-
1
-
-
0030348041
-
Rapid formation of a molten globule intermediate in refolding of α-lactalbumin
-
Arai M, Kuwajima K. 1996. Rapid formation of a molten globule intermediate in refolding of α-lactalbumin. Folding & Design 1:275-287.
-
(1996)
Folding & Design
, vol.1
, pp. 275-287
-
-
Arai, M.1
Kuwajima, K.2
-
2
-
-
0030347877
-
On-pathway versus off-pathway folding intermediate
-
Baldwin RL. 1996. On-pathway versus off-pathway folding intermediate. Folding & Design 1:R1-R8.
-
(1996)
Folding & Design
, vol.1
-
-
Baldwin, R.L.1
-
3
-
-
0022343373
-
2 subunit of Escherichia coli tryptophan synthase
-
2 subunit of Escherichia coli tryptophan synthase. J Mol Biol 182:597-606.
-
(1985)
J Mol Biol
, vol.182
, pp. 597-606
-
-
Blond, S.1
Goldberg, M.E.2
-
4
-
-
0024962376
-
Equilibrium dissociation and unfolding of the Arc repressor dimer
-
Bowie JU, Sauer RT. 1989. Equilibrium dissociation and unfolding of the Arc repressor dimer. Biochemistry 28:7139-7143.
-
(1989)
Biochemistry
, vol.28
, pp. 7139-7143
-
-
Bowie, J.U.1
Sauer, R.T.2
-
5
-
-
0028829823
-
Reversible dissociation and unfolding of dimeric creatine kinase isoenzyme MM in guanidine hydrochloride and urea
-
Couthon F, Clottes E, Ebel C, Vial C. 1995. Reversible dissociation and unfolding of dimeric creatine kinase isoenzyme MM in guanidine hydrochloride and urea. Eur J Biochem 234:160-170.
-
(1995)
Eur J Biochem
, vol.234
, pp. 160-170
-
-
Couthon, F.1
Clottes, E.2
Ebel, C.3
Vial, C.4
-
6
-
-
0019321480
-
Further evidence for nonsymmetric subunit association and intersubunit cooperativity in creatine kinase
-
Degani C, Degani Y. 1980. Further evidence for nonsymmetric subunit association and intersubunit cooperativity in creatine kinase. J Biol Chem 255: 8221-8228.
-
(1980)
J Biol Chem
, vol.255
, pp. 8221-8228
-
-
Degani, C.1
Degani, Y.2
-
7
-
-
0022423920
-
Theory for the folding and stability of globular proteins
-
Dill KA. 1985. Theory for the folding and stability of globular proteins. Biochemistry 24:1501-1509.
-
(1985)
Biochemistry
, vol.24
, pp. 1501-1509
-
-
Dill, K.A.1
-
8
-
-
0025370815
-
Dominant forces in protein folding
-
Dill KA. 1990. Dominant forces in protein folding. Biochemistry 29:7133-7155.
-
(1990)
Biochemistry
, vol.29
, pp. 7133-7155
-
-
Dill, K.A.1
-
9
-
-
0028929556
-
Principles of protein folding: A perspective from simple exact models
-
Dill KA, Bromberg S, Yue K, Fiebig KM, Yee DP, Thomas PD, Chan HS. 1995. Principles of protein folding: A perspective from simple exact models. Protein Sci 4:561-602.
-
(1995)
Protein Sci
, vol.4
, pp. 561-602
-
-
Dill, K.A.1
Bromberg, S.2
Yue, K.3
Fiebig, K.M.4
Yee, D.P.5
Thomas, P.D.6
Chan, H.S.7
-
10
-
-
0027958069
-
The use of fluorescence methods to monitor unfolding transitions in proteins
-
Eftink MR. 1994. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys J 66:482-501.
-
(1994)
Biophys J
, vol.66
, pp. 482-501
-
-
Eftink, M.R.1
-
11
-
-
3042934967
-
Tissue sulfhydryl groups
-
Ellman GL. 1959. Tissue sulfhydryl groups. Arch Biochem Biophys 82:70-77.
