hodgson, K.O.5
Kihara, H.6
-
15
-
-
0029157429
-
Compact intermediate states in protein folding
-
Fink A.L. Compact intermediate states in protein folding. Annu. Rev. Biophys. Biomol. Struct. 24:1995;495-522
-
(1995)
Annu. Rev. Biophys. Biomol. Struct.
, vol.24
, pp. 495-522
-
-
Fink, A.L.1
-
16
-
-
0027241814
-
Characterization of the stable, acid-induced, molten globule-like state of staphylococcal nuclease
-
Fink A.L., Calciano L.J., Goto Y., Nishimura M., Swedberg S.A. Characterization of the stable, acid-induced, molten globule-like state of staphylococcal nuclease. Protein Sci. 2:1993;1155-1160
-
(1993)
Protein Sci.
, vol.2
, pp. 1155-1160
-
-
Fink, A.L.1
Calciano, L.J.2
Goto, Y.3
Nishimura, M.4
Swedberg, S.A.5
-
17
-
-
0027995384
-
Classification of acid denaturation of proteins: Intermediates and unfolded states
-
Fink A.L., Calciano L.J., Goto Y., Kurotsu T., Palleros D.R. Classification of acid denaturation of proteins intermediates and unfolded states. Biochemistry. 33:1994;12504-12511
-
(1994)
Biochemistry
, vol.33
, pp. 12504-12511
-
-
Fink, A.L.1
Calciano, L.J.2
Goto, Y.3
Kurotsu, T.4
Palleros, D.R.5
-
18
-
-
0031933289
-
Discrete intermediates vs. molten globule models of protein folding: Characterization of partially folded intermediates of apomyoglobin
-
Fink A.L., Seshadri S., Oberg K.A. Discrete intermediates vs. molten globule models of protein folding Characterization of partially folded intermediates of apomyoglobin. Folding Design. 3:1997;19-25
-
(1997)
Folding Design
, vol.3
, pp. 19-25
-
-
Fink, A.L.1
Seshadri, S.2
Oberg, K.A.3
-
19
-
-
0031585990
-
Characterization of long-range structure in the denatured state of staphylococcal nuclease. 1. paramagnetic relaxation enhancement by nitroxide spin labels
-
Gillespie J.R., Shortle D. Characterization of long-range structure in the denatured state of staphylococcal nuclease. 1. paramagnetic relaxation enhancement by nitroxide spin labels. J. Mol. Biol. 268:1997;158-169
-
(1997)
J. Mol. Biol.
, vol.268
, pp. 158-169
-
-
Gillespie, J.R.1
Shortle, D.2
-
20
-
-
0031585992
-
Characterization of long-range structure in the denatured state of staphylococcal nuclease. 2. distance restraints from paramagnetic relaxation and calculation of an ensemble of structures
-
Gillespie J.R., Shortle D. Characterization of long-range structure in the denatured state of staphylococcal nuclease. 2. distance restraints from paramagnetic relaxation and calculation of an ensemble of structures. J. Mol. Biol. 268:1997;170-184
-
(1997)
J. Mol. Biol.
, vol.268
, pp. 170-184
-
-
Gillespie, J.R.1
Shortle, D.2
-
22
-
-
0024963570
-
Conformational states of β-lactamase: Molten globule states at acidic and alkaline pH with high salt
-
Goto Y., Fink A.L. Conformational states of β-lactamase molten globule states at acidic and alkaline pH with high salt. Biochemistry. 28:1989;945-952
-
(1989)
Biochemistry
, vol.28
, pp. 945-952
-
-
Goto, Y.1
Fink, A.L.2
-
24
-
-
0025195499
-
Mechanism of acid-induced folding of proteins
-
Goto Y., Takahashi N., Fink A.L. Mechanism of acid-induced folding of proteins. Biochemistry. 29:1990;3480-3488
-
(1990)
Biochemistry
, vol.29
, pp. 3480-3488
-
-
Goto, Y.1
Takahashi, N.2
Fink, A.L.3
-
25
-
-
0029740071
-
Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein
-
Hamada D., Segawa S., Goto Y. Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein. Nature Struct. Biol. 3:1996;868-873
-
(1996)
Nature Struct. Biol.
