-
1
-
-
0026585611
-
Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: The 'phosphocreatine circuit' for cellular energy homeostasis
-
T. Wallimann, M. Wyss, D. Brdicka, K. Nicolay, H.M. Eppenberger, Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: The 'phosphocreatine circuit' for cellular energy homeostasis. Biochem. J. 281 (1992) 21-40.
-
(1992)
Biochem. J.
, vol.281
, pp. 21-40
-
-
Wallimann, T.1
Wyss, M.2
Brdicka, D.3
Nicolay, K.4
Eppenberger, H.M.5
-
2
-
-
0031712655
-
Functional aspects of the X-ray structure of mitochondrial creatine kinase: A molecular physiology approach
-
U. Schlattner, M. Forstner, M. Eder, O. Stachowiak, K. Fritz-Wolf, T. Wallimann, Functional aspects of the X-ray structure of mitochondrial creatine kinase: A molecular physiology approach, Mol. Cell. Biochem. 184 (1998) 125-140.
-
(1998)
Mol. Cell. Biochem.
, vol.184
, pp. 125-140
-
-
Schlattner, U.1
Forstner, M.2
Eder, M.3
Stachowiak, O.4
Fritz-Wolf, K.5
Wallimann, T.6
-
3
-
-
0032515099
-
Crystal structure of rabbit muscle creatine kinase
-
J.K. Rao, G. Bujacz, A. Wlodawer, Crystal structure of rabbit muscle creatine kinase, FEBS Lett. 429 (1998) 133-137.
-
(1998)
FEBS Lett
, vol.429
, pp. 133-137
-
-
Rao, J.K.1
Bujacz, G.2
Wlodawer, A.3
-
4
-
-
0029884566
-
Structure of mitochondrial creatine kinase
-
K. Fritz-Wolf, T. Schnyder, T. Wallimann, W. Kabsch, Structure of mitochondrial creatine kinase, Nature 381 (1996) 341-345.
-
(1996)
Nature
, vol.381
, pp. 341-345
-
-
Fritz-Wolf, K.1
Schnyder, T.2
Wallimann, T.3
Kabsch, W.4
-
5
-
-
0032718703
-
Crystal structure of brain-type creatine kinase at 1.41 Å resolution
-
M. Eder, U. Schlattner, A. Becker, T. Wallimann, W. Kabsch, K. Fritz-Wolf, Crystal structure of brain-type creatine kinase at 1.41 Å resolution, Protein Sci. 8 (1999) 2258-2269.
-
(1999)
Protein Sci
, vol.8
, pp. 2258-2269
-
-
Eder, M.1
Schlattner, U.2
Becker, A.3
Wallimann, T.4
Kabsch, W.5
Fritz-Wolf, K.6
-
6
-
-
0034658257
-
Crystal structure of human ubiquitous mitochondrial creatine kinase
-
M. Eder, K. Fritz-Wolf, W. Kabsch, T. Wallimann, U. Schlattner, Crystal structure of human ubiquitous mitochondrial creatine kinase, Proteins 39 (2000) 216-225.
-
(2000)
Proteins
, vol.39
, pp. 216-225
-
-
Eder, M.1
Fritz-Wolf, K.2
Kabsch, W.3
Wallimann, T.4
Schlattner, U.5
-
7
-
-
0027979405
-
The N-terminal heptapeptide of mitochondrial creatine kinase is important for octamerization
-
P. Kaldis, R. Furter, T. Wallimann, The N-terminal heptapeptide of mitochondrial creatine kinase is important for octamerization, Biochemistry 33 (1994) 952-959.
-
(1994)
Biochemistry
, vol.33
, pp. 952-959
-
-
Kaldis, P.1
Furter, R.2
Wallimann, T.3
-
8
-
-
0029143228
-
Multiple-state equilibrium unfolding of guanidine kinase
-
M. Gross, A. Lustig, T. Wallimann, R. Furter, Multiple-state equilibrium unfolding of guanidine kinase, Biochemistry 34 (1995) 10350-10357.
