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  1. Artikel ; Online: A convenient preparation of N (ε)-methyl-L-lysine derivatives and its application to the synthesis of histone tail peptides.

    Chi, Hongfang / Islam, Md Shahidul / Nsiama, Tienabe K / Kato, Tamaki / Nishino, Norikazu

    Amino acids

    2014  Band 46, Heft 5, Seite(n) 1305–1311

    Abstract: A convenient route is established for the preparation of N (α)-Fmoc-N (ε)-(Boc, methyl)-L-lysine and N (α)-Fmoc-N (ε)-dimethyl-L-lysine as building blocks to be used for the synthesis of methylated peptides. This methodology is based on the use of ... ...

    Abstract A convenient route is established for the preparation of N (α)-Fmoc-N (ε)-(Boc, methyl)-L-lysine and N (α)-Fmoc-N (ε)-dimethyl-L-lysine as building blocks to be used for the synthesis of methylated peptides. This methodology is based on the use of malonate derivatives and dibromobutane to produce key intermediates, L-2-amino-6-bromohexanoic acid derivatives, which could be modified to the required group at the ε-position. Fmoc-protection is accessible, so these compounds can be used in solution as well as in solid-phase peptide synthesis. Also the peptides containing these methylated lysines have been proved to resist the action of trypsin and lysyl endopeptidase. Thus, this new method could be considered as an improvement of the synthesis of N (ε)-methyl-L-lysine derivatives.
    Mesh-Begriff(e) Histones/chemical synthesis ; Histones/chemistry ; Lysine/analogs & derivatives ; Lysine/chemistry ; Molecular Structure ; Peptides/chemical synthesis ; Peptides/chemistry ; Solid-Phase Synthesis Techniques/methods
    Chemische Substanzen Histones ; Peptides ; Lysine (K3Z4F929H6)
    Sprache Englisch
    Erscheinungsdatum 2014-05
    Erscheinungsland Austria
    Dokumenttyp Evaluation Studies ; Journal Article
    ZDB-ID 1121341-3
    ISSN 1438-2199 ; 0939-4451
    ISSN (online) 1438-2199
    ISSN 0939-4451
    DOI 10.1007/s00726-014-1690-6
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 3490: Hefte anzeigen Standort:
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    Jg. 1995 - 2021: Lesesall (2.OG)
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  2. Artikel ; Online: Design and synthesis of peptide-MCA substrates for a novel assay of histone methyltransferases and their inhibitors.

    Chi, Hongfang / Takemoto, Yasushi / Nsiama, Tienabe K / Kato, Tamaki / Nishino, Norikazu / Ito, Akihiro / Yoshida, Minoru

    Bioorganic & medicinal chemistry

    2014  Band 22, Heft 4, Seite(n) 1268–1275

    Abstract: Histone methyltransferases (HMTs) play an important role in controlling gene expression through site-specific methylation of lysines in core and linker histones within chromatin. As the typical HMTs, G9a and Set7/9 have been intensively studied that G9a ... ...

    Abstract Histone methyltransferases (HMTs) play an important role in controlling gene expression through site-specific methylation of lysines in core and linker histones within chromatin. As the typical HMTs, G9a and Set7/9 have been intensively studied that G9a is specific to the methylation at H3K9 and H3K27 and represses transcription, while Set7/9 methylates at H3K4. In this report we prepared various peptide-MCAs (4-methylcoumaryl-7-amides) related to histone tail and protein-substrates such as p53 and estrogen receptor-α. The fluorogenic substrates are applied for the assay of HMTs and an inhibitor, for example. The most sensitive and specific MCA-substrates to G9a and Set7/9 are discovered. The peptide-MCAs corresponding to the methylation sequences are promising for screening of HMT inhibitors.
    Mesh-Begriff(e) Amino Acid Sequence ; Coumarins/chemistry ; Drug Design ; Enzyme Activation/drug effects ; Enzyme Inhibitors/chemical synthesis ; Enzyme Inhibitors/pharmacology ; Histone-Lysine N-Methyltransferase/antagonists & inhibitors ; Histone-Lysine N-Methyltransferase/metabolism ; Humans ; Methylation ; Peptides/chemistry ; Substrate Specificity ; Transcription, Genetic/drug effects
    Chemische Substanzen 4-methyl-coumaryl-7-amide ; Coumarins ; Enzyme Inhibitors ; Peptides ; histone methyltransferase (EC 2.1.1.-) ; Histone-Lysine N-Methyltransferase (EC 2.1.1.43)
    Sprache Englisch
    Erscheinungsdatum 2014-02-15
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1161284-8
    ISSN 1464-3391 ; 0968-0896
    ISSN (online) 1464-3391
    ISSN 0968-0896
    DOI 10.1016/j.bmc.2014.01.011
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 3815: Hefte anzeigen Standort:
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    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
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  3. Artikel ; Online: Dynamics and regulation of lysine-acetylation during one-cell stage mouse embryos.