, vol.3
, pp. 868-873
-
-
Hamada, D.1
Segawa, S.2
Goto, Y.3
-
26
-
-
0029151158
-
Submillisecond folding of monomeric lambda repressor
-
Huang G.S., Oas T.G. Submillisecond folding of monomeric lambda repressor. Proc. Nat. Acad. Sci. USA. 92:1995;6878-6882
-
(1995)
Proc. Nat. Acad. Sci. USA
, vol.92
, pp. 6878-6882
-
-
Huang, G.S.1
Oas, T.G.2
-
27
-
-
0025186451
-
Structural characterization of a partly folded apomyoglobin intermediate
-
Hughson F.M., Wright P.E., Baldwin R.L. Structural characterization of a partly folded apomyoglobin intermediate. Science. 249:1990;1544-1548
-
(1990)
Science
, vol.249
, pp. 1544-1548
-
-
Hughson, F.M.1
Wright, P.E.2
Baldwin, R.L.3
-
28
-
-
0023041667
-
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
-
Ikeguchi M., Kuwajima K., Mitani M., Sugai S. 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. Biochemistry. 25:1986;6965-6972
-
(1986)
Biochemistry
, vol.25
, pp. 6965-6972
-
-
Ikeguchi, M.1
Kuwajima, K.2
Mitani, M.3
Sugai, S.4
-
29
-
-
0027749370
-
Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
-
Jennings P.A., Wright P.E. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science. 262:1993;892-896
-
(1993)
Science
, vol.262
, pp. 892-896
-
-
Jennings, P.A.1
Wright, P.E.2
-
30
-
-
0028832610
-
Kinetic folding and unfolding of staphylococcal nuclease and its six mutants studied by stopped-flow circular dichroism
-
Kalnin N.N., Kuwajima K. Kinetic folding and unfolding of staphylococcal nuclease and its six mutants studied by stopped-flow circular dichroism. Proteins: Struct. Funct. Genet. 23:1995;163-176
-
(1995)
Proteins: Struct. Funct. Genet.
, vol.23
, pp. 163-176
-
-
Kalnin, N.N.1
Kuwajima, K.2
-
31
-
-
0000739195
-
Melittin binding causes a large calcium-dependent conformational change in calmodulin
-
Kataoka M., Head J.F., Seaton B.A., Engelman D.M. Melittin binding causes a large calcium-dependent conformational change in calmodulin. Proc. Natl Acad. Sci. USA. 86:1989;6944-6948
-
(1989)
Proc. Natl Acad. Sci. USA
, vol.86
, pp. 6944-6948
-
-
Kataoka, M.1
Head, J.F.2
Seaton, B.A.3
Engelman, D.M.4
-
32
-
-
0027400842
-
Molten globule of cytochrome c studied by small angle X-ray scattering
-
Kataoka M., Hagihara Y., Mihara K., Goto Y. Molten globule of cytochrome c studied by small angle X-ray scattering. J. Mol. Biol. 229:1993;591-596
-
(1993)
J. Mol. Biol.
, vol.229
, pp. 591-596
-
-
Kataoka, M.1
Hagihara, Y.2
Mihara, K.3
Goto, Y.4
-
33
-
-
0025345415
-
Intermediates in the folding reactions of small proteins
-
Kim P.S., Baldwin R.L. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59:1990;631-660
-
(1990)
Annu. Rev. Biochem.
, vol.59
, pp. 631-660
-
-
Kim, P.S.1
Baldwin, R.L.2
-
34
-
-
0024417964
-
The molten globule as a clue for understanding the folding and cooperativity of globular proteins structure
-
Kuwajima K. The molten globule as a clue for understanding the folding and cooperativity of globular proteins structure. Proteins: Struct. Funct. Genet. 6:1989;87-103
-
(1989)
Proteins: Struct. Funct. Genet.
