The Control Layer

Part of the Biological and Medical Physics, Biomedical Engineering book series (BIOMEDICAL)


Alpha Helix Ramachandran Plot Control Layer Chromosome Territory Phosphoryl Group 
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General References

  1. Alberts B, Johnson A, Lewis J, Raff M, Roberts K, and Walker P [2002]. Molecular Biology of the Cell, 4th edition. New York: Garland Publishers.Google Scholar
  2. Matthews CK, van Holde KE, and Ahem KG [2000]. Biochemistry, 3rd edition. San Francisco: Pearson Benjamin Cummings.Google Scholar
  3. Stryer L [1995]. Biochemistry, 4th edition. New York: W.H. Freeman and Company.Google Scholar

References and Further Reading Chromatin and the Nucleosome

  1. Harp JM, et al. [2000]. Asymmetries in the nucleosome core particle at 2.5 Å resolution. Acta Cryst., D56: 1513–1534.Google Scholar
  2. Kornberg RD, and Lorch YL [1999]. Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome. Cell, 98: 285–294.CrossRefGoogle Scholar

Nuclear Organization

  1. Lamond AI, and Earnshaw WC [1998]. Structure and function in the nucleus. Science, 280: 547–553.CrossRefGoogle Scholar
  2. Lewis JD, and Tollervey D [2000]. Like attracts like: Getting RNA processing together in the nucleus. Science, 288: 1385–1389.CrossRefADSGoogle Scholar

Chromosome Organization

  1. Cremer T, and Cremer C [2001]. Chromosome territories, nuclear architecture and gene regulation in mammalian cells. Nat. Rev. Genet., 2: 292–301.CrossRefGoogle Scholar
  2. Manuelidis L [1990]. A view of interphase chromosomes. Science, 250: 1533–1540.ADSCrossRefGoogle Scholar

Protein Organization

  1. Hovmöller S, Zhou T, and Ohlson T [2002]. Conformations of amino acids in proteins. Acta Cryst., D58: 768–776.Google Scholar
  2. Kleywegt GJ, and Jones TA [1996]. Phi/Psi-chology: Ramachandran revisited. Structure, 4: 1395–1400.CrossRefGoogle Scholar

Post-Translational Modifications

  1. Fortini ME [2000]. Fringe benefits to carbohydrates. Nature, 406: 357–358, and references cited therein.CrossRefADSGoogle Scholar
  2. McLaughlin S, and Aderem A [1995]. The myristoyl-electrostatic switch: A modulator of reversible protein-membrane interactions. Trends Biochem. Sci., 20: 272–276.CrossRefGoogle Scholar
  3. Milligan G, Parenti M, and Magee AI [1995]. The dynamical role of palmitoylation in signal transduction. Trends Biochem. Sci., 20: 181–186.CrossRefGoogle Scholar
  4. Peschon JJ, et al. [1998]. An essential role for ectodomain shedding in mammalian development. Science, 282: 1281–1284.CrossRefADSGoogle Scholar
  5. Resh MD [1999]. Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta, 1451:1–16.CrossRefGoogle Scholar

Regulated Proteolysis

  1. Brown MS, et al. [2000]. Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans. Cell, 100: 391–398.CrossRefGoogle Scholar
  2. Maniatis T [1999]. A ubiquitin ligase complex essential for the NF-B, Wnt/Wingless, and Hedgehog signaling pathways. Genes Dev., 13: 505–510.CrossRefGoogle Scholar
  3. Townsley FM, and Ruderman JV [1998]. Proteolytic ratchets that control progression through mitosis. Trends Cell Biol., 8: 238–244.CrossRefGoogle Scholar


  1. Müller S, et al. [2001]. SUMO, ubiquitin’s mysterious cousin. Nature Rev. Mol. Cell Biol., 2: 202–210.CrossRefGoogle Scholar

Histone Modifications

  1. Grunstein M [1997]. Histone acetylation in chromatin structure and transcription. Nature, 389: 349–352.CrossRefADSGoogle Scholar
  2. Jenuwein T, and Allis CD [2001]. Translating the histone code. Science, 293: 1074–1080.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, Inc. 2005

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