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The Control Layer

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

Keywords

Alpha Helix Ramachandran Plot Control Layer Chromosome Territory Phosphoryl Group 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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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

Sumoylation

  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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