Terumichi Tanaka

Summary

Affiliation: Toyohashi University of Technology
Country: Japan

Publications

  1. ncbi request reprint Guide DNA technique in bacterial ribonuclease P reaction for effective processing of tRNA precursor
    Terumichi Tanaka
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku cho, Toyohashi, Aichi 441 8580, Japan
    Biotechnol Appl Biochem 36:85-8. 2002
  2. ncbi request reprint Application of a metal switch to aqualysin I, a subtilisin-type bacterial serine protease, to the S3 site residues, ser102 and gly131
    T Tanaka
    Department of Ecological Engineering, Toyohashi University of Technology, Aichi, Japan
    Biosci Biotechnol Biochem 64:2008-11. 2000
  3. ncbi request reprint Another cut for lysine tRNA: application of the hyperprocessing reaction reveals another stabilization strategy in metazoan lysine tRNAs
    Terumichi Tanaka
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku cho, Toyohashi, Aichi 441 8580, Japan
    J Biochem 131:839-47. 2002
  4. ncbi request reprint Escherichia coli tRNAs are resistant to the hyperprocessing reaction of homologous E. coli ribonuclease P ribozyme
    Terumichi Tanaka
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku cho, Toyohashi, Aichi 441 8580, Japan
    Biosci Biotechnol Biochem 67:1172-6. 2003
  5. ncbi request reprint Is your ribozyme design really correct?: A proposal of simple single turnover competition assay to evaluate ribozymes
    T Tanaka
    Department of Ecological Engineering, Toyohashi University of Technology, Aichi, Japan
    Biosci Biotechnol Biochem 65:1636-44. 2001
  6. ncbi request reprint Guide DNA technique reveals that the protein component of bacterial ribonuclease P is a modifier for substrate recognition
    T Tanaka
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku cho, Toyohashi, 441 8580, Aichi, Japan
    FEBS Lett 491:94-8. 2001
  7. ncbi request reprint Examining the bases of the J3/4 domain of Escherichia coli ribonuclease P
    Terumichi Tanaka
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Toyohashi, Japan
    Biosci Biotechnol Biochem 68:1388-92. 2004
  8. ncbi request reprint The P3 domain of E. coli ribonuclease P RNA can be truncated and replaced
    Terumichi Tanaka
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempakucho, Toyohashi, Aichi 441 8580, Japan
    FEBS Lett 577:101-4. 2004
  9. ncbi request reprint Identification and designing of the S3 site of aqualysin I, a thermophilic subtilisin-related serine protease
    T Tanaka
    Department of Biotechnology, The University of Tokyo, Bunkyo ku, Tokyo, 113 8657, Japan
    J Biochem 125:1016-21. 1999
  10. ncbi request reprint P1 specificity of aqualysin I (a subtilisin-type serine protease) from Thermus aquaticus YT-1, using P1-substituted derivatives of Streptomyces subtilisin inhibitor
    T Tanaka
    Department of Biotechnology, The University of Tokyo, Japan
    Biosci Biotechnol Biochem 62:2035-8. 1998

Collaborators

Detail Information

Publications47

  1. ncbi request reprint Guide DNA technique in bacterial ribonuclease P reaction for effective processing of tRNA precursor
    Terumichi Tanaka
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku cho, Toyohashi, Aichi 441 8580, Japan
    Biotechnol Appl Biochem 36:85-8. 2002
    ..The presence of a 5'-flanking region in the DNA did not affect the cleavage reaction. The guide DNA technique is a useful tool for effective preparation of mature tRNA molecules in vitro...
  2. ncbi request reprint Application of a metal switch to aqualysin I, a subtilisin-type bacterial serine protease, to the S3 site residues, ser102 and gly131
    T Tanaka
    Department of Ecological Engineering, Toyohashi University of Technology, Aichi, Japan
    Biosci Biotechnol Biochem 64:2008-11. 2000
    ..These results indicate that two histidines are near each other, and both side chains are metal-accessible. This is the first report on application of the metal-switch technique to a subtilisin-related enzyme...