-
(1959)
Arch Biochem Biophys
, vol.82
, pp. 70-77
-
-
Ellman, G.L.1
-
12
-
-
0029115374
-
Kinetics of interaction of partially folded proteins with a hydrophobic dye: Evidence that molten globule character is maximal in early folding intermediates
-
Engelhard M, Evans PA. 1995. Kinetics of interaction of partially folded proteins with a hydrophobic dye: Evidence that molten globule character is maximal in early folding intermediates. Protein Sci 4:1553-1562.
-
(1995)
Protein Sci
, vol.4
, pp. 1553-1562
-
-
Engelhard, M.1
Evans, P.A.2
-
13
-
-
0028082357
-
Probing the structure of folding intermediates
-
Evans PA, Radford SE. 1994. Probing the structure of folding intermediates. Curr Opin Struct Biol 4:100-106.
-
(1994)
Curr Opin Struct Biol
, vol.4
, pp. 100-106
-
-
Evans, P.A.1
Radford, S.E.2
-
14
-
-
0028856785
-
Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
-
Fersht AR. 1995. Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications. Proc Natl Acad Sci USA 92:10869-10873.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 10869-10873
-
-
Fersht, A.R.1
-
15
-
-
0029194798
-
Compact intermediate states in protein folding
-
Biswas BB, Roy S, eds. New York: Plenum Press
-
Fink AL. 1995. Compact intermediate states in protein folding. In: Biswas BB, Roy S, eds. Subcellular biochemistry. Volume 24. Proteins: Structure, function, and engineering. New York: Plenum Press, pp 27-53.
-
(1995)
Subcellular Biochemistry. Volume 24. Proteins: Structure, Function, and Engineering
, vol.24
, pp. 27-53
-
-
Fink, A.L.1
-
17
-
-
0030925611
-
Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressor
-
Gloss LM, Matthews CR. 1997. Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressor. Biochemistry 36:5612-5623.
-
(1997)
Biochemistry
, vol.36
, pp. 5612-5623
-
-
Gloss, L.M.1
Matthews, C.R.2
-
18
-
-
0029143228
-
Multiple-state equilibrium unfolding of guanidino kinase
-
Gross M, Lustig A, Wallimann T, Furter R. 1995. Multiple-state equilibrium unfolding of guanidino kinase. Biochemistry 34:10350-10357.
-
(1995)
Biochemistry
, vol.34
, pp. 10350-10357
-
-
Gross, M.1
Lustig, A.2
Wallimann, T.3
Furter, R.4
-
19
-
-
0025125731
-
Reversible dissociation and unfolding of aspartate aminotransferase from Escherichia coli: Characterization of a monomeric intermediate
-
Herold M, Kirschner K. 1990. Reversible dissociation and unfolding of aspartate aminotransferase from Escherichia coli: Characterization of a monomeric intermediate. Biochemistry 29:1907-1913
-
(1990)
Biochemistry
, vol.29
, pp. 1907-1913
-
-
Herold, M.1
Kirschner, K.2
-
20
-
-
0018266792
-
Expression of functionality of α-chymotrypsin. Effects of guanidine hydrochloride and urea in the onset of denaturation
-
Hibbard LS, Tulinsky A. 1978. Expression of functionality of α-chymotrypsin. Effects of guanidine hydrochloride and urea in the onset of denaturation. Biochemistry 17:5460-5468.
-
(1978)
Biochemistry
, vol.17
, pp. 5460-5468
-
-
Hibbard, L.S.1
Tulinsky, A.2
-
21
-
-
0022702283
-
2+-induced alteration in the unfolding behavior of α-lactalbumin
-
2+-induced alteration in the unfolding behavior of α-lactalbumin. J Biochem 99:1191-1201.
-
(1986)
J Biochem
, vol.99
, pp. 1191-1201
-
-
Ikeguchi, M.1
Kuwajima, K.2
Sugai, S.3
-
22
-
-
0025876740
-
Protein folding: Local structures, domains, subunits, and assemblies
-
Jeanicke R. 1991. Protein folding: Local structures, domains, subunits, and assemblies. Biochemistry 30:3147-3161.
-
(1991)
Biochemistry
, vol.30
, pp. 3147-3161
-
-
Jeanicke, R.1
-
23
-
-
0029981924
-
Packing interactions in the apomyoglobin folding intermediate
-
Kay MS, Baldwin RL. 1996. Packing interactions in the apomyoglobin folding intermediate. Nature Struct Biology 3:439-445.
