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  1. Article ; Online: Mn

    Yonekura, Shin-Ichiro / Toyoshima, Chikashi

    FEBS letters

    2016  Volume 590, Issue 24, Page(s) 4650

    Language English
    Publishing date 2016-12
    Publishing country England
    Document type Journal Article ; Published Erratum
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1002/1873-3468.12524
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  2. Article ; Online: Mn(2+) transport by Ca(2+) -ATPase of sarcoplasmic reticulum.

    Yonekura, Shin-Ichiro / Toyoshima, Chikashi

    FEBS letters

    2016  Volume 590, Issue 14, Page(s) 2086–2095

    Abstract: Ca(2+) -ATPase of sarcoplasmic reticulum is known to pump Mn(2+) in addition to Ca(2+) , but whether its transport mechanism is identical to that of Ca(2+) is ambiguous. To clarify, we examined, by atomic absorption spectroscopy, competition between Mn(2+ ...

    Abstract Ca(2+) -ATPase of sarcoplasmic reticulum is known to pump Mn(2+) in addition to Ca(2+) , but whether its transport mechanism is identical to that of Ca(2+) is ambiguous. To clarify, we examined, by atomic absorption spectroscopy, competition between Mn(2+) and Ca(2+) in active transport using vesicles of sarcoplasmic reticulum (SR). Here, we demonstrate that Ca(2+) -ATPase transports Ca(2+) and Mn(2+) concomitantly but has a much lower affinity for Mn(2+) (apparent Kd ~ 0.5 mm). Stoichiometries of transported ions per ATP hydrolysed, Vmax values and activation energies are very similar. Altogether, Ca(2+) -ATPase appears to use the same mechanism for transporting Mn(2+) as that for Ca(2+) .
    MeSH term(s) Adenosine Triphosphate/metabolism ; Animals ; Ion Transport/physiology ; Manganese/metabolism ; Rabbits ; Sarcoplasmic Reticulum/enzymology ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/metabolism
    Chemical Substances Manganese (42Z2K6ZL8P) ; Adenosine Triphosphate (8L70Q75FXE) ; Sarcoplasmic Reticulum Calcium-Transporting ATPases (EC 3.6.3.8)
    Language English
    Publishing date 2016-07
    Publishing country England
    Document type Letter
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1002/1873-3468.12244
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Escherichia coli pyruvate:flavodoxin oxidoreductase, YdbK - regulation of expression and biological roles in protection against oxidative stress.

    Nakayama, Takayuki / Yonekura, Shin-Ichiro / Yonei, Shuji / Zhang-Akiyama, Qiu-Mei

    Genes & genetic systems

    2013  Volume 88, Issue 3, Page(s) 175–188

    Abstract: E. coli YdbK is predicted to be a pyruvate:flavodoxin oxidoreductase (PFOR). However, enzymatic activity and the regulation of gene expression of it are not well understood. In this study, we found that E. coli cells overexpressing the ydbK gene had ... ...

