Publications of S. Shima
All genres
Journal Article (145)
2000
Journal Article
267 (22), pp. 6619 - 6623 (2000)
A mutation affecting the association equilibrium of formyltransferase from the hyperthermophilic Methanopyrus kandleri and its influence on the enzyme's activity and thermostability. EUROPEAN JOURNAL OF BIOCHEMISTRY 1999
Journal Article
7 (10), pp. 1257 - 1268 (1999)
The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri. Structure
Journal Article
171 (5), pp. 317 - 323 (1999)
Purification, characterization, and primary structure of a monofunctional catalase from Methanosarcina barkeri. Archives of Microbiology 1998
Journal Article
8 (6), pp. 749 - 758 (1998)
Active sites of transition-metal enzymes with a focus on nickel. Current Opinion in Structural Biology
Journal Article
258 (1), pp. 85 - 92 (1998)
Lyotropic‐salt‐induced changes in monomer/dimer/tetramer association equilibrium of formyltransferase from the hyperthermophilic Methanopyrus kandleri in relation to the activity and thermostability of the enzyme. European Journal of Biochemistry
Journal Article
Unique structures of the enzymes from methanogens. Seibutsu-Kogaku Kaishi (76), 353 (1998)
Journal Article
[Mechanism of biological methane formation structure and function of methyl-coenzyme M reductase]. Protein, Nucleic acid and Enzyme (43), pp. 1461 - 1467 (1998)
Journal Article
170 (6), pp. 469 - 472 (1998)
Activation and thermostabilization effects of cyclic 2,3-diphosphoglycerate on enzymes from the hyperthermophilic Methanopyrus kandleri. ARCHIVES OF MICROBIOLOGY 1997
Journal Article
278 (5342), pp. 1457 - 1462 (1997)
Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation. Science
Journal Article
5 (5), pp. 635 - 646 (1997)
Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri — new insights into salt-dependence and thermostability. Structure
Journal Article
121 (5), pp. 829 - 830 (1997)
Crystallization and preliminary X-ray diffraction studies of methyl-coenzyme M reductase from methanobacterium thermoautotrophicum. Journal of Biochemistry 1996
Journal Article
26 (1), pp. 118 - 120 (1996)
Crystallization and preliminary X‐ray diffraction studies of formylmethanofuran: Tetrahydromethanopterin formyltransferase from Methanopyrus kandleri. Proteins: Structure, Function, and Bioinformatics
Journal Article
165 (2), pp. 97 - 105 (1996)
Primary structure and properties of the formyltransferase from the mesophilic Methanosarcina barkeri: Comparison with the enzymes from thermophilic and hyperthermophilic methanogens. ARCHIVES OF MICROBIOLOGY 1995
Journal Article
230 (3), pp. 906 - 913 (1995)
FORMYLMETHANOFURAN - TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE (FTR) FROM THE HYPERTHERMOPHILIC METHANOPYRUS-KANDLERI - CLONING, SEQUENCING AND FUNCTIONAL EXPRESSION OF THE FTR GENE AND ONE-STEP PURIFICATION OF THE ENZYME OVERPRODUCED IN ESCHERICHIA-COLI. EUROPEAN JOURNAL OF BIOCHEMISTRY 1994
Journal Article
119 (1-2), pp. 119 - 122 (1994)
The phylogenetic position of Hydrogenobacter acidophilus based on 16S rRNA sequence analysis. FEMS Microbiology Letters 1993
Journal Article
Hydrogenobacter acidophilus: Is its ancestor a missing-link between the Bacteria and the Archaea? RIKEN review (3), pp. 3 - 4 (1993)
Journal Article
Cellulases of clostridia: genetics and biochemistry. The Heredity (43), pp. 56 - 60 (1993)
Journal Article
38 (6), pp. 750 - 754 (1993)
Purification and properties of two truncated endoglucanases produced in Escherichia coli harbouring Clostridium cellulolyticum endoglucanase gene celCCD. Appl Microbiol Biotechnol
Journal Article
43 (4), pp. 703 - 708 (1993)
Hydrogenobacter acidophilus sp. nov., a Thermoacidophilic, Aerobic, Hydrogen-Oxidizing Bacterium Requiring Elemental Sulfur for Growth. INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLOGY 1991
Journal Article
104 (1), pp. 33 - 38 (1991)
NUCLEOTIDE-SEQUENCE ANALYSIS OF THE ENDOGLUCANASE-ENCODING GENE, CELCCD, OF CLOSTRIDIUM-CELLULOLYTICUM. GENE