-
(1996)
Nature Struct Biology
, vol.3
, pp. 439-445
-
-
Kay, M.S.1
Baldwin, R.L.2
-
24
-
-
0025345415
-
Intermediates in the folding reactions of small proteins
-
Kim PS, Baldwin RL. 1990. Intermediates in the folding reactions of small proteins. Ann Rev Biochem 59:631-660.
-
(1990)
Ann Rev Biochem
, vol.59
, pp. 631-660
-
-
Kim, P.S.1
Baldwin, R.L.2
-
25
-
-
0024417964
-
The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
-
Kuwajima K. 1989. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins Struct Funct Genet 6:87-103.
-
(1989)
Proteins Struct Funct Genet
, vol.6
, pp. 87-103
-
-
Kuwajima, K.1
-
26
-
-
0030059690
-
The molten globule state of α-lactalbumin
-
Kuwajima K. 1996. The molten globule state of α-lactalbumin. FASEB J 10:102-109.
-
(1996)
FASEB J
, vol.10
, pp. 102-109
-
-
Kuwajima, K.1
-
27
-
-
0028866093
-
Spin-labeling probe on conformational change at the active site of creatine kinase during denaturation by guanidine hydrochloride
-
Liu ZJ, Zhou JM. 1995. Spin-labeling probe on conformational change at the active site of creatine kinase during denaturation by guanidine hydrochloride. Biochim Biophys Acta 1255:63-68.
-
(1995)
Biochim Biophys Acta
, vol.1255
, pp. 63-68
-
-
Liu, Z.J.1
Zhou, J.M.2
-
28
-
-
0000636916
-
Studies on adenosine triphosphate transphosphorylases III. Inhibition reactions
-
Mahowald TA, Noltmann EA, Kuby SA. 1962. Studies on adenosine triphosphate transphosphorylases III. Inhibition reactions. J Biol Chem 237:1535-1548.
-
(1962)
J Biol Chem
, vol.237
, pp. 1535-1548
-
-
Mahowald, T.A.1
Noltmann, E.A.2
Kuby, S.A.3
-
29
-
-
0026416043
-
Chaperonin-mediated protein folding at the surface of groEL through a molten globule-like intermediate
-
Martin J, Langer T, Boteva R, Schramel A, Horwich AL, Hartl F-U. 1991. Chaperonin-mediated protein folding at the surface of groEL through a molten globule-like intermediate. Nature 352:36-42.
-
(1991)
Nature
, vol.352
, pp. 36-42
-
-
Martin, J.1
Langer, T.2
Boteva, R.3
Schramel, A.4
Horwich, A.L.5
Hartl, F.-U.6
-
30
-
-
0027313673
-
Pathways of protein foldings
-
Matthews CR. 1993. Pathways of protein foldings. Annu Rev Biochem 62:653-683.
-
(1993)
Annu Rev Biochem
, vol.62
, pp. 653-683
-
-
Matthews, C.R.1
-
31
-
-
0015976865
-
The interaction of 8-anilino-1-naphthalenesulfonate with creatine kinase
-
McLaughlin AC. 1974. The interaction of 8-anilino-1-naphthalenesulfonate with creatine kinase. J Biol Chem 249:1445-1452.
-
(1974)
J Biol Chem
, vol.249
, pp. 1445-1452
-
-
McLaughlin, A.C.1
-
32
-
-
0025356710
-
Monoclonal antibody studies suggest a catalytic site at the interface between domains in creatine kinase
-
Morris GE, Cartwright AJ. 1990. Monoclonal antibody studies suggest a catalytic site at the interface between domains in creatine kinase. Biochim Biophys Acta 1039:318-322.
-
(1990)
Biochim Biophys Acta
, vol.1039
, pp. 318-322
-
-
Morris, G.E.1
Cartwright, A.J.2
-
33
-
-
0028606077
-
Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturation
-
Neet KE, Timm DE. 1994. Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturation. Protein Sci 4:2167-2174.