    Abstract E. coli YdbK is predicted to be a pyruvate:flavodoxin oxidoreductase (PFOR). However, enzymatic activity and the regulation of gene expression of it are not well understood. In this study, we found that E. coli cells overexpressing the ydbK gene had enhanced PFOR activity, indicating the product of ydbK to be a PFOR. The PFOR was labile to oxygen. The expression of ydbK was induced by superoxide generators such as methyl viologen (MV) in a SoxS-dependent manner after a lag period. We identified a critical element upstream of ydbK gene required for the induction by MV and proved direct binding of SoxS to the element. E. coli ydbK mutant was highly sensitive to MV, which was enhanced by additional inactivation of fpr gene encoding ferredoxin (flavodoxin):NADP(H) reductase (FPR). Aconitase activity, a superoxide sensor, was more extensively decreased by MV in the E. coli ydbK mutant than in wild-type strain. The induction level of soxS gene was higher in E. coli ydbK fpr double mutant than in wild-type strain. These results indicate that YdbK helps to protect cells from oxidative stress. It is possible that YdbK maintains the cellular redox state together with FPR and is involved in the reduction of oxidized proteins including SoxR in the late stages of the oxidative stress response in E. coli.
    MeSH term(s) Aconitate Hydratase/metabolism ; Amino Acid Motifs ; Base Sequence ; Escherichia coli/enzymology ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Ferredoxin-NADP Reductase/genetics ; Ferredoxin-NADP Reductase/metabolism ; Gene Expression Regulation, Bacterial ; Ketone Oxidoreductases/genetics ; Ketone Oxidoreductases/metabolism ; Molecular Sequence Data ; Mutagenesis ; Oxidation-Reduction ; Oxidative Stress ; Paraquat/pharmacology ; Promoter Regions, Genetic ; Superoxides/metabolism ; Trans-Activators/genetics ; Trans-Activators/metabolism
    Chemical Substances Escherichia coli Proteins ; Trans-Activators ; Superoxides (11062-77-4) ; SoxS protein, E coli (137804-82-1) ; Ferredoxin-NADP Reductase (EC 1.18.1.2) ; Ketone Oxidoreductases (EC 1.2.-) ; pyruvate-flavodoxin oxidoreductase (EC 1.2.99.-) ; Aconitate Hydratase (EC 4.2.1.3) ; Paraquat (PLG39H7695)
    Language English
    Publishing date 2013-08-30
    Publishing country Japan
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1323536-9
    ISSN 1880-5779 ; 1341-7568
    ISSN (online) 1880-5779
    ISSN 1341-7568
    DOI 10.1266/ggs.88.175
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: CiMutT, an asidian MutT homologue, has a 7, 8-dihydro-8-oxo-dGTP pyrophosphohydrolase activity responsible for sanitization of oxidized nucleotides in Ciona intestinalis.

    Yonekura, Shin-Ichiro / Sanada, U / Zhang-Akiyama, Qiu-Mei

    Genes & genetic systems

    2010  Volume 85, Issue 4, Page(s) 287–295

    Abstract: The oxidized nucleotide precursors 7, 8-dihydro-8-oxo-dGTP (8-oxo-dGTP) and 1, 2-dihydro-2-oxo-dATP (2-oxo-dATP) are readily incorporated into nascent DNA strands during replication, which would cause base substitution mutations. E. coli MutT and human ... ...

