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    Article

    Phosphorylation of Connexin 43 by Cdk5 Modulates Neuronal Migration During Embryonic Brain Development

    The gap junction protein, connexin 43 (Cx43), is only present and abundantly expressed in astrocytes but is absent in neurons in the mature brain tissues. However, both the expression and function of Cx43 in n...

    Guang-Jian Qi, Qiang Chen, Li-Jun Chen, Yang Shu, Lu-Lu Bu in Molecular Neurobiology (2016)

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    Living Reference Work Entry In depth

    MOZ and MORF Lysine Acetyltransferases

    Jiang-** Zhang, **aoyu Du, Kezhi Yan in Encyclopedia of Signaling Molecules

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    Living Reference Work Entry In depth

    PCAF Lysine Acetyltransferase

    Linya You, Kezhi Yan, **ang-Jiao Yang in Encyclopedia of Signaling Molecules

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    Protocol

    Molecular and Functional Characterization of Histone Deacetylase 4 (HDAC4)

    Histone deacetylases (HDACs) regulate various nuclear and cytoplasmic processes. In mammals, these enzymes are divided into four classes, with class II further divided into two subclasses: IIa (HDAC4, HDAC5, H...

    Lin Li, **ang-Jiao Yang in Histone Deacetylases (2016)

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    Article

    Tubulin acetylation: responsible enzymes, biological functions and human diseases

    Microtubules have important functions ranging from maintenance of cell morphology to subcellular transport, cellular signaling, cell migration, and formation of cell polarity. At the organismal level, microtub...

    Lin Li, **ang-Jiao Yang in Cellular and Molecular Life Sciences (2015)

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    Reference Work Entry In depth

    MOZ and MORF Lysine Acetyltransferases

    Jiang-** Zhang, **aoyu Du, Dr. **ang-Jiao Yang in Encyclopedia of Signaling Molecules (2012)

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    Reference Work Entry In depth

    PCAF Lysine Acetyltransferase

    Linya You, Dr. **ang-Jiao Yang in Encyclopedia of Signaling Molecules (2012)

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    Chapter

    Covalent Protein Modification as a Mechanism for Dynamic Recruitment of Specific Interactors

    The dynamic interchange of information within a cell, which subsumes the regulation of protein function, activity and multiprotein complex membership, depends upon the flux of the sets of modifications of prot...

    Nicholas R. Bertos, Veena Sangwan in Post-Translational Modifications in Health… (2011)

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    Article

    The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men

  10. In the past decade, protein Lys acetylation has emerged as a major post-translational modification that occurs even in bacteria. This modification not only reg...

  11. **ang-Jiao Yang, Edward Seto in Nature Reviews Molecular Cell Biology (2008)

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    Article

    Multisite protein modification and intramolecular signaling

    Post-translational modification is a major mechanism by which protein function is regulated in eukaryotes. Instead of single-site action, many proteins such as histones, p53, RNA polymerase II, tubulin, Cdc25C...

    **ang-Jiao Yang in Oncogene (2005)

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    Article

    PCAF is a coactivator for p73-mediated transactivation

    The tumor suppressor p53-related p73 shares significant amino-acid sequence identity with p53. Like p53, p73 recognizes canonical p53 DNA-binding sites and activates p53-responsive target genes and induces apo...

    Lisa Y Zhao, Yue Liu, Nicholas R Bertos, **ang-Jiao Yang, Daiqing Liao in Oncogene (2003)

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    Article

    MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2

    The monocytic leukemia zinc finger protein MOZ and its homologue MORF have been implicated in leukemogenesis. Both MOZ and MORF are histone acetyltransferases with weak transcriptional repression domains and s...

    Nadine Pelletier, Nathalie Champagne, Stefano Stifani, **ang-Jiao Yang in Oncogene (2002)

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    Article

    The monocytic leukemia zinc finger protein MOZ is a histone acetyltransferase

    The monocytic leukemia zinc finger protein (MOZ) gene is rearranged in t(8;16)(p11;p13), t(8;22)(p11;q13) and inv(8)(p11q13) associated with acute myeloid leukemia. The other fusion partners involved are CBP, ...

    Nathalie Champagne, Nadine Pelletier, **ang-Jiao Yang in Oncogene (2001)

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