  3. ncbi request reprint Another cut for lysine tRNA: application of the hyperprocessing reaction reveals another stabilization strategy in metazoan lysine tRNAs
    Terumichi Tanaka
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku cho, Toyohashi, Aichi 441 8580, Japan
    J Biochem 131:839-47. 2002
    ..Our data strongly suggest that the cloverleaf shape of other metazoan lysine tRNAs should also be stabilized by means of similar strategies to in the case of human tRNA(Lys3)...
  4. ncbi request reprint Escherichia coli tRNAs are resistant to the hyperprocessing reaction of homologous E. coli ribonuclease P ribozyme
    Terumichi Tanaka
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku cho, Toyohashi, Aichi 441 8580, Japan
    Biosci Biotechnol Biochem 67:1172-6. 2003
    ..coli RNase P, to find that these homologous tRNAs were resistant to the toxic hyperprocessing reaction. Our results display the evidence for molecular co-evolution between homologous tRNAs and RNase P in the bacterium E. coli...
  5. ncbi request reprint Is your ribozyme design really correct?: A proposal of simple single turnover competition assay to evaluate ribozymes
    T Tanaka
    Department of Ecological Engineering, Toyohashi University of Technology, Aichi, Japan
    Biosci Biotechnol Biochem 65:1636-44. 2001
    ..We found that this assay method is capable of application to those enzymes, as a powerful tool for the selection and designing of RNA-cleaving enzymes...
  6. ncbi request reprint Guide DNA technique reveals that the protein component of bacterial ribonuclease P is a modifier for substrate recognition
    T Tanaka
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku cho, Toyohashi, 441 8580, Aichi, Japan
    FEBS Lett 491:94-8. 2001
    ..Our results suggested that the protein component of RNase P is a modifier for substrate recognition...
  7. ncbi request reprint Examining the bases of the J3/4 domain of Escherichia coli ribonuclease P
    Terumichi Tanaka
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Toyohashi, Japan
    Biosci Biotechnol Biochem 68:1388-92. 2004
    ..Our data showed that the bases in the J3/4 and P4 domains displayed different responses to the metal ions that were affected by the presence of the protein component...
  8. ncbi request reprint The P3 domain of E. coli ribonuclease P RNA can be truncated and replaced
    Terumichi Tanaka
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempakucho, Toyohashi, Aichi 441 8580, Japan
    FEBS Lett 577:101-4. 2004
    ..coli RNase P was able to be truncated to certain length and was replaceable, but could not be deleted in the ribozyme...
  9. ncbi request reprint Identification and designing of the S3 site of aqualysin I, a thermophilic subtilisin-related serine protease
    T Tanaka
    Department of Biotechnology, The University of Tokyo, Bunkyo ku, Tokyo, 113 8657, Japan
    J Biochem 125:1016-21. 1999
    ..Especially, the S102K mutant protein hydrolyzed the polyalanine peptide efficiently. The strategies we have adopted in this paper are applicable to all subtilisin-related enzymes...
  10. ncbi request reprint P1 specificity of aqualysin I (a subtilisin-type serine protease) from Thermus aquaticus YT-1, using P1-substituted derivatives of Streptomyces subtilisin inhibitor
    T Tanaka
    Department of Biotechnology, The University of Tokyo, Japan
    Biosci Biotechnol Biochem 62:2035-8. 1998
    ..SSIs efficiently inhibited the activity of aqualysin I, with low substrate specificity. Charge and hydrophobicity of side chain of the P1 amino acid residue showed no significant effect to the P1-specificity of this enzyme...
  11. ncbi request reprint Engineering of S2 site of aqualysin I; alteration of P2 specificity by excluding P2 side chain
    T Tanaka
    Department of Biotechnology, The University of Tokyo, Japan
    Biochemistry 37:17402-7. 1998
    ..The strategies we have adopted in this paper are applicable to all subtilisin-related enzymes...
