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2.4.9: D9. Recent References

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    64230
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    3. Dunker, A. et al. The unfoldomics decade: an update on intrinsically disordered proteins.BMC Genomics 2008, 9(Suppl 2):S1 doi:10.1186/1471-2164-9-S2-S1
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    5. Riemer, J. et al. Disulfide Formation in the ER and Mitochondria: Two Solutions to a Common Process. Science 324, 1284 (2009)
    6. Depuydt, M. et al. A Periplasmic Reducing System Protects Single Cysteine Residues from Oxidation. Science 326, 1109 (2009)
    7. Uversky, V & Dunker, A. Controlled Chaos. Science. 320, 1340 (2008)
    8. Bemporad, F. et al. Biological function in a non-native partially folded state of a protein. EMBO Journal 27, 1525 (2008)
    9. Murzin, A. Metamorphic Proteins. Science 320, 1725 (2008)
    10. Kimchi-Sarfaty, C. et al. A "Silent Polymorphism in the MDR1 Gene Alters Substrate Specificity. Science 315, 525 (2007)
    11. Religa, T. et al. Solution Structure of a protein denatured state and folding intermediate. Nature. 437, 1053 (2005)
    12. Cecconi et al. Direct Observation of the Three-State Folding of a Single Protein Molecule. Science 309, 2057 (2005)
    13. Krantz, B.A. et al. A Phenylalanine Clamp Catalyzes Protein Translocation Through the Anthrax Toxin Pore. Science 309, 777 (2005)
    14. Hessa, T. et al. Recognition of transmembrane helices by the endoplasmic reticulum translocon. Nature 433, 377 (2005)
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    24. Batey et al. Crystal structure of the ribonucleoprotein core of the signal recognition particle. (which binds newly synthesized proteins cotranslationally, arrests the synthesis, and docks the particle to the endoplasmic reticulum where synthesis restarts and the protein is discharged into the ER lumen for movement elsewhere in the cell). Science. 287, pg 1232 (2000)
    25. Shin et al. Interaction of partially unfolded forms of Torpedo acetylcholinesterase with liposomes. Protein Science. 5, pg 42 (1996)
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    This page titled 2.4.9: D9. Recent References is shared under a CC BY-NC-SA license and was authored, remixed, and/or curated by Henry Jakubowski.