Identification of equilibrium and kinetic intermediates involved in folding of urea-denatured creatine kinase.

[1]  A. Fersht,et al.  Equilibrium folding properties of the yeast prion protein determinant Ure2. , 1999, Journal of molecular biology.

[2]  Y. Yang,et al.  Reactivation and refolding of a partially folded creatine kinase modified by 5,5'-dithio-bis(2-nitrobenzoic acid). , 1999, Biochemical and biophysical research communications.

[3]  Hiroshi Kihara,et al.  Unfolding and refolding of dimeric creatine kinase equilibrium and kinetic studies , 1998, Protein science : a publication of the Protein Society.

[4]  A. Wlodawer,et al.  Crystal structure of rabbit muscle creatine kinase 1 , 1998, FEBS letters.

[5]  O. Marcillat,et al.  Role of quaternary structure in muscle creatine kinase stability: Tryptophan 210 is important for dimer cohesion , 1998, Proteins.

[6]  R. Sauer,et al.  Formation of a denatured dimer limits the thermal stability of Arc repressor. , 1997, Journal of molecular biology.

[7]  Y. Amemiya,et al.  Unfolding of dimeric creatine kinase in urea and guanidine hydrochloride as measured using small angle X‐ray scattering with synchrotron radiation , 1997, FEBS letters.

[8]  Li Zhu,et al.  The influence of intersubunit cross‐linking on the conformational changes of creatine kinase during denaturation by guanidine hydrochloride , 1997, Biochemistry and molecular biology international.

[9]  Matthews Cr,et al.  Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressor. , 1997 .

[10]  Thomas E. Creighton,et al.  Protein structure : a practical approach , 1997 .

[11]  H. M. Zhou,et al.  Dissociation, unfolding and inactivation of creatine kinase in urea solutions. , 2009, International journal of peptide and protein research.

[12]  K. Kuwajima,et al.  Rapid formation of a molten globule intermediate in refolding of α-lactalbumin , 1996 .

[13]  Z. X. Wang,et al.  Ascertaining the number of essential thiol groups for the folding of creatine kinase. , 1996, Biochemical and biophysical research communications.

[14]  K. Kuwajima The molten globule state of α‐lactalbumin , 1996, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[15]  C. Ebel,et al.  Reversible dissociation and unfolding of dimeric creatine kinase isoenzyme MM in guanidine hydrochloride and urea. , 1995, European journal of biochemistry.

[16]  A. Lustig,et al.  Multiple-state equilibrium unfolding of guanidino kinases. , 1995, Biochemistry.

[17]  O. Ptitsyn,et al.  Molten globule and protein folding. , 1995, Advances in protein chemistry.

[18]  Siddhartha Roy,et al.  Proteins: Structure, Function, and Engineering , 1995, Subcellular Biochemistry.

[19]  K. Neet,et al.  Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturation , 1994, Protein science : a publication of the Protein Society.

[20]  G. Strambini,et al.  Pressure effects on protein flexibility monomeric proteins. , 1994, Journal of molecular biology.

[21]  K. Neet,et al.  Comparative equilibrium denaturation studies of the neurotrophins: nerve growth factor, brain-derived neurotrophic factor, neurotrophin 3, and neurotrophin 4/5. , 1994, Biochemistry.

[22]  R. L. Baldwin,et al.  The molten globule intermediate of apomyoglobin and the process of protein folding , 1993, Protein Science.

[23]  K. Neet,et al.  Spectroscopic and chemical studies of the interaction between nerve growth factor (NGF) and the extracellular domain of the low affinity NGF receptor , 1992, Protein science : a publication of the Protein Society.

[24]  J. W. Taylor,et al.  Dimeric structure and conformational stability of brain-derived neurotrophic factor and neurotrophin-3. , 1992, Biochemistry.

[25]  K. Neet,et al.  Equilibrium denaturation studies of mouse beta-nerve growth factor. , 1992, Protein science : a publication of the Protein Society.

[26]  Matthews Cr,et al.  Folding and stability of trp aporepressor from Escherichia coli. , 1990 .

[27]  K. Kirschner,et al.  Reversible dissociation and unfolding of aspartate aminotransferase from Escherichia coli: characterization of a monomeric intermediate. , 1990, Biochemistry.

[28]  P. S. Kim,et al.  Intermediates in the folding reactions of small proteins. , 1990, Annual review of biochemistry.

[29]  R. Sauer,et al.  Equilibrium dissociation and unfolding of the Arc repressor dimer. , 1989, Biochemistry.

[30]  K. Kuwajima,et al.  The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structure , 1989, Proteins.

[31]  R. Gregory The influence of glycerol on hydrogen isotope exchange in lysozyme , 1988, Biopolymers.

[32]  C. Tsou,et al.  Comparison of activity and conformation changes during refolding of urea-denatured creatine kinase. , 1986, Biochimica et biophysica acta.

[33]  M. Goldberg,et al.  Kinetics and importance of the dimerization step in the folding pathway of the beta 2 subunit of Escherichia coli tryptophan synthase. , 1985, Journal of molecular biology.

[34]  W. Herlihy,et al.  Rabbit muscle creatine phosphokinase. CDNA cloning, primary structure and detection of human homologues. , 1984, The Journal of biological chemistry.

[35]  C. Tsou,et al.  Comparison of the rates of inactivation and conformational changes of creatine kinase during urea denaturation. , 1984, Biochemistry.

[36]  P. S. Kim,et al.  Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. , 1982, Annual review of biochemistry.

[37]  N. C. Price,et al.  The refolding of denatured rabbit muscle creatine kinase. Search for intermediates in the refolding process and effect of modification at the reactive thiol group on refolding. , 1982, The Biochemical journal.

[38]  S. Grossman,et al.  Kinetic evidence for active monomers during the reassembly of denatured creatine kinase. , 1981, Biochemistry.

[39]  C. Zetina,et al.  Reversible unfolding of the β2 subunit of Escherichia coli tryptophan synthetase and its proteolytic fragments , 1980 .

[40]  E. Noltmann,et al.  Studies on adenosine triphosphate transphosphorylases. III. Inhibition reactions. , 1962, The Journal of biological chemistry.

[41]  H. Lardy,et al.  [100] ATP-Creatine transphosphorylase: ATP+Cr⇋ADP+Cr∼P , 1955 .