Published in Appl Environ Microbiol on April 28, 2017
Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (1970) 1528.65
Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol (1993) 64.61
Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene (1989) 60.30
APE: Analyses of Phylogenetics and Evolution in R language. Bioinformatics (2004) 39.31
The carbohydrate-active enzymes database (CAZy) in 2013. Nucleic Acids Res (2013) 10.24
Psychrophilic enzymes: hot topics in cold adaptation. Nat Rev Microbiol (2003) 3.18
Advances in microbial amylases. Biotechnol Appl Biochem (2000) 3.11
Structure and possible catalytic residues of Taka-amylase A. J Biochem (1984) 2.89
Properties and applications of starch-converting enzymes of the alpha-amylase family. J Biotechnol (2002) 2.77
Protein thermal stability, hydrogen bonds, and ion pairs. J Mol Biol (1997) 2.69
Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes. Biochim Biophys Acta (2001) 2.21
Cold-adapted enzymes. Annu Rev Biochem (2006) 2.21
The Bradford method for protein quantitation. Methods Mol Biol (1994) 2.08
How enzymes adapt: lessons from directed evolution. Trends Biochem Sci (2001) 2.03
Cold-adapted enzymes: from fundamentals to biotechnology. Trends Biotechnol (2000) 1.92
A thermophilic extracellular -amylase from Bacillus licheniformis. Arch Biochem Biophys (1973) 1.73
Minimalist active-site redesign: teaching old enzymes new tricks. Angew Chem Int Ed Engl (2007) 1.67
Low-temperature extremophiles and their applications. Curr Opin Biotechnol (2002) 1.65
Psychrophilic enzymes: molecular basis of cold adaptation. Cell Mol Life Sci (1997) 1.63
Activity-stability relationships in extremophilic enzymes. J Biol Chem (2003) 1.62
Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution. J Mol Biol (1995) 1.48
Protein engineering of bacterial alpha-amylases. Biochim Biophys Acta (2000) 1.40
Engineering proteins for thermostability: the use of sequence alignments versus rational design and directed evolution. Curr Opin Biotechnol (2001) 1.36
Structures of the psychrophilic Alteromonas haloplanctis alpha-amylase give insights into cold adaptation at a molecular level. Structure (1998) 1.35
A quantitative starch-iodine method for measuring alpha-amylase and glucoamylase activities. Anal Biochem (2006) 1.30
α-Amylase: an enzyme specificity found in various families of glycoside hydrolases. Cell Mol Life Sci (2013) 1.19
Improving the catalytic activity of a thermophilic enzyme at low temperatures. Biochemistry (2000) 1.15
Structure of the Aspergillus oryzae alpha-amylase complexed with the inhibitor acarbose at 2.0 A resolution. Biochemistry (1997) 1.15
Biotechnological uses of enzymes from psychrophiles. Microb Biotechnol (2011) 1.14
Diversity and cold-active hydrolytic enzymes of culturable bacteria associated with Arctic sea ice, Spitzbergen. Extremophiles (2004) 1.14
Nucleotide sequence of the alpha-amylase gene (ALP1) in the yeast Saccharomycopsis fibuligera. FEBS Lett (1987) 1.08
Selection of mutations for increased protein stability. Curr Opin Biotechnol (2002) 1.05
Temperature adaptation of proteins: engineering mesophilic-like activity and stability in a cold-adapted alpha-amylase. J Mol Biol (2003) 1.04
Expression of Talaromyces emersonii cellobiohydrolase Cel7A in Saccharomyces cerevisiae and rational mutagenesis to improve its thermostability and activity. Protein Eng Des Sel (2009) 1.02
Structural determinants of cold adaptation and stability in a large protein. J Biol Chem (2001) 1.02
Status of protein engineering for biocatalysts: how to design an industrially useful biocatalyst. Curr Opin Chem Biol (2010) 1.01
Acid stabilization of Bacillus licheniformis alpha amylase through introduction of mutations. Appl Microbiol Biotechnol (2008) 0.98
Solution of the structure of Aspergillus niger acid alpha-amylase by combined molecular replacement and multiple isomorphous replacement methods. Acta Crystallogr B (1991) 0.98
A novel multifunctional α-amylase from the thermophilic fungus Malbranchea cinnamomea: biochemical characterization and three-dimensional structure. Appl Biochem Biotechnol (2013) 0.97
Purification and characterization of a cold-adapted alpha-amylase produced by Nocardiopsis sp. 7326 isolated from Prydz Bay, Antarctic. Mar Biotechnol (NY) (2007) 0.96