  12. ncbi request reprint Substrate shape preference of Escherichia coli ribonuclease P ribozyme and holo enzyme using bottom-half part-shifting variants of pre-tRNA
    Terumichi Tanaka
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Toyohashi, Aichi, Japan
    Biosci Biotechnol Biochem 69:1992-4. 2005
    ....
  13. doi request reprint Analysis on substrate specificity of Escherichia coli ribonuclease P using shape variants of pre-tRNA: proposal of subsites model for substrate shape recognition
    Satoshi Suwa
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Toyohashi, Aichi 441 8580, Japan
    J Biochem 145:151-60. 2009
    ..From these facts, we propose a new substrate recognition model that can explain many experimental facts that have been seen as enigmatic...
  14. ncbi request reprint Kinetics of hyperprocessing reaction of human tyrosine tRNA by ribonuclease P ribozyme from Escherichia coli
    Tomoaki Ando
    Department of Ecological Engineering, Toyohashi University of Technology, Aichi, Japan
    Biosci Biotechnol Biochem 66:1967-71. 2002
    ..These results indicated that the occurrence of hyperprocessing depends on the magnesium ion concentration, and suggested that magnesium ions contribute to the recognition of the shape of the substrate by bacterial RNase P enzymes...
  15. ncbi request reprint The protein component of bacterial ribonuclease P flickers the metal ion response to the substrate shape preference of the ribozyme
    Tomoaki Ando
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Toyohashi, Aichi, Japan
    Biosci Biotechnol Biochem 67:2294-6. 2003
    ..Considering that the homologous E. coli tRNAs are resistant to internal cleavage by the RNase P, the phenomena suggest that this catalytic activity might take part in the removing the mis-folded RNAs in the cell...
  16. ncbi request reprint Comparative analyses of hairpin substrate recognition by Escherichia coli and Bacillus subtilis ribonuclease P ribozymes
    Tomoaki Ando
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku cho, Toyohashi, Aichi 441 8580, Japan
    Biosci Biotechnol Biochem 67:1825-7. 2003
    ..The results of kinetic studies showed that the metal ion concentration affected both the catalysis and the affinity of the ribozymes toward a hairpin RNA substrate...
  17. pmc Extracellular production of an RNA aptamer by ribonuclease-free marine bacteria harboring engineered plasmids: a proposal for industrial RNA drug production
    Hiromichi Suzuki
    Division of Life Science and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Toyohashi, Aichi 441 8580, Japan
    Appl Environ Microbiol 76:786-93. 2010
    ..This is the first demonstration of extracellular production of a functional artificial RNA in vivo, which will pave the way for inexpensive production of RNA drugs...
  18. ncbi request reprint Substrate shape specificity of E coli RNase P ribozyme is dependent on the concentration of magnesium ion
    Tomoaki Ando
    Department of Ecological Engineering, Toyohashi University of Technology, Tempaku cho, Toyohashi, Aichi 441 8580
    J Biochem 133:445-51. 2003
    ..Additional studies using another hairpin substrate demonstrated the same tendency. Our data strongly suggest that raising the concentration of metal ion induces a conformational change in the RNA enzyme...
  19. ncbi request reprint Mutational analysis of the length of the J3/4 domain of Escherichia coli ribonuclease P ribozyme
    Shinnosuke Haga
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempakkucho, Toyohashi, Aichi 441 8580, Japan
    Biosci Biotechnol Biochem 68:2630-2. 2004
    ..Our data indicate that the conserved AGGA sequence was important for efficient ribozyme reactions, and suggested that the length mutations affected ribozyme activity through metal ion binding steps...
  20. ncbi request reprint Porphyrins and porphines bind strongly and specifically to tRNA, precursor tRNA and to M1 RNA and inhibit the ribonuclease P ribozyme reaction
    Yoshiaki Hori
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku cho, Toyohashi, 441 8580, Japan
    Biochim Biophys Acta 1730:47-55. 2005
    ....