    Abstract The oxidized nucleotide precursors 7, 8-dihydro-8-oxo-dGTP (8-oxo-dGTP) and 1, 2-dihydro-2-oxo-dATP (2-oxo-dATP) are readily incorporated into nascent DNA strands during replication, which would cause base substitution mutations. E. coli MutT and human homologue hMTH1 hydrolyze 8-oxo-dGTP, thereby preventing mutations. In this study, we searched for hMTH1 homologues in the ascidian Ciona intestinalis using the NCBI-BLAST database. Among several candidates, we focused on one open reading frame, designated as CiMutT, because of its high degree of identity (41.7%) and similarity (58.3%) to the overall amino acid sequence of hMTH1, including the Nudix box. CiMutT significantly suppressed the mutator activity of E. coli mutT mutant. Purified CiMutT had a pyrophosphohydrolase activity that hydrolyzed 8-oxo-dGTP to 8-oxo-dGMP and inorganic pyrophosphate. It had a pH optimum of 9.5 and Mg(++) requirement with optimal activity at 5 mM. The activity of CiMutT for 8-oxo-dGTP was comparable to that of hMTH1, while it was 100-fold lower for 2-oxo-dATP than that of hMTH1. These facts indicate that CiMutT is a functional homologue of E. coli MutT. In addition, the enzyme hydrolyzed all four of the unoxidized nucleoside triphosphates, with a preference for dATP. The specific activity for 8-oxo-dGTP was greater than that for unoxidized dATP and dGTP. These results suggest that CiMutT has the potential to prevent mutations by 8-oxo-dGTP in C. intestinalis.
    MeSH term(s) Amino Acid Sequence ; Animals ; Ciona intestinalis/enzymology ; DNA Repair ; DNA Repair Enzymes/biosynthesis ; DNA Repair Enzymes/genetics ; DNA Repair Enzymes/isolation & purification ; Deoxyadenine Nucleotides/metabolism ; Deoxyguanine Nucleotides/metabolism ; Escherichia coli Proteins/genetics ; Humans ; Molecular Sequence Data ; Mutation ; Phosphoric Monoester Hydrolases/biosynthesis ; Phosphoric Monoester Hydrolases/genetics ; Phosphoric Monoester Hydrolases/isolation & purification ; Pyrophosphatases/genetics ; Recombinant Fusion Proteins/biosynthesis ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/isolation & purification ; Sequence Alignment
    Chemical Substances 8-oxo-7,8-dihydrodeoxyguanosine diphosphate ; 8-oxodeoxyadenosine triphosphate ; Deoxyadenine Nucleotides ; Deoxyguanine Nucleotides ; Escherichia coli Proteins ; Recombinant Fusion Proteins ; 8-oxodeoxyguanosine triphosphate (139307-94-1) ; Phosphoric Monoester Hydrolases (EC 3.1.3.2) ; Pyrophosphatases (EC 3.6.1.-) ; mutT protein, E coli (EC 3.6.1.-) ; 8-oxodGTPase (EC 3.6.1.55) ; DNA Repair Enzymes (EC 6.5.1.-)
    Language English
    Publishing date 2010-12-17
    Publishing country Japan
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1323536-9
    ISSN 1880-5779 ; 1341-7568
    ISSN (online) 1880-5779
    ISSN 1341-7568
    DOI 10.1266/ggs.85.287
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Trinitrophenyl derivatives bind differently from parent adenine nucleotides to Ca2+-ATPase in the absence of Ca2+.

    Toyoshima, Chikashi / Yonekura, Shin-Ichiro / Tsueda, Junko / Iwasawa, Shiho

    Proceedings of the National Academy of Sciences of the United States of America

    2011  Volume 108, Issue 5, Page(s) 1833–1838

    Abstract: Trinitrophenyl derivatives of adenine nucleotides are widely used for probing ATP-binding sites. Here we describe crystal structures of Ca(2+)-ATPase, a representative P-type ATPase, in the absence of Ca(2+) with bound ATP, trinitrophenyl-ATP, -ADP, and - ...

    Abstract Trinitrophenyl derivatives of adenine nucleotides are widely used for probing ATP-binding sites. Here we describe crystal structures of Ca(2+)-ATPase, a representative P-type ATPase, in the absence of Ca(2+) with bound ATP, trinitrophenyl-ATP, -ADP, and -AMP at better than 2.4-Å resolution, stabilized with thapsigargin, a potent inhibitor. These crystal structures show that the binding mode of the trinitrophenyl derivatives is distinctly different from the parent adenine nucleotides. The adenine binding pocket in the nucleotide binding domain of Ca(2+)-ATPase is now occupied by the trinitrophenyl group, and the side chains of two arginines sandwich the adenine ring, accounting for the much higher affinities of the trinitrophenyl derivatives. Trinitrophenyl nucleotides exhibit a pronounced fluorescence in the E2P ground state but not in the other E2 states. Crystal structures of the E2P and E2 ∼ P analogues of Ca(2+)-ATPase with bound trinitrophenyl-AMP show that different arrangements of the three cytoplasmic domains alter the orientation and water accessibility of the trinitrophenyl group, explaining the origin of "superfluorescence." Thus, the crystal structures demonstrate that ATP and its derivatives are highly adaptable to a wide range of site topologies stabilized by a variety of interactions.
    MeSH term(s) Adenine Nucleotides/metabolism ; Calcium/metabolism ; Calcium-Transporting ATPases/metabolism ; Crystallization ; Models, Molecular ; Molecular Sequence Data ; Protein Binding ; Trinitrobenzenes/metabolism
    Chemical Substances Adenine Nucleotides ; Trinitrobenzenes ; Calcium-Transporting ATPases (EC 7.2.2.10) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2011-01-14
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1017659108
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    Zs.A 1148: Show issues Location:
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  6. Article: Functional analysis of SERCA1b, a highly expressed SERCA1 variant in myotonic dystrophy type 1 muscle.