Improving the thermostability and catalytic efficiency of Bacillus deramificans pullulanase by site-directed mutagenesis. Appl Environ Microbiol (2013) 0.95
Improved thermostability of a Bacillus alpha-amylase by deletion of an arginine-glycine residue is caused by enhanced calcium binding. Biochem Biophys Res Commun (1998) 0.95
Crystallization and preliminary X-ray diffraction studies of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23. Protein Sci (1996) 0.95
Engineering of the alpha-amylase from Geobacillus stearothermophilus US100 for detergent incorporation. Biotechnol Bioeng (2009) 0.94
Cloning of the aapT gene and characterization of its product, alpha-amylase-pullulanase (AapT), from thermophilic and alkaliphilic Bacillus sp. strain XAL601. Appl Environ Microbiol (1994) 0.94
Enzyme redesign. Chem Rev (2001) 0.93
Cold adaptation of a mesophilic subtilisin-like protease by laboratory evolution. J Biol Chem (2000) 0.92
Structure-based engineering of histidine residues in the catalytic domain of α-amylase from Bacillus subtilis for improved protein stability and catalytic efficiency under acidic conditions. J Biotechnol (2012) 0.92
Enhancing the thermostability of alpha-glucosidase from Thermoanaerobacter tengcongensis MB4 by single proline substitution. J Biosci Bioeng (2010) 0.89
Cold and Hot Extremozymes: Industrial Relevance and Current Trends. Front Bioeng Biotechnol (2015) 0.88
Deletion analysis of the C-terminal region of the alpha-amylase of Bacillus sp. strain TS-23. Arch Microbiol (2002) 0.87
Phylogenetic and biochemical characterization of a novel cluster of intracellular fungal alpha-amylase enzymes. Microbiology (2007) 0.87
Enhancement of the thermostability and the catalytic efficiency of Bacillus pumilus CBS protease by site-directed mutagenesis. Biochimie (2010) 0.87
In silico rational design and systems engineering of disulfide bridges in the catalytic domain of an alkaline α-amylase from Alkalimonas amylolytica to improve thermostability. Appl Environ Microbiol (2013) 0.86
The effect of proline insertions on the thermostability of a barley alpha-glucosidase. Protein Eng (2002) 0.85
Engineering of a truncated alpha-amylase of Bacillus sp. strain TS-23 for the simultaneous improvement of thermal and oxidative stabilities. J Biosci Bioeng (2009) 0.85
Engineering the properties of a cold active enzyme through rational redesign of the active site. Eur J Biochem (2001) 0.83
Remarkable evolutionary relatedness among the enzymes and proteins from the α-amylase family. Cell Mol Life Sci (2016) 0.80
Phylogenomic relationships between amylolytic enzymes from 85 strains of fungi. PLoS One (2012) 0.79
Molecular cold-adaptation of protein function and gene regulation: The case for comparative genomic analyses in marine ciliated protozoa. Mar Genomics (2009) 0.79
Monoclinic crystal form of Aspergillus niger alpha-amylase in complex with maltose at 1.8 angstroms resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun (2006) 0.79
Recent advances in biocatalyst discovery, development and applications. Bioorg Med Chem (2014) 0.79
alpha-Amylases and approaches leading to their enhanced stability. FEBS Lett (1992) 0.78
Protein engineering by random mutagenesis and structure-guided consensus of Geobacillus stearothermophilus Lipase T6 for enhanced stability in methanol. Appl Environ Microbiol (2013) 0.78
Structural thermal adaptation of β-tubulins from the Antarctic psychrophilic protozoan Euplotes focardii. Proteins (2012) 0.78
Characterization and comparative analysis of psychrophilic and mesophilic alpha-amylases from Euplotes species: a contribution to the understanding of enzyme thermal adaptation. Biochem Biophys Res Commun (2013) 0.78
Enzyme surface rigidity tunes the temperature dependence of catalytic rates. Proc Natl Acad Sci U S A (2016) 0.77
Evolutionary drivers of thermoadaptation in enzyme catalysis. Science (2016) 0.76
Comparative studies on a mesophilic and a thermophilic alpha-amylase. Appl Biochem Biotechnol (2001) 0.76
Enhancement of the thermostability of the maltogenic amylase MAUS149 by Gly312Ala and Lys436Arg substitutions. Bioresour Technol (2010) 0.76