-
(1994)
Protein Sci
, vol.4
, pp. 2167-2174
-
-
Neet, K.E.1
Timm, D.E.2
-
35
-
-
0027787520
-
Further examination of the intermediate state in the denaturation of the tryptophan synthase α-subunit: Evidence that the equilibrium denaturation intermediate is a molten globule
-
Ogasahara K, Matsushita E, Yutani K. 1993. Further examination of the intermediate state in the denaturation of the tryptophan synthase α-subunit: Evidence that the equilibrium denaturation intermediate is a molten globule. J Mol Biol 234:1197-1206.
-
(1993)
J Mol Biol
, vol.234
, pp. 1197-1206
-
-
Ogasahara, K.1
Matsushita, E.2
Yutani, K.3
-
36
-
-
0028258789
-
Unfolding-refolding kinetics of the tryptophan synthase α-subunit by CD and fluorescence measurements
-
Ogasahara K, Yutani K. 1994. Unfolding-refolding kinetics of the tryptophan synthase α-subunit by CD and fluorescence measurements. J Mol Biol 236:1227-1240.
-
(1994)
J Mol Biol
, vol.236
, pp. 1227-1240
-
-
Ogasahara, K.1
Yutani, K.2
-
37
-
-
0022555885
-
Determination and analysis of urea and guanidine hydrochloride denaturation curves
-
Pace CN. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 131:266-280.
-
(1986)
Methods Enzymol
, vol.131
, pp. 266-280
-
-
Pace, C.N.1
-
38
-
-
0025271463
-
pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease a and ribonuclease T1
-
Pace CN, Laurents DV, Thomson JA. 1990. pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1. Biochemistry 29:2564-2572.
-
(1990)
Biochemistry
, vol.29
, pp. 2564-2572
-
-
Pace, C.N.1
Laurents, D.V.2
Thomson, J.A.3
-
39
-
-
0002101049
-
Assembly of multi-subunit structures
-
Pain RH, ed. New York: Oxford University Press Inc.
-
Price NC. 1994. Assembly of multi-subunit structures. In: Pain RH, ed. Mechanisms of protein folding. New York: Oxford University Press Inc. pp 160-193.
-
(1994)
Mechanisms of Protein Folding
, pp. 160-193
-
-
Price, N.C.1
-
40
-
-
0023626273
-
Protein folding: Hypotheses and experiments
-
Ptitsyn OB. 1987. Protein folding: Hypotheses and experiments. J Protein Chem 6:273-293.
-
(1987)
J Protein Chem
, vol.6
, pp. 273-293
-
-
Ptitsyn, O.B.1
-
41
-
-
0029124248
-
Molten globule and protein folding
-
Ptitsyn OB. 1995. Molten globule and protein folding. Adv Prot Chem 47:83-229.
-
(1995)
Adv Prot Chem
, vol.47
, pp. 83-229
-
-
Ptitsyn, O.B.1
-
42
-
-
0025212107
-
Evidence for a molten globule state as a general intermediate in protein folding
-
Ptitsyn OB, Pain RH, Semisotnov GV, Zerovnik E, Razgulyaev OI. 1990. Evidence for a molten globule state as a general intermediate in protein folding. FEBS Lett 262:20-24.
-
(1990)
FEBS Lett
, vol.262
, pp. 20-24
-
-
Ptitsyn, O.B.1
Pain, R.H.2
Semisotnov, G.V.3
Zerovnik, E.4
Razgulyaev, O.I.5
-
43
-
-
0021733938
-
Rabbit muscle creatine phosphokinase
-
Putney S, Herlihy W, Royal N, Pang H, Vasken-Aposhian H, Pickering L, Belagaje R, Biemann K, Page D, Kuby S, Schimmel P. 1984. Rabbit muscle creatine phosphokinase. J Biol Chem 259:14317-14320.
-
(1984)
J Biol Chem
, vol.259
, pp. 14317-14320
-
-
Putney, S.1
Herlihy, W.2
Royal, N.3
Pang, H.4
Vasken-Aposhian, H.5
Pickering, L.6
Belagaje, R.7
Biemann, K.8
Page, D.9
Kuby, S.10
Schimmel, P.11
-
44
-
-
0018759627
-
Inhibition of creatine kinase by iodoalkanes: Further appraisal of the essential nature of the reactive thiol group
-
Reddy SRR, Watts DC. 1979. Inhibition of creatine kinase by iodoalkanes: Further appraisal of the essential nature of the reactive thiol group. Biochem Biophys Acta 569:109-113.