    Zhao, Yimeng / Ogawa, Haruo / Yonekura, Shin-Ichiro / Mitsuhashi, Hiroaki / Mitsuhashi, Satomi / Nishino, Ichizo / Toyoshima, Chikashi / Ishiura, Shoichi

    Biochimica et biophysica acta

    2015  Volume 1852, Issue 10 Pt A, Page(s) 2042–2047

    Abstract: Myotonic dystrophy type 1 (DM1) is a genetic disorder in which multiple genes are aberrantly spliced. Sarco/endoplasmic reticulum Ca(2+)-ATPase 1 (SERCA1) is one of these genes, and it encodes a P-type ATPase. SERCA1 transports Ca(2+) from the cytosol to ...

    Abstract Myotonic dystrophy type 1 (DM1) is a genetic disorder in which multiple genes are aberrantly spliced. Sarco/endoplasmic reticulum Ca(2+)-ATPase 1 (SERCA1) is one of these genes, and it encodes a P-type ATPase. SERCA1 transports Ca(2+) from the cytosol to the lumen, and is involved in muscular relaxation. It has two splice variants (SERCA1a and SERCA1b) that differ in the last eight amino acids, and the contribution of these variants to DM1 pathology is unclear. Here, we show that SERCA1b protein is highly expressed in DM1 muscle tissue, mainly localised at fast twitch fibres. Additionally, when SERCA1a and SERCA1b were overexpressed in cells, we found that the ATPase and Ca(2+) uptake activity of SERCA1a was almost double that of SERCA1b. Although the affinity for both ATP and Ca(2+) was similar between the two variants, SERCA1b was more sensitive to the inner microsomal environment. Thus, we hypothesise that aberrant expression of SERCA1b in DM1 patients is the cause of abnormal intracellular Ca(2+) homeostasis.
    Language English
    Publishing date 2015-10
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbadis.2015.07.006
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  7. Article ; Online: Structural and functional properties of CiNTH, an endonuclease III homologue of the ascidian Ciona intestinalis: critical role of N-terminal region.

    Kato, Seiji / Hashiguchi, Kazunari / Igarashi, Kento / Moriwaki, Takahito / Yonekura, Shin-Ichiro / Zhang-Akiyama, Qiu-Mei

    Genes & genetic systems

    2012  Volume 87, Issue 2, Page(s) 115–124

    Abstract: Oxidatively damaged bases in DNA can cause cell death, mutation and/or cancer induction. To overcome such deleterious effects of DNA base oxidation, cells are equipped with base excision repair (BER) initiated by DNA glycosylases. Endonuclease III (Nth), ...

