Stefan Janecek
Stefan Janecek
Laboratory of Protein Evolution, Institute of Molecular Biology, Slovak Academy of Sciences
Overená e-mailová adresa na: - Domovská stránka
Citované v
Citované v
Relationship of sequence and structure to specificity in the α-amylase family of enzymes
EA MacGregor, Š Janeček, B Svensson
Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular …, 2001
α-Amylase: an enzyme specificity found in various families of glycoside hydrolases
Š Janeček, B Svensson, EA MacGregor
Cellular and molecular life sciences 71 (7), 1149-1170, 2014
Thermophilic archaeal amylolytic enzymes
E Lévêque, Š Janeček, B Haye, A Belarbi
Enzyme and microbial technology 26 (1), 3-14, 2000
α-Amylase family: molecular biology and evolution
S Janec̆ek
Progress in biophysics and molecular biology 67 (1), 67-97, 1997
Domain evolution in the α-amylase family
S Janecek, B Svensson, B Henrissat
Journal of molecular evolution 45, 322-331, 1997
The carbohydrate‐binding module family 20–diversity, structure, and function
C Christiansen, M Abou Hachem, Š Janeček, A Viksø‐Nielsen, ...
The FEBS journal 276 (18), 5006-5029, 2009
How many conserved sequence regions are there in the α-amylase family
Š Janeček
Biologia 57 (Suppl 11), 29-41, 2002
Pectin degrading glycoside hydrolases of family 28: sequence-structural features, specificities and evolution
O Markovič, Š Janeček
Protein engineering 14 (9), 615-631, 2001
Starch-binding domains in the post-genome era
M Machovič, Š Janeček
Cellular and Molecular Life Sciences CMLS 63, 2710-2724, 2006
Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes
CAZypedia Consortium
Glycobiology 28 (1), 3-8, 2018
The evolution of starch-binding domain
Š Janeček, J Ševčı́k
FEBS letters 456 (1), 119-125, 1999
Sequence Similarities and Evolutionary Relationships of Microbial, Plant and Animal α‐amylases
Š Janeček
European Journal of Biochemistry 224 (2), 519-524, 1994
Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals
Š Janeček, B Svensson, EA MacGregor
Enzyme and microbial technology 49 (5), 429-440, 2011
Relation between domain evolution, specificity, and taxonomy of the α‐amylase family members containing a C‐terminal starch‐binding domain
Š Janeček, B Svensson, EA MacGregor
European Journal of Biochemistry 270 (4), 635-645, 2003
Pectin methylesterases: sequence-structural features and phylogenetic relationships
O Markovič, Š Janeček
Carbohydrate Research 339 (13), 2281-2295, 2004
Bioinformatics of the glycoside hydrolase family 57 and identification of catalytic residues in amylopullulanase from Thermococcus hydrothermalis
R Zona, F Chang‐Pi‐Hin, MJ O'Donohue, Š Janeček
European Journal of Biochemistry 271 (14), 2863-2872, 2004
Oligo-1, 6-glucosidase and neopullulanase enzyme subfamilies from the α-amylase family defined by the fifth conserved sequence region
A Oslancova, Š Janeček
Cellular and Molecular Life Sciences CMLS 59, 1945-1959, 2002
Strategies for obtaining stable enzymes
S Janec̆ek
Process Biochemistry 28 (7), 435-445, 1993
Starch-binding domains as CBM families–history, occurrence, structure, function and evolution
Š Janeček, F Mareček, EA MacGregor, B Svensson
Biotechnology Advances 37 (8), 107451, 2019
The evolution of putative starch-binding domains
M Machovič, Š Janeček
FEBS letters 580 (27), 6349-6356, 2006
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Články 1–20