Increasing the thermal stability of cellulase C using rules learned from thermophilic proteins: a pilot study.

[1]  O. Shoseyov,et al.  Analysis of functional domains of endoglucanases from Clostridium cellulovorans by gene cloning, nucleotide sequencing and chimeric protein construction , 1992, Molecular and General Genetics MGG.

[2]  P. Bork,et al.  Homology among (betaalpha)(8) barrels: implications for the evolution of metabolic pathways. , 2000, Journal of molecular biology.

[3]  P. Bork,et al.  Homology among (βα) 8 barrels: implications for the evolution of metabolic pathways 1 1Edited by G. Von Heijne , 2000 .

[4]  A. Szilágyi,et al.  Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey. , 2000, Structure.

[5]  A. Szilágyi,et al.  Mirror image mutations reveal the significance of an intersubunit ion cluster in the stability of 3‐isopropylmalate dehydrogenase , 2000, FEBS letters.

[6]  Tohru Kobayashi,et al.  Deduced Amino Acid Sequence and Possible Catalytic Residues of a Thermostable, Alkaline Cellulase from an Alkaliphilic Bacillus Strain , 2000, Bioscience, biotechnology, and biochemistry.

[7]  L. Wyns,et al.  The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: A comparative thermostability structural analysis of ten different TIM structures , 1999, Proteins.

[8]  D Eisenberg,et al.  Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability. , 1999, Journal of molecular biology.

[9]  G. Böhm,et al.  The stability of proteins in extreme environments. , 1998, Current opinion in structural biology.

[10]  A. Elcock.  The stability of salt bridges at high temperatures: implications for hyperthermophilic proteins. , 1998, Journal of molecular biology.

[11]  G. Vriend,et al.  Engineering an enzyme to resist boiling. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[12]  G. Vriend,et al.  Evolution reversed: engineering and enzyme to resist boiling , 1998 .

[13]  T. Oshima,et al.  Stabilization of Escherichia coli isopropylmalate dehydrogenase by single amino acid substitution. , 1997, Protein engineering.

[14]  M. Lascombe,et al.  The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism. , 1996, Journal of molecular biology.

[15]  Zbigniew Dauter,et al.  A common protein fold and similar active site in two distinct families of β-glycanases , 1996, Nature Structural Biology.

[16]  J. Martial,et al.  Crystal structure of recombinant triosephosphate isomerase from bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three‐dimensional structures points to the importance of hydrophobic interactions , 1995, Protein science : a publication of the Protein Society.

[17]  B. Henrissat,et al.  Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[18]  R. Pickersgill,et al.  β‐Glucosidase, β‐galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes wit 8‐fold β/α architecture and with two conserved glutamates near the carboxy‐terminal ends of β‐strands four and seven , 1995 .

[19]  Robert L. Campbell,et al.  Thermostabilization of the Bacillus circulansxylanase by the introduction of disulfide bonds , 1994 .

[20]  M. Yaguchi,et al.  Thermostabilization of the Bacillus circulans xylanase by the introduction of disulfide bonds. , 1994, Protein engineering.

[21]  R. Dominguez,et al.  Characterization of two crystal forms of Clostridium thermocellum endoglucanase CelC , 1994 .

[22]  B. Tidor,et al.  Do salt bridges stabilize proteins? A continuum electrostatic analysis , 1994, Protein science : a publication of the Protein Society.

[23]  P. Dhurjati,et al.  Properties conferred on Clostridium thermocellum endoglucanase CelC by grafting the duplicated segment of endoglucanase CelD. , 1993, Protein engineering.

[24]  A Bairoch,et al.  New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. , 1993, The Biochemical journal.

[25]  J. Navas,et al.  Site-directed mutagenesis of conserved residues of Clostridium thermocellum endoglucanase CelC. , 1992, Biochemical and biophysical research communications.

[26]  S. Withers,et al.  Stereoselective hydrolysis catalyzed by related beta-1,4-glucanases and beta-1,4-xylanases. , 1992, The Journal of biological chemistry.

[27]  B. Matthews,et al.  Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. , 1992, Science.

[28]  R. Jaenicke,et al.  Protein stability and molecular adaptation to extreme conditions. , 1991, European journal of biochemistry.

[29]  U. Sauer,et al.  Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. , 1991, Biochemistry.

[30]  R. Jaenicke,et al.  Proteins under extreme physical conditions , 1990, FEBS letters.

[31]  B. Matthews,et al.  Substantial increase of protein stability by multiple disulphide bonds , 1989, Nature.

[32]  N Srinivasan,et al.  Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis. , 1989, Protein engineering.

[33]  C. Pace,et al.  Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds. , 1988, The Journal of biological chemistry.

[34]  W. Schwarz,et al.  Nucleotide sequence of the celC gene encoding endoglucanase C of Clostridium thermocellum. , 1988, Gene.

[35]  J. Ponder,et al.  Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. , 1987, Journal of molecular biology.

[36]  J. Millet,et al.  Purification and properties of the endoglucanase C of Clostridium thermocellum produced in Escherichia coli. , 1986, Biochimie.

[37]  C. Pace.  Determination and analysis of urea and guanidine hydrochloride denaturation curves. , 1986, Methods in enzymology.

[38]  T. Creighton.  Disulfide bond formation in proteins. , 1984, Methods in enzymology.

[39]  J M Thornton,et al.  Amino and carboxy-terminal regions in globular proteins. , 1983, Journal of molecular biology.