    Abstract Oxidatively damaged bases in DNA can cause cell death, mutation and/or cancer induction. To overcome such deleterious effects of DNA base oxidation, cells are equipped with base excision repair (BER) initiated by DNA glycosylases. Endonuclease III (Nth), a major DNA glycosylase, mainly excises oxidatively damaged pyrimidines from DNA. The aims of this study were to obtain an overview of the repair mechanism of oxidatively damaged bases and to elucidate the function of BER in maintaining genome stability during embryogenesis and development. In this study, we used the ascidian Ciona intestinalis because at every developmental stage it is possible to observe the phenotype of individuals with DNA damage or mutations. Sequence alignment analysis revealed that the amino acid sequence of Ciona intestinalis Nth homologue (CiNTH) had high homology with those of Escherichia coli, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Caenorhabditis elegans and human Nth homologues. It was evident that two domains, the Helix-hairpin-Helix and 4Fe-4S cluster domains that are critical regions for the Nth activity, are well conserved in CiNTH. CiNTH efficiently complemented the sensitivity of E. coli nth nei mutant to H(2)O(2). CiNTH was bifunctional, with DNA glycosylase and AP lyase activities. It removed thymine glycol, 5-formyluracil and 8-oxoguanine paired with G from DNA via a β-elimination reaction. Interestingly, the N-terminal 44 amino acids were essential for the DNA glycosylase activity of CiNTH.
    MeSH term(s) Amino Acid Sequence ; Animals ; Ciona intestinalis/genetics ; Ciona intestinalis/metabolism ; DNA/genetics ; DNA Damage ; DNA Glycosylases/genetics ; DNA Glycosylases/metabolism ; DNA Repair ; Deoxyribonuclease (Pyrimidine Dimer)/genetics ; Deoxyribonuclease (Pyrimidine Dimer)/metabolism ; Escherichia coli/genetics ; Gene Expression Regulation ; Guanine/analogs & derivatives ; Guanine/metabolism ; Humans ; Hydrogen Peroxide/metabolism ; Molecular Sequence Data ; Reactive Oxygen Species ; Sequence Alignment ; Thymine/analogs & derivatives ; Thymine/metabolism ; Uracil/analogs & derivatives ; Uracil/metabolism
    Chemical Substances Reactive Oxygen Species ; 5-formyluracil (1195-08-0) ; thymine glycol (2943-56-8) ; 8-hydroxyguanine (5614-64-2) ; Uracil (56HH86ZVCT) ; Guanine (5Z93L87A1R) ; DNA (9007-49-2) ; Hydrogen Peroxide (BBX060AN9V) ; Deoxyribonuclease (Pyrimidine Dimer) (EC 3.1.25.1) ; DNA Glycosylases (EC 3.2.2.-) ; Thymine (QR26YLT7LT)
    Language English
    Publishing date 2012-07-10
    Publishing country Japan
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1323536-9
    ISSN 1880-5779 ; 1341-7568
    ISSN (online) 1880-5779
    ISSN 1341-7568
    DOI 10.1266/ggs.87.115
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  8. Article: Trinitrophenyl derivatives bind differently from parent adenine nucleotides to Ca²⁺-ATPase in the absence of Ca²⁺

    Toyoshima, Chikashi / Yonekura, Shin-Ichiro / Tsueda, Junko / Iwasawa, Shiho

    Proceedings of the National Academy of Sciences of the United States of America. 2011 Feb. 1, v. 108, no. 5

    2011  

    Abstract: Trinitrophenyl derivatives of adenine nucleotides are widely used for probing ATP-binding sites. Here we describe crystal structures of Ca²⁺-ATPase, a representative P-type ATPase, in the absence of Ca²⁺ with bound ATP, trinitrophenyl-ATP, -ADP, ... ...

    Abstract Trinitrophenyl derivatives of adenine nucleotides are widely used for probing ATP-binding sites. Here we describe crystal structures of Ca²⁺-ATPase, a representative P-type ATPase, in the absence of Ca²⁺ with bound ATP, trinitrophenyl-ATP, -ADP, and -AMP at better than 2.4-Å resolution, stabilized with thapsigargin, a potent inhibitor. These crystal structures show that the binding mode of the trinitrophenyl derivatives is distinctly different from the parent adenine nucleotides. The adenine binding pocket in the nucleotide binding domain of Ca²⁺-ATPase is now occupied by the trinitrophenyl group, and the side chains of two arginines sandwich the adenine ring, accounting for the much higher affinities of the trinitrophenyl derivatives. Trinitrophenyl nucleotides exhibit a pronounced fluorescence in the E2P ground state but not in the other E2 states. Crystal structures of the E2P and E2
    Keywords Ca2-transporting ATPase ; adenine ; adenosine triphosphate ; adenosinetriphosphatase ; calcium ; crystal structure ; fluorescence
    Language English
    Dates of publication 2011-0201
    Size p. 1833-1838.
    Publishing place National Academy of Sciences
    Document type Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1017659108
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  9. Article: Generation, biological consequences and repair mechanisms of cytosine deamination in DNA.