    Matsubara, Keigo / Lee, Ah Reum / Kishigami, Satoshi / Ito, Akio / Matsumoto, Kazuya / Chi, Hongfang / Nishino, Norikazu / Yoshida, Minoru / Hosoi, Yoshihiko

    Biochemical and biophysical research communications

    2013  Band 434, Heft 1, Seite(n) 1–7

    Abstract: Previous studies show that treatment of zygotes with trichostatin A (TSA), a histone deacetylase inhibitor (HDACi), impacts the subsequent development to a blastocyst as well as full-term development. To reveal the dynamics of protein acetylation, with ... ...

    Abstract Previous studies show that treatment of zygotes with trichostatin A (TSA), a histone deacetylase inhibitor (HDACi), impacts the subsequent development to a blastocyst as well as full-term development. To reveal the dynamics of protein acetylation, with and without TSA treatment during one-cell stage, we examined oocytes and zygotes by immunofluorescence and Western Blot analyses using anti-acetylated lysine and acetylated α-tubulin antibodies. In unfertilized oocytes, lysine acetylation level was extremely low over all but faintly detected in the spindle. Once oocyte activation occurs, a dramatic increase of lysine acetylation signal was observed mostly in the pronuclei and a fiber-like structure, the so called midbody, suggesting activation coupled up-regulation of lysine acetylation presumably in histones and α-tubulin. TSA treatment resulted in significantly more hyperacetylation not only in the midbody structure and pronuclei but also in the whole cytoplasm. Consistently, Western Blot analysis revealed that acetylation of proteins about 53 kDa and 11 kDa in size, corresponding to α-tubulin and histone H4 sizes respectively, were increased mainly after oocyte activation and exclusively enhanced by TSA treatment in zygotes. To confirm this behavior of acetylated nonhistone proteins, acetylated α-tubulin was examined and found to be faintly detected in the spindle of MII oocytes but later in whole in the cell of zygotes including the midbody, which was enhanced by TSA treatment. To elucidate the mechanism underlying up-regulation of lysine acetylation following oocyte activation, we assayed the HDAC activity, and found significant reduction of HDAC activity from MII to zygotic stages. Taken together, our data indicate that HDACs play an important role in maintaining low acetylated status in a MII oocyte. However, once an oocyte has been activated, histone and nonhistone proteins including α-tubulin are hyperacetylated partly due to a reduction of HDAC activity. TSA treatment of zygotes enhances their acetylation, which could affect subsequent embryonic development.
    Mesh-Begriff(e) Acetylation/drug effects ; Animals ; Female ; Fertilization in Vitro ; Histone Deacetylase Inhibitors/pharmacology ; Hydroxamic Acids/pharmacology ; Lysine/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Inbred DBA ; Oocytes/drug effects ; Oocytes/metabolism ; Protein Processing, Post-Translational/drug effects ; Tubulin/metabolism ; Up-Regulation/drug effects ; Zygote/drug effects ; Zygote/metabolism
    Chemische Substanzen Histone Deacetylase Inhibitors ; Hydroxamic Acids ; Tubulin ; trichostatin A (3X2S926L3Z) ; Lysine (K3Z4F929H6)
    Sprache Englisch
    Erscheinungsdatum 2013-04-26
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2013.03.083
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 116: Hefte anzeigen Standort:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  4. Artikel: Dynamics and regulation of lysine-acetylation during one-cell stage mouse embryos

    Matsubara, Keigo / Lee, Ah Reum / Kishigami, Satoshi / Ito, Akio / Matsumoto, Kazuya / Chi, Hongfang / Nishino, Norikazu / Yoshida, Minoru / Hosoi, Yoshihiko

    Biochemical and biophysical research communications. 2013 Apr. 26, v. 434, no. 1

    2013  

    Abstract: Previous studies show that treatment of zygotes with trichostatin A (TSA), a histone deacetylase inhibitor (HDACi), impacts the subsequent development to a blastocyst as well as full-term development. To reveal the dynamics of protein acetylation, with ... ...

