Kanazawa H - Search Results

1

Futai M, Kanazawa H. Futai M, et al. Among authors: kanazawa h. Tanpakushitsu Kakusan Koso. 1984 Aug;29(8):635-60. Tanpakushitsu Kakusan Koso. 1984. PMID: 6095366 Review. Japanese. No abstract available.

2

[Proton-translocating ATPase of Escherichia coli (author's transl)].

Kanazawa H, Futai M. Kanazawa H, et al. Tanpakushitsu Kakusan Koso. 1981 Oct;26(13):1999-2013. Tanpakushitsu Kakusan Koso. 1981. PMID: 6276919 Review. Japanese. No abstract available.

3

Physiological change in the ionophore-portion of proton-translocating ATPase in an uncoupled mutant of Escherichia coli.

Kanazawa H, Futai M. Kanazawa H, et al. FEBS Lett. 1979 Sep 15;105(2):275-7. doi: 10.1016/0014-5793(79)80628-6. FEBS Lett. 1979. PMID: 39783 Free article. No abstract available.

4

Coupling factor ATPase from Escherichia coli. An uncA mutant (uncA401) with defective alpha subunit.

Kanazawa H, Saito S, Futai M. Kanazawa H, et al. J Biochem. 1978 Dec;84(6):1513-7. doi: 10.1093/oxfordjournals.jbchem.a132276. J Biochem. 1978. PMID: 153904 Free article.

5

[Proton translocating ATPase of Escherichia coli (author's transl)].

Kanazawa H, Futai M. Kanazawa H, et al. Seikagaku. 1979 Oct 25;51(10):1139-44. Seikagaku. 1979. PMID: 160921 Review. Japanese. No abstract available.

6

Change of inhibitor sensitivities of Escherichia coli F1-ATPase due to a mutational substitution of Phe for Ser at residue 174 of the beta subunit.

Takeda K, Miki J, Kanazawa H, Tsuchiya T, Futai M. Takeda K, et al. Among authors: kanazawa h. J Biochem. 1985 May;97(5):1401-7. doi: 10.1093/oxfordjournals.jbchem.a135194. J Biochem. 1985. PMID: 2863263 Free article.

The F1-ATPase from the uncD11 mutant of E. coli (Kanazawa, H., Horiuchi, Y., Takagi, M., Ishino, Y., & Futai, M. (1980) J. Biochem. 88, 695-703), showed different enzymological properties from the wild-type enzyme. ...Previous studies (Noumi, T., Mosher, M.E., N …

The F1-ATPase from the uncD11 mutant of E. coli (Kanazawa, H., Horiuchi, Y., Takagi, M., Ishino, Y., & Futai, M. (1980) J. …

7

Deletion of seven amino acid residues from the gamma subunit of Escherichia coli H+-ATPase causes total loss of F1 assembly on membranes.

Kanazawa H, Hama H, Rosen BP, Futai M. Kanazawa H, et al. Arch Biochem Biophys. 1985 Sep;241(2):364-70. doi: 10.1016/0003-9861(85)90558-2. Arch Biochem Biophys. 1985. PMID: 2864018

8

ATP synthesis and hydrolysis by a hybrid system reconstituted from the beta-subunit of Escherichia coli F1-ATPase and beta-less chromatophores of Rhodospirillum rubrum.

Gromet-Elhanan Z, Khananshvili D, Weiss S, Kanazawa H, Futai M. Gromet-Elhanan Z, et al. Among authors: kanazawa h. J Biol Chem. 1985 Oct 15;260(23):12635-40. J Biol Chem. 1985. PMID: 2864345 Free article.

9

Mutational replacements of conserved amino acid residues in the beta subunit resulted in defective assembly of H+-translocating ATPase (F0F1) in Escherichia coli.

Noumi T, Oka N, Kanazawa H, Futai M. Noumi T, et al. Among authors: kanazawa h. J Biol Chem. 1986 May 25;261(15):7070-5. J Biol Chem. 1986. PMID: 2871027 Free article.

10

Replacement of arginine 246 by histidine in the beta subunit of Escherichia coli H+-ATPase resulted in loss of multi-site ATPase activity.

Noumi T, Taniai M, Kanazawa H, Futai M. Noumi T, et al. Among authors: kanazawa h. J Biol Chem. 1986 Jul 15;261(20):9196-201. J Biol Chem. 1986. PMID: 2873142 Free article.

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