, vol.6
, pp. 87-103
-
-
Kuwajima, K.1
-
36
-
-
0029014386
-
Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway
-
Loh S.N., Kay M.S., Baldwin R.L. Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway. Proc. Nat. Acad. Sci. USA. 92:1995;5446-5450
-
(1995)
Proc. Nat. Acad. Sci. USA
, vol.92
, pp. 5446-5450
-
-
Loh, S.N.1
Kay, M.S.2
Baldwin, R.L.3
-
37
-
-
0002343673
-
Measuring the conformational stability of a protein
-
T.E. Creighton. Oxford, New York, Tokyo: IRL Press at Oxford University Press
-
Pace C.N., Shirley B.A., Thomson J.A. Measuring the conformational stability of a protein. Creighton T.E. Protein Structure. A Practical Approach. 1989;311-330 IRL Press at Oxford University Press, Oxford, New York, Tokyo
-
(1989)
Protein Structure. a Practical Approach
, pp. 311-330
-
-
Pace, C.N.1
Shirley, B.A.2
Thomson, J.A.3
-
38
-
-
0027322906
-
Three-state denaturation of DnaK induced by guanidine hydrochloride. Evidence for an expandable intermediate
-
Palleros D.R., Shi L., Reid K.L., Fink A.L. Three-state denaturation of DnaK induced by guanidine hydrochloride. Evidence for an expandable intermediate. Biochemistry. 32:1993;4314-4321
-
(1993)
Biochemistry
, vol.32
, pp. 4314-4321
-
-
Palleros, D.R.1
Shi, L.2
Reid, K.L.3
Fink, A.L.4
-
39
-
-
0015920746
-
Stages in the mechanism of self-organization of protein molecules
-
Ptitsyn O.B. Stages in the mechanism of self-organization of protein molecules. Dokl. Acad. Nauk SSSR. 210:1973;1213-1215
-
(1973)
Dokl. Acad. Nauk SSSR
, vol.210
, pp. 1213-1215
-
-
Ptitsyn, O.B.1
-
40
-
-
0023626273
-
Protein folding: Hypotheses and experiments
-
Ptitsyn O.B. Protein folding hypotheses and experiments. J. Protein Chem. 6:1987;273-293
-
(1987)
J. Protein Chem.
, vol.6
, pp. 273-293
-
-
Ptitsyn, O.B.1
-
41
-
-
0002940127
-
The molten globule state
-
T.E. Creighton. New York: W. H. Freeman and Company
-
Ptitsyn O.B. The molten globule state. Creighton T.E. Protein Folding. 1992;243-300 W. H. Freeman and Company, New York
-
(1992)
Protein Folding
, pp. 243-300
-
-
Ptitsyn, O.B.1
-
42
-
-
0029124248
-
Molten globule and protein folding
-
Ptitsyn O.B. Molten globule and protein folding. Advan. Protein Chem. 47:1995;83-229
-
(1995)
Advan. Protein Chem.
, vol.47
, pp. 83-229
-
-
Ptitsyn, O.B.1
-
43
-
-
0030010408
-
Intermediate states in protein folding
-
Privalov P.L. Intermediate states in protein folding. J. Mol. Biol. 258:1996;707-725
-
(1996)