-
(1995)
Biochemistry
, vol.34
, pp. 10350-10357
-
-
Gross, M.1
Lustig, A.2
Wallimann, T.3
Furter, R.4
-
9
-
-
0031033159
-
Protease digestion studies of an equilibrium intermediate in the unfolding of creatine kinase
-
T. Webb, P.J. Jackson, G.E. Morris, Protease digestion studies of an equilibrium intermediate in the unfolding of creatine kinase, Biochem. J. 321 (1997) 82-88.
-
(1997)
Biochem. J.
, vol.321
, pp. 82-88
-
-
Webb, T.1
Jackson, P.J.2
Morris, G.E.3
-
11
-
-
0031590320
-
Unfolding of dimeric creatine kinase in urea and guanidine hydrochloride as measured using small angle X-ray scattering with synchrotron radiation
-
J.M. Zhou, Y.X. Fan, H. Kihara, K. Kimura, Y. Amemiya, Unfolding of dimeric creatine kinase in urea and guanidine hydrochloride as measured using small angle X-ray scattering with synchrotron radiation, FEBS Lett. 415 (1997) 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
-
12
-
-
0033532615
-
Reactivation and refolding of a partially folded creatine kinase modified by 5,5′-dithio-bis (2-nitrobenzoic acid)
-
Y. Yang, Y.D. Park, T.W. Yu, H.M. Zhou, Reactivation and refolding of a partially folded creatine kinase modified by 5,5′-dithio-bis (2-nitrobenzoic acid), Biochim. Biophys. Res. Commun. 259 (1999) 450-454.
-
(1999)
Biochim. Biophys. Res. Commun.
, vol.259
, pp. 450-454
-
-
Yang, Y.1
Park, Y.D.2
Yu, T.W.3
Zhou, H.M.4
-
13
-
-
0029564086
-
Conformational changes of active sites during refolding of urea-denatured creatine kinase
-
Z.F. Wang, Y. Yang, H.M. Zhou, Conformational changes of active sites during refolding of urea-denatured creatine kinase, Biochimie 77 (1995) 953-956.
-
(1995)
Biochimie
, vol.77
, pp. 953-956
-
-
Wang, Z.F.1
Yang, Y.2
Zhou, H.M.3
-
14
-
-
0003139458
-
Comparison of activity and conformation changes during refolding of urea-denatured creatine kinase
-
H.M. Zhou, C.L. Tsou, Comparison of activity and conformation changes during refolding of urea-denatured creatine kinase, Biochim. Biophys. Acta 830 (1986) 59-63.
-
(1986)
Biochim. Biophys. Acta
, vol.830
, pp. 59-63
-
-
Zhou, H.M.1
Tsou, C.L.2
-
15
-
-
0029918937
-
Ascerting the number of essential thiol groups of creatine kinase for its folding
-
H.R. Wang, J.H. Bai, S.Y. Zheng, Z.X. Wang, H.M. Zhou, Ascerting the number of essential thiol groups of creatine kinase for its folding, Biochim. Biophys. Res. Commun. 221 (1996) 174-180.
-
(1996)
Biochim. Biophys. Res. Commun.
, vol.221
, pp. 174-180
-
-
Wang, H.R.1
Bai, J.H.2
Zheng, S.Y.3
Wang, Z.X.4
Zhou, H.M.5
-
16
-
-
0034811760
-
Relationship between kinetic and equilibrium folding intermediates of creatine kinase
-
L. Zhu, Y.X. Fan, S. Perrett, J.M. Zhou, Relationship between kinetic and equilibrium folding intermediates of creatine kinase, Biochim. Biophys. Res. Commun. 285 (2001) 857-862.
-
(2001)
Biochim. Biophys. Res. Commun.
, vol.285
, pp. 857-862
-
-
Zhu, L.1
Fan, Y.X.2
Perrett, S.3
Zhou, J.M.4
-
17
-
-
0027941819
-
An equilibrium study of the dependence of secondary and tertiary structure of creatine kinase on subunit association
-
S.H. Grossman, An equilibrium study of the dependence of secondary and tertiary structure of creatine kinase on subunit association, Biochim. Biophys. Acta 1209 (1994) 19-23.
