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Wallimann T, Wyss M, Brdiczka D, Nicolay K, Eppenberger HM. Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the ‘PCr-circuit’ for cellular energy homeostasis. Biochem J 1992;281:21–40.
McFarland EW, Kushmerick MJ, Moerland T. Activity of creatine kinase in a contracting mammalian muscle of uniform fiber type. Biophy J 1994;67:1912–24.
Wiseman RW, Kushmerick M. Creatine kinase equilibrium follows solution thermodynamics in skeletal muscle:31P-NMR studies using creatine analogs. J Biol Chem 1995;270:12428–38.
Wallimann T.31P-NMR-measured creatine kinase reaction flux in muscle: a CAVEAT!. J Muscle Res Cell Motil 1994;17:177–81.
VanDeursen J, Wieringa B, et al. Creatine kinase in skeletal muscle energy metabolism: a study of mouse mutants with graded reduction in muscle CK expression. Proc Natl Acad Sci USA 1994;91:9091–5.
Wallimann T. Dissecting the role of creatine kinase. Curr Biol 1994;1:42–6.
Kreis R, Koster M, Kamber M, Hoppeler H, Boesch C. Peak assignment in localized1H MR spectra of human muscle based on oral creatine supplementation. Magn Res Med 1997;37:159–63.
LeRumeur E, LeTallec N, Kernec F, de Certaines JD. Kinetics of ATP to ADP β-phosphoryl conversion in contracting skeletal muscle by in vivo31P-NMR magnetization transfer. NMR Biomed 1997;10:67–72.
Ntziachristos V, Kreis R, Boesch C, Quistorff B. Dipolar resonance frequency shifts in1H MR spectra of skeletal muscle: confirmation in rats at 4.7 T in vivo and observation of changes postmortem. Magn Reson Med 1997;38:33–9.
Williams JP, Headrick JP. Differences in nucleotide compartmentation and energy state in isolated and in sit rat heart: assessment by31P-NMR spectroscopy. Biochim Biophys Acta 1996;1276:71–9.
Hochachka PW, Mossey MK. Does muscle creatine phosphokinase have access to the total pool of phosphocreatine plus creatine? Am J Physiol 1998;274:868–72.
VanDorsten F, Wyss M, Wallimann T, Nicolay K. Activation of sea urchin sperm motility is accompanied by an increase in the creatine kinase exchange flux. Biochem J 1997;325:411–6.
Kaldis P, Kamp G, Piendl T, Wallimann T. Functions of creatine kinase isoenzymes in spermatozoa. Adv Develop Biol 1997;5:275–312.
Steeghs K, Wieringa B, et al. Altered Ca2+-response in muscles with combined mitochondrial and cytosolic creatine kinase deficiencies. Cell 1997;89:93–103.
Rossi AM, Eppenberger HM, Volpe P, Cotrufo R, Wallimann T. Muscle type MM-creatine kinase is specifically bound to sarcoplasmic reticulum and can support Ca2+-uptake and regulate local ATP/ADP ratios. J Biol Chem 1990;265:5258–66.
Korge P, Campbell KB. Local ATP regeneration is important for sarcoplasmic reticulum Ca2+-pump function. Am J Physiol 1994;267:357–66.
Minajeva A, Ventura-Calapier R, Veksler V. Ca2+-uptake by cardiac sarcoplasmic reticulum ATPase in situ strongly depends on bound creatine kinase. Pflügers Arch 1996;432:904–12.
Ponticos M, Lu QL, Morgan JE, Hardie DG, Partridge TA, Carling D. Dual regulation of AMP-activated protein kinase provides a novel mechanism for the control of creatine kinase in skeletal muscle. EMBO J 1998;17:1688–99.
Stolz M, Wallimann T. Myofibrillar interaction of cytosolic creatine kinase (CK) isoenzymes: allocation of N-terminal binding epitope in MM-CK and BB-CK. J Cell Sci 1998;111:1207–16.
Kraft Th, Nier V, Brenner B, Wallimann T. Binding of creatine kinase to theI-band of skinned skeletal muscle fibers is mediated by glycolytic enzymes: an in situ biochemical approach. Biophys J 1996;70:A292.
Schlattner U, Forstner M, Eder M, Stachowiak O, Fritz-Wolf K, and Wallimann T (1998) Functional aspects of the X-ray structure of mitochondrial creatine kinase: a molecular physiology approach. Mol Cell Biochem 184 (in press).
Wyss M, Smeitink J, Wevers R, Wallimann T. Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism. Biochim Biophys Acta 1992;1102:119–66.
Brdiczka D, Kaldis P, Wallimann T. In vitro complex formation between the octamer of mitochondrial creatine kinase and porin. J Biol Chem 1994;269:27640–4.
Beutner G, Rück A, Riede B, Welte W, Brdiczka D. Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore. FEBS Lett 1997;396:189–95.
O’Gorman E, Beutner G, Dolder M, Koretsky AP, Brdiczka D, Wallimann T. The role of creatine kinase in inhibition of mitochondrial permeability transition. FEBS Lett 1997;414:253–7.
Fritz-Wolf K, Schnyder T, Wallimann T, Kabsch W. Structure of mitochondrial creatine kinase. Nature 1996;381:341–5.
Stachowiak O, Schlattner U, Dolder M, and Wallimann T (1998) Oligomeric state and membrane binding behaviour of creatine kinase isoenzymes: implicaitons for cellular function and mitochondrial structure. Mol Cell Biochem 184 (in press).
O’Gorman E, Fuchs K-H, Tittmann P, Gross H, Wallimann T. Crystalline mitochondrial inclusion bodies isolated from creatine-depleted rat soleus muscle. J Cell Sci 1997;110:1403–11.
Stachowiak O, Dolder M, Wallimann T, Richter Ch. Mitochondrial creatine kinase is a prime target of peroxynitrite-induced modification and inactivation. J Biol Chem 1998;273:16194–699.
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Wallimann, T., Dolder, M., Schlattner, U. et al. Creatine kinase: An enzyme with a central role in cellular energy metabolism. MAGMA 6, 116–119 (1998). https://doi.org/10.1007/BF02660927
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DOI: https://doi.org/10.1007/BF02660927