J. Mol. Biol.
, vol.258
, pp. 707-725
-
-
Privalov, P.L.1
-
44
-
-
0024659268
-
Two-stage equilibrium unfolding of carbonic anhydrase B by strong denaturants
-
Rodionova N.A., Semisotnov G.V., Kutyshenko V.P., Uversky V.N., Bolotina I.A., Bychkova V.E., Ptitsyn O.B. Two-stage equilibrium unfolding of carbonic anhydrase B by strong denaturants. Mol. Biol. (Moscow). 23:1989;683-692
-
(1989)
Mol. Biol. (Moscow)
, vol.23
, pp. 683-692
-
-
Rodionova, N.A.1
Semisotnov, G.V.2
Kutyshenko, V.P.3
Uversky, V.N.4
Bolotina, I.A.5
Bychkova, V.E.6
Ptitsyn, O.B.7
-
46
-
-
0023657937
-
Sequential mechanism of refolding of carbonic anhydrase B
-
Semisotnov G.V., Rodionova N.A., Kutyshenko V.P., Ebert B., Blank J., Ptitsyn O.B. Sequential mechanism of refolding of carbonic anhydrase B. FEBS Letters. 224:1987;9-13
-
(1987)
FEBS Letters
, vol.224
, pp. 9-13
-
-
Semisotnov, G.V.1
Rodionova, N.A.2
Kutyshenko, V.P.3
Ebert, B.4
Blank, J.5
Ptitsyn, O.B.6
-
47
-
-
0026096545
-
Study of the molten globule intermediate state by a hydrophobic fluorescent probe
-
Semisotnov G.V., Rodionova N.A., Razgulyaev O.I., Uversky V.N., Gripas A.F., Gilmanshin R.I. Study of the molten globule intermediate state by a hydrophobic fluorescent probe. Biopolymers. 31:1991;119-128
-
(1991)
Biopolymers
, vol.31
, pp. 119-128
-
-
Semisotnov, G.V.1
Rodionova, N.A.2
Razgulyaev, O.I.3
Uversky, V.N.4
Gripas, A.F.5
Gilmanshin, R.I.6
-
48
-
-
0030569018
-
Protein globularization during folding. a study by synchrotron small-angle X-ray scattering
-
Semisotnov G.V., Kihara H., Kotova N.V., Kimura K., Amemiya Y., Wakabayashi K., Serdyuk I.N., Timchenko A.A., Chiba K., Nikaido K., Ikura T., Kuwajima K. Protein globularization during folding. A study by synchrotron small-angle X-ray scattering. J. Mol. Biol. 262:1996;559-574
-
(1996)
J. Mol. Biol.
, vol.262
, pp. 559-574
-
-
Semisotnov, G.V.1
Kihara, H.2
Kotova, N.V.3
Kimura, K.4
Amemiya, Y.5
Wakabayashi, K.6
Serdyuk, I.N.7
Timchenko, A.A.8
Chiba, K.9
Nikaido, K.10
Ikura, T.11
Kuwajima, K.12
-
50
-
-
0013800421
-
The interaction of naphthalene dye with apomyoglobin and apohemoglobin: A fluorescent probe of non-polar binding sites
-
Stryer L. The interaction of naphthalene dye with apomyoglobin and apohemoglobin A fluorescent probe of non-polar binding sites. J. Mol. Biol. 13:1965;482-495
-
(1965)
J. Mol. Biol.
, vol.13
, pp. 482-495
-
-
Stryer, L.1
-
51
-
-
0014354873
-
Fluorescence spectroscopy of proteins
-
Stryer L. Fluorescence spectroscopy of proteins. Science. 162:1968;526-540
-
(1968)
Science
, vol.162
, pp. 526-540
-
-
Stryer, L.1
-
52
-
-
0025911196
-
Folding of staphylococcal nuclease a studied by equilibrium and kinetic circular dichroism spectra
-
Sugawara T., Kuwajima K., Sugai S. Folding of staphylococcal nuclease A studied by equilibrium and kinetic circular dichroism spectra. Biochemisty. 30:1991;2698-2706
-
(1991)
Biochemisty
, vol.30
, pp. 2698-2706
-
-
Sugawara, T.1
Kuwajima, K.2
Sugai, S.3
-
53
-
-
0014364651
-
Protein denaturation
-
Tanford C. Protein denaturation. Advan. Protein Chem. 23:1968;121-282
-
(1968)
Advan. Protein Chem.