  21. doi request reprint Artificial RNA aptamer production by the marine bacterium Rhodovulum sulfidophilum: improvement of the aptamer yield using a mutated transcriptional promoter
    Hiromichi Suzuki
    Division of Bioscience and Biotechnology, Department of Environmental and Life Sciences, Toyohashi University of Technology, Tempaku cho, Toyohashi, Aichi 441 8580, Japan
    J Biosci Bioeng 112:458-61. 2011
    ..Using this system, the extracellular RNA aptamer of approximately 200 ng and the total RNA aptamer (both extra- and intracellular form) of about 20 μg from 1 L culture were accomplished by constitutive expression of the gene...
  22. ncbi request reprint Porphyrins and porphines inhibit the ribonuclease P reaction in vitro
    Yoshiaki Hori
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku cho, Toyohashi, Aichi 441 8580, Japan
    Nucleic Acids Res Suppl . 2002
    ..In addition to the benzimidazole inhibition that we have previously reported, these unusual substrate-binding inhibitions may provide new leads for the novel anti-bacterial reagent design...
  23. ncbi request reprint Mutational analyses of neighboring domains of active center of RNase P ribozyme
    Terumichi Tanaka
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempakucho, Toyohashi, Aichi 441 8580, Japan
    Nucleic Acids Symp Ser (Oxf) . 2004
    ..The results indicated that mutations in these domains did not affect the cleavage site selection of the enzyme, but affected cleavage efficiencies and dependence on magnesium ion concentrations...
  24. ncbi request reprint Extracellular tRNAs of the marine photosynthetic bacterium Rhodovulum sulfidophilum are not aminoacylated
    Hiromichi Suzuki
    Division of Life Science and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Aichi, Japan
    Biosci Biotechnol Biochem 73:425-7. 2009
    ..Most of the tRNAs have mature 3'-terminal CCA sequences. In the present study we found that these extracellular tRNAs were not aminoacylated, although almost all intracellular tRNAs are aminoacylated...
  25. ncbi request reprint In vitro hyperprocessing of Drosophila tRNAs by the catalytic RNA of RNase P the cloverleaf structure of tRNA is not always stable?
    Y Hori
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku cho, Toyohashi, Japan
    Eur J Biochem 267:4781-8. 2000
    ..We show here that M1 RNA can be used as a powerful tool to detect the alternative conformation of tRNAs. The relationship between these hyperprocessing reactions and stability of the tRNA structure will also be discussed...
  26. ncbi request reprint Recognition of tRNA bottom half by bacterial ribonuclease P
    Yasuhiro Nagai
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Hibarigaoka 1 1, Tempaku cho, Toyohashi, Aichi 441 8580, Japan
    Nucleic Acids Res Suppl . 2003
    ..We also found that RNase P holoenzyme prefered somewhat mutated tRNA precursor to the wild-type tRNA precursor...
  27. doi request reprint Characterization of extracellular DNA production and flocculation of the marine photosynthetic bacterium Rhodovulum sulfidophilum
    Hiromichi Suzuki
    Division of Life Science and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Toyohashi, Aichi, 441 8580, Japan
    Appl Microbiol Biotechnol 84:349-56. 2009
    ..In the presence of alpha-cyclodextrin, the floc was rapidly degraded and extracellular soluble DNA production increased...
  28. ncbi request reprint The natural intron sequence of human tyrosine pre-transfer RNA is not a temporal stabilizer for cloverleaf structure
    Tomoaki Ando
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempakucho, Toyohashi, Aichi 441 8580, Japan
    Biosci Biotechnol Biochem 68:1782-5. 2004
    ..Our data suggested that the contemporary intron sequence may be a vestige of the ancient pre-biotic world, but not has been retained as a temporal stabilizer of the pre-tRNA before the base modifications...
  29. ncbi request reprint Human tyrosine tRNA is also internally cleavable by E. coli ribonuclease P RNA ribozyme in vitro
    T Ando
    Department of Ecological Engineering, Toyohashi University of Technology, Aichi, Japan
    Biosci Biotechnol Biochem 65:2798-801. 2001
    ..coli RNase P RNA. This tRNA is the first example for hyperprocessed non-Drosophila tRNAs. The results suggest that the hyperprocessing reaction can be a useful tool detect destablized tRNA molecules from any species...