    Yonekura, Shin-Ichiro / Nakamura, Nobuya / Yonei, Shuji / Zhang-Akiyama, Qiu-Mei

    Journal of radiation research

    2008  Volume 50, Issue 1, Page(s) 19–26

    Abstract: Base moieties in DNA are spontaneously threatened by naturally occurring chemical reactions such as deamination, hydrolysis and oxidation. These DNA modifications have been considered to be major causes of cell death, mutations and cancer induction in ... ...

    Abstract Base moieties in DNA are spontaneously threatened by naturally occurring chemical reactions such as deamination, hydrolysis and oxidation. These DNA modifications have been considered to be major causes of cell death, mutations and cancer induction in organisms. Organisms have developed the DNA base excision repair pathway as a defense mechanism to protect them from these threats. DNA glycosylases, the key enzyme in the base excision repair pathway, are highly conserved in evolution. Uracil constantly occurs in DNA. Uracil in DNA arises by spontaneous deamination of cytosine to generate pro-mutagenic U:G mispairs. Uracil in DNA is also produced by the incorporation of dUMP during DNA replication. Uracil-DNA glycosylase (UNG) acts as a major repair enzyme that protects DNA from the deleterious consequences of uracil. The first UNG activity was discovered in E. coli in 1974. This was also the first discovery of base excision repair. The sequence encoded by the ung gene demonstrates that the E. coli UNG is highly conserved in viruses, bacteria, archaea, yeast, mice and humans. In this review, we will focus on central and recent findings on the generation, biological consequences and repair mechanisms of uracil in DNA and on the biological significance of uracil-DNA glycosylase.
    MeSH term(s) Animals ; Arabinofuranosyluracil/metabolism ; Computer Simulation ; DNA Damage/physiology ; DNA Repair/physiology ; DNA Repair/radiation effects ; Humans ; Models, Biological ; Uracil-DNA Glycosidase/metabolism
    Chemical Substances Arabinofuranosyluracil (3083-77-0) ; Uracil-DNA Glycosidase (EC 3.2.2.-)
    Language English
    Publishing date 2008-11-06
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 603983-2
    ISSN 0449-3060
    ISSN 0449-3060
    DOI 10.1269/jrr.08080
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    Zs.B 388: Show issues Location:
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  10. Article: [Biological consequences and base excision repair mechanisms of oxidative base damage in DNA].

    Zhang, Qiu Mei / Nakamura, Nobuya / Yonekura, Shin-Ichiro / Yonei, Shuji / Zhang, Qui-Mei / Yonekura, Shin-Ichiro

    Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme

    2005  Volume 50, Issue 4, Page(s) 322–329

    MeSH term(s) Animals ; DNA/metabolism ; DNA Damage/genetics ; DNA Glycosylases/physiology ; DNA Repair/genetics ; Guanine/analogs & derivatives ; Guanine/metabolism ; Humans ; Mutation/genetics ; Oxidative Stress/genetics ; Reactive Oxygen Species ; Thymine/metabolism
    Chemical Substances Reactive Oxygen Species ; 8-hydroxyguanine (5614-64-2) ; Guanine (5Z93L87A1R) ; DNA (9007-49-2) ; DNA Glycosylases (EC 3.2.2.-) ; Thymine (QR26YLT7LT)
    Language Japanese
    Publishing date 2005-04
    Publishing country Japan
    Document type Journal Article ; Review
    ZDB-ID 391163-9
    ISSN 0039-9450
    ISSN 0039-9450
    Database MEDical Literature Analysis and Retrieval System OnLINE

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