-
(1994)
Biochim. Biophys. Acta
, vol.1209
, pp. 19-23
-
-
Grossman, S.H.1
-
18
-
-
0032577216
-
Equilibrium intermediates in the unfolding pathway of creatine kinase
-
Y.L. Zhang, Y.X. Fan, G.C. Huang, J.X. Zhou, J.M. Zhou, Equilibrium intermediates in the unfolding pathway of creatine kinase, Biochim. Biophys. Res. Commun. 246 (1998) 609-612.
-
(1998)
Biochim. Biophys. Res. Commun.
, 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
-
19
-
-
0036538649
-
Unraveling multistate unfolding of rabbit muscle creatine kinase
-
I.M. Kuznetsova, O.V. Stepanenko, K.K. Turoverov, L. Zhu, J.M. Zhou, A.L. Fink, V.N. Uversky, Unraveling multistate unfolding of rabbit muscle creatine kinase, Biochim. Biophys. Acta 1596 (2002) 138-155.
-
(2002)
Biochim. Biophys. Acta
, vol.1596
, pp. 138-155
-
-
Kuznetsova, I.M.1
Stepanenko, O.V.2
Turoverov, K.K.3
Zhu, L.4
Zhou, J.M.5
Fink, A.L.6
Uversky, V.N.7
-
20
-
-
0035847059
-
Identification of equilibrium and kinetic intermediates involved in folding of urea-denatured creatine kinase
-
L. Zhu, Y.X. Fan, J.M. Zhou, Identification of equilibrium and kinetic intermediates involved in folding of urea-denatured creatine kinase, Biochim. Biophys. Acta 1544 (2001) 320-332.
-
(2001)
Biochim. Biophys. Acta
, vol.1544
, pp. 320-332
-
-
Zhu, L.1
Fan, Y.X.2
Zhou, J.M.3
-
21
-
-
0028829823
-
Reversible dissociation and unfolding of dimeric creatine kinase isoenzyme MM in guanidine hydrochloride and urea
-
F. Couthon, E. Clottes, C. Ebel, C. Vial, Reversible dissociation and unfolding of dimeric creatine kinase isoenzyme MM in guanidine hydrochloride and urea, Eur. J. Biochem. 234 (1995) 160-170.
-
(1995)
Eur. J. Biochem.
, vol.234
, pp. 160-170
-
-
Couthon, F.1
Clottes, E.2
Ebel, C.3
Vial, C.4
-
22
-
-
0035255007
-
Structure of an intermediates in the unfolding of creatine kinase
-
T.I. Webb, G.E. Morris, Structure of an intermediates in the unfolding of creatine kinase, Proteins 42 (2001) 269-278.
-
(2001)
Proteins
, vol.42
, pp. 269-278
-
-
Webb, T.I.1
Morris, G.E.2
-
23
-
-
0021733938
-
Rabbit muscle creatine phosphokinase cDNA cloning, primary structure, and detection of human homologues
-
S. Putney, W. Herlihy, N. Royal, H. Pang, H.V. Aposhian, L. Pickering, R. Belagaje, K. Biemann, D. Page, S. Kuby, P. Schimmel, Rabbit muscle creatine phosphokinase cDNA cloning, primary structure, and detection of human homologues, J. Biol. Chem. 259 (1984) 14317-14320.
-
(1984)
J. Biol. Chem.
, vol.259
, pp. 14317-14320
-
-
Putney, S.1
Herlihy, W.2
Royal, N.3
Pang, H.4
Aposhian, H.V.5
Pickering, L.6
Belagaje, R.7
Biemann, K.8
Page, D.9
Kuby, S.10
Schimmel, P.11
-
24
-
-
0017184389
-
A rapid and sensitive method for the quantination of microgram quantities of protein utilizing the principle of protein-dye binding
-
M.M. Bradford, A rapid and sensitive method for the quantination of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248-254.
-
(1976)
Anal. Biochem.