  30. ncbi request reprint Regulation of ribozyme activity by engineered protein switch
    Terumichi Tanaka
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempakucho, Toyohashi, Aichi 441 8580, Japan
    Nucleic Acids Symp Ser (Oxf) . 2005
    ..Our results showed that the P3 domain of this enzyme can be engineered, and addition of some heterologous protein subunits can also be done to this domain...
  31. doi request reprint Substrate recognition of pre-tRNA by ribonuclease P---subsite model of natural ribozyme originated from Escherichia coli
    Akihiro Fujimoto
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Toyohashi, Aichi 441 8580, Japan
    Nucleic Acids Symp Ser (Oxf) . 2009
    ..In the meeting, we will show the possibility that the S-domain can contribute to stabilize the transition state of the cleavage reaction of a pre-tRNA substrate...
  32. ncbi request reprint Bacterial ribonuclease P reaction is affected by substrate shape and magnesium ion concentration
    Tomoaki Ando
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku cho, Toyohashi shi, Aichi 441 8580, Japan
    Nucleic Acids Res Suppl . 2003
    ..We also examined the effect of the protein component of the E. coli RNase P. Under the conditions tested, magnesium ion concentration dependency to substrate shape recognition was not observed when the holo enzyme was used...
  33. ncbi request reprint Revisiting the substrate recognition of bacterial ribonuclease P: in the view of the recognition of the base N73 in the substrate
    Terumichi Tanaka
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku cho, Toyohashi, Aichi 441 8580, Japan
    Nucleic Acids Res Suppl . 2003
    ....
  34. ncbi request reprint Characterization of extracellular RNAs produced by the marine photosynthetic bacterium Rhodovulum sulfidophilum
    Tomoaki Ando
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku cho, Toyohashi, Aichi 441 8580
    J Biochem 139:805-11. 2006
    ..Analyses of modified bases and genes of the RNAs revealed no structural difference between the intracellular and extracellular RNAs. This is the first report of structural analyses of bacterial extracellular RNAs...
  35. ncbi request reprint Mutational analysis on the S-domain of bacterial ribonuclease P ribozyme
    Terumichi Tanaka
    Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi Universitry of Technology, Tempakucho, Toyohashi, Aichi 441 8580, Japan
    Nucleic Acids Symp Ser (Oxf) . 2007
    ..The results showed the P12 and P13 domains are necessary for efficient enzymatic reactions and the absence of P14 and P17 domains are easily rescued by the presence of high concentration of magnesium ions...
  36. ncbi request reprint Molecular cloning and nucleotide sequence of Thermus thermophilus HB8 trpE and trpG
    S Sato
    Mitsubishi Kasei Institute of Life Sciences, Tokyo, Japan
    Biochim Biophys Acta 950:303-12. 1988
    ..The amino-acid sequences of the T. themophilus anthranilate synthase I and II deduced from the nucleotide sequence were compared with those of other organisms...
  37. ncbi request reprint Synthesis of bacterial magnetic particles during cell cycle of Magnetospirillum magneticum AMB-1
    C D Yang
    Department of Biotechnology, Tokyo University of Agriculture and Technology, Koganei, Japan
    Appl Biochem Biotechnol 91:155-60. 2001
    ..A sharp increase in BMPs occurred just before cell division and resulted in maximum BMP production of 30 particles/cell. The transcription of magA was regulated immediately before and after cell division...
  38. ncbi request reprint Adenovirus-mediated transduction of Escherichia coli uracil phosphoribosyltransferase gene sensitizes cancer cells to low concentrations of 5-fluorouracil
    F Kanai
    Second Department of Internal Medicine, Faculty of Medicine, The University of Tokyo, Japan
    Cancer Res 58:1946-51. 1998
    ..The adenovirus vector transduction of the UPRT gene followed by 5-FU administration is representative of a new chemosensitization strategy for cancer gene therapy...
