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Harvard Medical School |
Natalia Beglova |
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1. Beglova N, Fischer D, Hengge-Aronis R, Gehring K. 1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Escherichia coli GlgS protein. Eur J Biochem. 1997;246(2):301-10. 2. Beglova N, LeSauteur L, Ekiel I, Saragovi HU, Gehring K. Solution structure and internal motion of a bioactive peptide derived from nerve growth factor. J Biol Chem. 1998;273(37):23652-8. 3. LeSauteur L, Beglova N, Gehring K, Saragovi HU. Development and uses of small molecule ligands of TrkA receptors. In: In: Fisher A, Hanin I, Yoshida M, editors. Progress in Alzheimer's and Parkinson's diseases. Plenum Pub Corp;1998. p. 615-27. 4. Maliartchouk S, Debeir T, Beglova N, Cuello AC, Gehring K, Saragovi HU. Genuine monovalent ligands of TrkA nerve growth factor receptors reveal a novel pharmacological mechanism of action. J Biol Chem. 2000;275(14):9946-56. 5. Kozlov G, Ekiel I, Beglova N, Yee A, Dharamsi A, Engel A, Siddiqui N, Nong A, Gehring K. Rapid fold and structure determination of the archaeal translation elongation factor 1beta from Methanobacterium thermoautotrophicum. J Biomol NMR. 2000;17(3):187-94. 6. Beglova N, Maliartchouk S, Ekiel I, Zaccaro MC, Saragovi HU, Gehring K. Design and solution structure of functional peptide mimetics of nerve growth factor. J Med Chem. 2000;43(19):3530-40. 7. Beglova N, North CL, Blacklow SC. Backbone dynamics of a module pair from the ligand-binding domain of the LDL receptor. Biochemistry. 2001;40(9):2808-15. 8. Takagi J, Beglova N, Yalamanchili P, Blacklow SC, Springer TA. Definition of EGF-like, closely interacting modules that bear activation epitopes in integrin beta subunits. Proc Natl Acad Sci U S A. 2001;98(20):11175-80. 9. Beglova N, Blacklow SC, Takagi J, Springer TA. Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation. Nat Struct Biol. 2002;9(4):282-7. 10. Beglova N, Jeon H, Fisher C, Blacklow SC. Structural features of the low-density lipoprotein receptor facilitating ligand binding and release. Biochem Soc Trans. 2004;32(Pt 5):721-3. 11. Beglova N, Jeon H, Fisher C, Blacklow SC. Cooperation between fixed and low pH-inducible interfaces controls lipoprotein release by the LDL receptor. Mol Cell. 2004;16(2):281-92. 12. Abdul-Aziz D, Fisher C, Beglova N, Blacklow SC. Folding and binding integrity of variants of a prototype ligand-binding module from the LDL receptor possessing multiple alanine substitutions. Biochemistry. 2005;44(13):5075-85. 13. Beglova N, Blacklow SC. The LDL receptor: how acid pulls the trigger. Trends Biochem Sci. 2005;30(6):309-17. 14. Fisher C*, Beglova N*, Blacklow SC. Structure of an LDLR-RAP complex reveals a general mode for ligand recognition by lipoprotein receptors. Mol Cell. 2006;22(2):277-83. (* equal contribution) |
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