    Abstract Previous studies show that treatment of zygotes with trichostatin A (TSA), a histone deacetylase inhibitor (HDACi), impacts the subsequent development to a blastocyst as well as full-term development. To reveal the dynamics of protein acetylation, with and without TSA treatment during one-cell stage, we examined oocytes and zygotes by immunofluorescence and Western Blot analyses using anti-acetylated lysine and acetylated α-tubulin antibodies. In unfertilized oocytes, lysine acetylation level was extremely low over all but faintly detected in the spindle. Once oocyte activation occurs, a dramatic increase of lysine acetylation signal was observed mostly in the pronuclei and a fiber-like structure, the so called midbody, suggesting activation coupled up-regulation of lysine acetylation presumably in histones and α-tubulin. TSA treatment resulted in significantly more hyperacetylation not only in the midbody structure and pronuclei but also in the whole cytoplasm. Consistently, Western Blot analysis revealed that acetylation of proteins about 53kDa and 11kDa in size, corresponding to α-tubulin and histone H4 sizes respectively, were increased mainly after oocyte activation and exclusively enhanced by TSA treatment in zygotes. To confirm this behavior of acetylated nonhistone proteins, acetylated α-tubulin was examined and found to be faintly detected in the spindle of MII oocytes but later in whole in the cell of zygotes including the midbody, which was enhanced by TSA treatment. To elucidate the mechanism underlying up-regulation of lysine acetylation following oocyte activation, we assayed the HDAC activity, and found significant reduction of HDAC activity from MII to zygotic stages. Taken together, our data indicate that HDACs play an important role in maintaining low acetylated status in a MII oocyte. However, once an oocyte has been activated, histone and nonhistone proteins including α-tubulin are hyperacetylated partly due to a reduction of HDAC activity. TSA treatment of zygotes enhances their acetylation, which could affect subsequent embryonic development.
    Schlagwörter Western blotting ; acetylation ; antibodies ; blastocyst ; cytoplasm ; embryogenesis ; fluorescent antibody technique ; histone deacetylase ; histones ; lysine ; mice ; oocytes ; pronucleus ; tubulin ; zygote
    Sprache Englisch
    Erscheinungsverlauf 2013-0426
    Umfang p. 1-7.
    Erscheinungsort Elsevier Inc.
    Dokumenttyp Artikel
    ZDB-ID 205723-2
    ISSN 0006-291X ; 0006-291X
    ISSN (online) 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2013.03.083
    Datenquelle NAL Katalog (AGRICOLA)

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    Verfügbar in ZB MED Bonn

    Z 71/706: Hefte anzeigen
    Z 3.8: Hefte anzeigen

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  5. Artikel: convenient preparation of N ε-methyl-L-lysine derivatives and its application to the synthesis of histone tail peptides

    Chi, Hongfang / Islam, Md. Shahidul / Nsiama, Tienabe K. / Kato, Tamaki / Nishino, Norikazu

    Amino acids

    Band v. 46,, Heft no. 5

    Abstract: A convenient route is established for the preparation of Nᵅ-Fmoc-Nᵋ-(Boc, methyl)-L-lysine and Nᵅ-Fmoc-Nᵋ-dimethyl-L-lysine as building blocks to be used for the synthesis of methylated peptides. This methodology is based on the use of malonate ... ...

    Abstract A convenient route is established for the preparation of Nᵅ-Fmoc-Nᵋ-(Boc, methyl)-L-lysine and Nᵅ-Fmoc-Nᵋ-dimethyl-L-lysine as building blocks to be used for the synthesis of methylated peptides. This methodology is based on the use of malonate derivatives and dibromobutane to produce key intermediates, L-2-amino-6-bromohexanoic acid derivatives, which could be modified to the required group at the ε-position. Fmoc-protection is accessible, so these compounds can be used in solution as well as in solid-phase peptide synthesis. Also the peptides containing these methylated lysines have been proved to resist the action of trypsin and lysyl endopeptidase. Thus, this new method could be considered as an improvement of the synthesis of Nᵋ-methyl-L-lysine derivatives.
    Schlagwörter trypsin ; histones ; peptides ; methodology
    Sprache Englisch
    Dokumenttyp Artikel
    ISSN 0939-4451
    Datenquelle AGRIS - International Information System for the Agricultural Sciences and Technology

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