  39. pmc Isolation of a novel human gene, MARKL1, homologous to MARK3 and its involvement in hepatocellular carcinogenesis
    T Kato
    Laboratory of Molecular Medicine, Human Genome Center, Institute of Medical Science, The University of Tokyo, Tokyo, Japan
    Neoplasia 3:4-9. 2001
    ..Expression levels of MARKL1 were markedly elevated in eight of nine HCCs in which nuclear accumulation of beta-catenin were observed, which may suggest that MARKL1 plays some role in hepatocellular carcinogenesis...
  40. ncbi request reprint Possible role of hepatic glutathione in transport of methylmercury into mouse kidney
    A Naganuma
    Department of Public Health, School of Pharmaceutical Sciences, Kitasato University, Tokyo, Japan
    Biochem Pharmacol 37:291-6. 1988
    ....
  41. ncbi request reprint Sequence analysis of hepatitis C virus isolated from a fulminant hepatitis patient
    T Kato
    Department of Microbiology, Tokyo Metropolitan Institute of Neuroscience, Tokyo, Japan
    J Med Virol 64:334-9. 2001
    ....
  42. ncbi request reprint Production of luciferase-magnetic particle complex by recombinant Magnetospirillum sp. AMB-1
    T Matsunaga
    Department of Biotechnology, Tokyo University of Agriculture and Technology, 2 24 16, Naka cho, Koganei, Tokyo 184 8588, Japan
    Biotechnol Bioeng 70:704-9. 2000
    ..Magnetite production by fed-batch culture of AMB-1 was about 3 times that obtained by batch culture. There were no significant differences in BMPs yield between recombinant AMB-1 cultivated by fed-batch culture and wild type of AMB-1...
  43. ncbi request reprint Hepatitis C virus population dynamics in human lymphocytes and hepatocytes infected in vitro
    N Kato
    Virology Division, National Cancer Center Research Institute, Tokyo, Japan
    J Gen Virol 79:1859-69. 1998
    ..Following a comparison of the sequences, 11 amino acids were identified as candidates for determinants of the cell tropism of HCV...
  44. ncbi request reprint Characterization of hypervariable region in hepatitis C virus envelope protein during acute and chronic infection
    K Higashi
    Department of Microbiology and Cell Biology, The Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan
    Arch Virol 150:883-98. 2005
    ..The sequence variation in HVR-1 may instead indicate the existence of various clones in acute phase infection and the adaption of these clones is thought to have caused persistent and chronic infection in each patient...
  45. ncbi request reprint Cloning, functional expression and tissue distribution of human cDNA for the alpha 1C-adrenergic receptor
    A Hirasawa
    Department of Molecular, Cell Pharmacology, National Children s Medical Research Center, Tokyo, Japan
    Biochem Biophys Res Commun 195:902-9. 1993
    ..The data show that the clone P2C4 encodes a human alpha 1C-adrenergic receptor cDNA, and the receptor subtype is expressed not widely but localized in several human tissues...
  46. ncbi request reprint Albumin induces endoplasmic reticulum stress and apoptosis in renal proximal tubular cells
    T Ohse
    Division of Nephrology and Endocrinology, University of Tokyo School of Medicine, Tokyo, Japan
    Kidney Int 70:1447-55. 2006
    ..In conclusion, renal tubular cells exposed to high protein load suffer from ER stress. ER stress may subsequently lead to tubular damage by activation of caspase-12...
  47. ncbi request reprint Cloning, functional expression and tissue distribution of human alpha 1c-adrenoceptor splice variants
    A Hirasawa
    Department of Molecular, Cell Pharmacology, National Children s Medical Research Center, Tokyo, Japan
    FEBS Lett 363:256-60. 1995
    ..Despite the structural differences, functional experiments in transfected CHO cells showed that the three isoforms have similar ligand binding properties, and all couple with phospholipase C/Ca2+ signaling pathway...