-
(1979)
Biochem Biophys Acta
, vol.569
, pp. 109-113
-
-
Reddy, S.R.R.1
Watts, D.C.2
-
45
-
-
0031592933
-
Formation of a denatured dimer limits the thermal stability of Arc repressor
-
Robinson CR, Rentzeperis D, Silva JL, Sauer RT. 1997. Formation of a denatured dimer limits the thermal stability of Arc repressor. J Mol Biol 273:692-700.
-
(1997)
J Mol Biol
, vol.273
, pp. 692-700
-
-
Robinson, C.R.1
Rentzeperis, D.2
Silva, J.L.3
Sauer, R.T.4
-
46
-
-
0002775727
-
Early stages of protein folding
-
Pain RH, ed. New York: Oxford University Press Inc.
-
Roder H, Elöve GA. 1994. Early stages of protein folding. In: Pain RH, ed. Mechanisms of protein folding. New York: Oxford University Press Inc. pp 26-54.
-
(1994)
Mechanisms of Protein Folding
, pp. 26-54
-
-
Roder, H.1
Elöve, G.A.2
-
47
-
-
0026524198
-
An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate
-
Sancho J, Neira JL, Fersht AR. 1992. An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate. J Mol Biol 224:749-758.
-
(1992)
J Mol Biol
, vol.224
, pp. 749-758
-
-
Sancho, J.1
Neira, J.L.2
Fersht, A.R.3
-
48
-
-
0000904331
-
Protein denaturation, Part B. The transition from native to denatured state
-
Tanford C. 1968. Protein denaturation, Part B. The transition from native to denatured state. Adv Protein Chem 23:218-275.
-
(1968)
Adv Protein Chem
, vol.23
, pp. 218-275
-
-
Tanford, C.1
-
49
-
-
0028219924
-
Comparative equilibrium denaturation studies of the neurotrophins: Nerve growth factor, brain-derived neurotrophic factor, neurotrophin 3, and neurotrophin 4/5
-
Timm DE, deHaseth PL, Neet KE. 1994. Comparative equilibrium denaturation studies of the neurotrophins: Nerve growth factor, brain-derived neurotrophic factor, neurotrophin 3, and neurotrophin 4/5. Biochemistry 33:4667-4676.
-
(1994)
Biochemistry
, vol.33
, pp. 4667-4676
-
-
Timm, D.E.1
DeHaseth, P.L.2
Neet, K.E.3
-
50
-
-
0027104286
-
Equilibrium denaturation studies of mouse β-nerve growth factor
-
Timm DE, Neet KE. 1992. Equilibrium denaturation studies of mouse β-nerve growth factor. Protein Sci 1:236-244.
-
(1992)
Protein Sci
, vol.1
, pp. 236-244
-
-
Timm, D.E.1
Neet, K.E.2
-
51
-
-
0023055739
-
Folding of dihydrofolate reductase from Escherichia coli
-
Touchette NA, Perry KM, Matthews CR. 1986. Folding of dihydrofolate reductase from Escherichia coli. Biochemistry 25:5445-5452.
-
(1986)
Biochemistry
, vol.25
, pp. 5445-5452
-
-
Touchette, N.A.1
Perry, K.M.2
Matthews, C.R.3
-
52
-
-
0028807509
-
Inactivation precedes overall molecular conformation changes during enzyme denaturation
-
Tsou CL. 1995. Inactivation precedes overall molecular conformation changes during enzyme denaturation. Biochim Biophys Acta 1253:151-162.
-
(1995)
Biochim Biophys Acta
, vol.1253
, pp. 151-162
-
-
Tsou, C.L.1
-
53
-
-
0029564086
-
Conformational changes of active sites during refolding of urea-denatured creatine kinase
-
Wang ZF, Yang Y, Zhou HM. 1995. Conformational changes of active sites during refolding of urea-denatured creatine kinase. Biochimie 77:953-956.