, vol.23
, pp. 121-282
-
-
Tanford, C.1
-
54
-
-
0027733616
-
Use of fast-protein size-exclusion chromatography to study the unfolding of proteins which denature through the molten globule
-
Uversky V.N. Use of fast-protein size-exclusion chromatography to study the unfolding of proteins which denature through the molten globule. Biochemistry. 32:1993;13288-13298
-
(1993)
Biochemistry
, vol.32
, pp. 13288-13298
-
-
Uversky, V.N.1
-
55
-
-
0028311781
-
Gel-permeation chromatography as a unique instrument for quantitative and qualitative analysis of protein denaturation and unfolding
-
Uversky V.N. Gel-permeation chromatography as a unique instrument for quantitative and qualitative analysis of protein denaturation and unfolding. Int. J. Bio-Chromatog. 1:1994;103-114
-
(1994)
Int. J. Bio-Chromatog.
, vol.1
, pp. 103-114
-
-
Uversky, V.N.1
-
56
-
-
0028176911
-
"partly folded" state, a new equilibrium state of protein molecules: Four-state guanidinium chloride-induced unfolding of β-lactamase at low temperatures
-
Uversky V.N., Ptitsyn O.B. "Partly folded" state, a new equilibrium state of protein molecules four-state guanidinium chloride-induced unfolding of β-lactamase at low temperatures. Biochemistry. 33:1994;2782-2791
-
(1994)
Biochemistry
, vol.33
, pp. 2782-2791
-
-
Uversky, V.N.1
Ptitsyn, O.B.2
-
57
-
-
0029924194
-
Further evidence on the equilibrium "pre-molten globule state": Four-state GdmCl-induced unfolding of carbonic anhydrase at low temperature
-
Uversky V.N., Ptitsyn O.B. Further evidence on the equilibrium "pre-molten globule state" Four-state GdmCl-induced unfolding of carbonic anhydrase at low temperature. J. Mol. Biol. 255:1996;215-228
-
(1996)
J. Mol. Biol.
, vol.255
, pp. 215-228
-
-
Uversky, V.N.1
Ptitsyn, O.B.2
-
58
-
-
0040495009
-
Unfolding of the molten globule state by strong denaturants follows the "all-or-none" principles
-
Uversky V.N., Semisotnov G.V., Ptitsyn O.B. Unfolding of the molten globule state by strong denaturants follows the "all-or-none" principles. Biophysics (Moscow). 38:1993;31-39
-
(1993)
Biophysics (Moscow)
, vol.38
, pp. 31-39
-
-
Uversky, V.N.1
Semisotnov, G.V.2
Ptitsyn, O.B.3
-
60
-
-
0031010618
-
Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease
-
Wallenhorst W.F., Green S.M., Roder H. Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease. Biochemistry. 36:1997;5795-5805
-
(1997)
Biochemistry
, vol.36
, pp. 5795-5805
-
-
Wallenhorst, W.F.1
Green, S.M.2
Roder, H.3
-
61
-
-
0030628174
-
Residual helical and turn structure in the denatured state of staphylococcal nuclease: Analysis of peptide fragments
-
Wang Y., Shortle D. Residual helical and turn structure in the denatured state of staphylococcal nuclease analysis of peptide fragments. Folding Design. 2:1997;93-100
-
(1997)
Folding Design
, vol.2
, pp. 93-100
-
-
Wang, Y.1
Shortle, D.2
-
62
-
-
0030592173
-
Sequential unfolding of adenylate kinase during denaturation by guanidine hydrochloride
-
Zhang Y.-L., Zhou J.-M., Tsou C.-L. Sequential unfolding of adenylate kinase during denaturation by guanidine hydrochloride. Biochem. Biophys. Acta. 1295:1996;239-244
-
(1996)
Biochem. Biophys. Acta.
, vol.1295
, pp. 239-244
-
-
Zhang, Y.-L.1
Zhou, J.-M.2
Tsou, C.-L.3
|