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Determination of the NMR structure of Gln25-ribonuclease T1.
Hatano K, Kojima M, Suzuki E, Tanokura M, Takahashi K. Hatano K, et al. Biol Chem. 2003 Aug;384(8):1173-83. doi: 10.1515/BC.2003.130. Biol Chem. 2003. PMID: 12974386
Structure and function of a pepstatin-insensitive acid proteinase from Aspergillus niger var. Macrosporus.
Takahashi K, Tanokura M, Inoue H, Kojima M, Muto Y, Yamasaki M, Makabe O, Kimura T, Takizawa T, Hamaya T, et al. Takahashi K, et al. Adv Exp Med Biol. 1991;306:203-11. doi: 10.1007/978-1-4684-6012-4_24. Adv Exp Med Biol. 1991. PMID: 1812707 No abstract available.
Primary structure, sequence-specific 1H-NMR assignments and secondary structure in solution of bromelain inhibitor VI from pineapple stem.
Hatano K, Kojima M, Tanokura M, Takahashi K. Hatano K, et al. Eur J Biochem. 1995 Sep 1;232(2):335-43. Eur J Biochem. 1995. PMID: 7556179
These results revealed that the protein consists of an 11-residue light chain and a 41-residue heavy chain, cross-linked to each other by disulfide bonds to form the native inhibitor of 52 residues (M(r) = 5888). ...
These results revealed that the protein consists of an 11-residue light chain and a 41-residue heavy chain, cross-linked to each other by di …
A calorimetric study of Ca2+ binding by wheat germ calmodulin. Regulatory steps driven by entropy.
Tanokura M, Yamada K. Tanokura M, et al. J Biol Chem. 1993 Apr 5;268(10):7090-2. J Biol Chem. 1993. PMID: 8463243
A hypothesis has been proposed for Ca(2+)-binding proteins that a regulatory Ca2+ binding step is endothermic and is driven solely by entropy in the absence of Mg2+ (Imaizumi, M., Tanokura, M., and Yamada, K. (1987) J. ...
A hypothesis has been proposed for Ca(2+)-binding proteins that a regulatory Ca2+ binding step is endothermic and is driven solely by entrop …
Conformation analysis of non-pepsin-type acid proteinase A from the fungus Aspergillus niger by NMR.
Kojima M, Tanokura M, Muto Y, Miyano H, Suzuki E, Hamaya T, Takizawa T, Kono T, Takahashi K. Kojima M, et al. Adv Exp Med Biol. 1995;362:611-5. doi: 10.1007/978-1-4615-1871-6_82. Adv Exp Med Biol. 1995. PMID: 8540381 No abstract available.
Effects of replacement of Lys25 with Gln on the conformation of ribonuclease T1: sequence-specific 1H NMR resonance assignments of Gln25 ribonuclease T1 by two-dimensional NMR spectroscopy.
Kojima M, Miyano H, Suzuki E, Tanokura M, Takahashi K. Kojima M, et al. J Biochem. 1995 Oct;118(4):710-6. doi: 10.1093/oxfordjournals.jbchem.a124970. J Biochem. 1995. PMID: 8576083
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