, vol.72
, pp. 248-254
-
-
Bradford, M.M.1
-
25
-
-
0020344240
-
A comparison of denaturation and inactivation rates of creatinine kinase in guanidine solutions
-
Q.Z. Yao, H.M. Zhou, L.X. Hou, C.L. Tsou, A comparison of denaturation and inactivation rates of creatinine kinase in guanidine solutions, Sci. Sin. 25B (1982) 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
-
26
-
-
0031715149
-
Inactivation of creatine kinase is due to the conformational changes of the active sites during thermal denaturation
-
J.H. Bai, S.Y. Zheng, H.M. Zhou, Inactivation of creatine kinase is due to the conformational changes of the active sites during thermal denaturation, Biochem. Mol. Biol. Int. 45 (1998) 941-951.
-
(1998)
Biochem. Mol. Biol. Int.
, vol.45
, pp. 941-951
-
-
Bai, J.H.1
Zheng, S.Y.2
Zhou, H.M.3
-
27
-
-
0029894773
-
Rabbit muscle creatine kinase: Consequences of the mutagenesis of conserved histidine residues
-
L.H. Chen, C.L. Borders Jr, J.R. Vasquez, G.L. Kenyon, Rabbit muscle creatine kinase: Consequences of the mutagenesis of conserved histidine residues, Biochemistry 35 (1996) 7895-7902.
-
(1996)
Biochemistry
, vol.35
, pp. 7895-7902
-
-
Chen, L.H.1
Borders Jr., C.L.2
Vasquez, J.R.3
Kenyon, G.L.4
-
28
-
-
0032127359
-
Role of quaternary structure in muscle creatine kinase stability: Tryptophan 210 is important for dimmer cohesion
-
C. Perraut, E. Clottes, C. Leydier, C. Vial, O. Marcillat, Role of quaternary structure in muscle creatine kinase stability: Tryptophan 210 is important for dimmer cohesion, Proteins 32 (1998) 43-51.
-
(1998)
Proteins
, vol.32
, pp. 43-51
-
-
Perraut, C.1
Clottes, E.2
Leydier, C.3
Vial, C.4
Marcillat, O.5
-
29
-
-
0034282672
-
A conserved negatively charged cluster in the active site of creatine kinase is critical for enzymatic activity
-
M. Eder, M. Stolz, T. Wallimann, U. Schlattners, A conserved negatively charged cluster in the active site of creatine kinase is critical for enzymatic activity. J. Biol. Chem. 275 (2000) 27094-27099.
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 27094-27099
-
-
Eder, M.1
Stolz, M.2
Wallimann, T.3
Schlattners, U.4
-
30
-
-
0032555162
-
Transition state structure of arginine kinase: Implications for catalysis of bimolecular reactions
-
G. Zhao, T. Somasundaram, E. Blanc, G. Parthasarathy, W.R. Ellington, M.S. Chapman, Transition state structure of arginine kinase: Implications for catalysis of bimolecular reactions, Proc. Natl. Acad. Sci. 95 (1998) 8449-8454.
-
(1998)
Proc. Natl. Acad. Sci.
, vol.95
, pp. 8449-8454
-
-
Zhao, G.1
Somasundaram, T.2
Blanc, E.3
Parthasarathy, G.4
Ellington, W.R.5
Chapman, M.S.6
-
31
-
-
0028246759
-
The tryptophan residues of mitochondrial creatine kinase: Roles of Trp-223, Trp-206 and Trp-264 in active-site and quaternary structure formation
-
M. Gross, E.M. Furter-Graves, T. Wallimann, H.M. Eppenberger, R. Furter, The tryptophan residues of mitochondrial creatine kinase: Roles of Trp-223, Trp-206 and Trp-264 in active-site and quaternary structure formation, Protein Sci. 3 (1994) 1058-1068.
-
(1994)
Protein Sci
, vol.3
, pp. 1058-1068
-
-
Gross, M.1
Furter-Graves, E.M.2
Wallimann, T.3
Eppenberger, H.M.4
Furter, R.5
-
32
-
-
0027268548
-
Creatine kinase: The reactive cysteine is required for synergism but is nonessential for catalysis
-
R. Furter, E.M. Furter-Graves, T. Wallimann, Creatine kinase: The reactive cysteine is required for synergism but is nonessential for catalysis, Biochemistry 32 (1993) 7022-7029.
-
(1993)
Biochemistry
, vol.32
, pp. 7022-7029
-
-
Furter, R.1
Furter-Graves, E.M.2
Wallimann, T.3
|