-
(1995)
Biochimie
, vol.77
, pp. 953-956
-
-
Wang, Z.F.1
Yang, Y.2
Zhou, H.M.3
-
54
-
-
0028960492
-
How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of Ribonuclease a stability
-
Yao M, Bolen DW. 1995. How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of Ribonuclease A stability. Biochemistry 34:3771-3781.
-
(1995)
Biochemistry
, vol.34
, pp. 3771-3781
-
-
Yao, M.1
Bolen, D.W.2
-
55
-
-
0020212384
-
Conformational changes of creatine kinase during guanidine hydrochloride denaturation
-
Yao QZ, Hou LX, Zhou HM, Tsou CL. 1982a. Conformational changes of creatine kinase during guanidine hydrochloride denaturation. Sci Sin 25B:1186-1193.
-
(1982)
Sci Sin
, vol.25 B
, pp. 1186-1193
-
-
Yao, Q.Z.1
Hou, L.X.2
Zhou, H.M.3
Tsou, C.L.4
-
56
-
-
0008886110
-
The rapid inactivation and slow conformational changes of creatine kinase during guanidine and urea denaturation
-
Bradshaw RA. Tang J, eds. New York: Academic Press, Inc.
-
Yao QZ, Tsou CL. 1985. The rapid inactivation and slow conformational changes of creatine kinase during guanidine and urea denaturation. In: Bradshaw RA. Tang J, eds. Molecule architecture of proteins and enzymes. New York: Academic Press, Inc. pp 99-115.
-
(1985)
Molecule Architecture of Proteins and Enzymes
, pp. 99-115
-
-
Yao, Q.Z.1
Tsou, C.L.2
-
57
-
-
0020344240
-
A comparison of denaturation and inactivation rates of creatine kinase in guanidine solutions
-
Yao QZ, Zhou HM, Hou LX, Tsou CL. 1982b. A comparison of denaturation and inactivation rates of creatine kinase in guanidine solutions. Sci Sin 25B:1296-1302.
-
(1982)
Sci Sin
, vol.25 B
, pp. 1296-1302
-
-
Yao, Q.Z.1
Zhou, H.M.2
Hou, L.X.3
Tsou, C.L.4
-
58
-
-
0032577216
-
Equilibrium intermediates in the unfolding pathway of creative kinase
-
Zhang YL, Fan YX, Huang GC, Zhou JX, Zhou JM. 1998. Equilibrium intermediates in the unfolding pathway of creative kinase. Biochem Biophys Res Comm 246:609-612.
-
(1998)
Biochem Biophys Res Comm
, vol.246
, pp. 609-612
-
-
Zhang, Y.L.1
Fan, Y.X.2
Huang, G.C.3
Zhou, J.X.4
Zhou, J.M.5
-
59
-
-
0031590320
-
Unfolding of dimeric creatine kinase in urea and guanidine hydrochloride as measured using small angle X-ray scattering with synchrotron radiation
-
Zhou JM, Fan YX, Kihara H, Kimura K, Amemiya Y. 1997. Unfolding of dimeric creatine kinase in urea and guanidine hydrochloride as measured using small angle X-ray scattering with synchrotron radiation. FEBS Lett 415:183-185.
-
(1997)
FEBS Lett
, vol.415
, pp. 183-185
-
-
Zhou, J.M.1
Fan, Y.X.2
Kihara, H.3
Kimura, K.4
Amemiya, Y.5
-
60
-
-
0022645377
-
Comparison of activity and conformation changes during refolding of urea-denatured creatine kinase
-
Zhou HM, Tsou CL. 1986. Comparison of activity and conformation changes during refolding of urea-denatured creatine kinase. Biochim Biophys Acta 869:69-74.
-
(1986)
Biochim Biophys Acta
, vol.869
, pp. 69-74
-
-
Zhou, H.M.1
Tsou, C.L.2
-
61
-
-
0027502655
-
Conformational changes at the active site of creatine kinase at low concentrations of guanidine hydrochloride
-
Zhou HM, Zhang XH, Yin Y, Tsou CL. 1993. Conformational changes at the active site of creatine kinase at low concentrations of guanidine hydrochloride. Biochem J 291:103-107.
-
(1993)
Biochem J
, vol.291
, pp. 103-107
-
-
Zhou, H.M.1
Zhang, X.H.2
Yin, Y.3
Tsou, C.L.4
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