Biomedical Engineering Reference
In-Depth Information
20. Roychaudhuri, R., Yang, M., Hoshi, M.M., Teplow, D.B.: Amyloid beta-protein assembly and
Alzheimer disease. J. Biol. Chem. 284 (8), 4749-4753 (2009)
21. Westermark, P., Wernstedt, C., Obrien, T.D., Hayden, D.W., Johnson, K.H.: Islet amyloid in
type-2 human diabetes-mellitus and adult diabetic cats contains a novel putative polypeptide
hormone. Am. J. Pathol. 127 (3), 414-417 (1987)
22. Hoppener, J.W.M., Lips, C.J.M.: Role of islet amyloid in type 2 diabetes mellitus. Int. J.
Biochem. Cell Biol. 38 (5-6), 726-736 (2006)
23. Swendsen, R.H., Wang, J.S.: Replica Monte Carlo simulation of spin-glasses. Phys. Rev. Lett.
57 , 2607-2609 (1986)
24. Sugita, Y., Okamoto, Y.: Replica-exchange molecular dynamics method for protein folding.
Chem.Phys.Lett. 314 (1-2), 141-151 (1999)
25. Bellesia, G., Lampoudi, S., Shea, J.E.: Computational methods in nanostructure design:
replica exchange simulations of self-assembling peptides. In: Gazit, E., Nussinov, R. (eds.)
Nanostructure Design: Methods and Protocols, vol. 474, Methods in Molecular Biology,
pp. 133-152. Humana Press, Totowa, NJ (2008)
26. Nymeyer, H., Gnanakaran, S., Garcia, A.E.: Atomic simulations of protein folding, using the
replica exchange algorithm. Methods enzymol. 383 , 119-149 (2004)
27. Penev, E.S., Lampoudi, S., Shea, J.E.: TiREX: replica-exchange molecular dynamics using
TINKER. Comput. Phys. Commun. 180 (10), 2013-2019 (2009)
28. Daura,
X.,
van
Gunsteren,
W.F.,
Mark,
A.E.:
Folding-unfolding
thermodynamics
of
a “-heptapeptide
from
equilibrium
simulations.
Proteins:
Struct.
Funct.
Genet.
34 (3),
269-280 (1999)
29. Straub, J.E., Thirumalai, D.: Principles governing oligomer formation in amyloidogenic
peptides. Curr. Opin. Struct. Biol. 20 (2), 187-195 (2010)
30. Straub, J.E., Thirumalai, D.: Toward a molecular theory of early and late events in monomer to
amyloid fibril formation. Annu. Rev. Phys. Chem. 62 , 437-463 (2011)
31. Bitan, G., Kirkitadze, M.D., Lomakin, A., Vollers, S.S., Benedek, G.B., Teplow, D.B.: Amyloid
“ protein .A“/ assembly: A“40 and A“42 oligomerize through distinct pathways. Proc. Natl.
Acad. Sci. U.S.A. 100 (1), 330-335 (2003)
32. Bernstein, S.L., Wyttenbach, T., Baumketner, A., Shea, J.E., Bitan, G., Teplow, D.B., Bowers,
M.T.: Amyloid “-protein: monomer structure and early aggregation states of A“42 and its
Pro19alloform.J.Am.Chem.Soc. 127 (7), 2075-2084 (2005)
33. Luhrs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Doeli, H., Schubert, D.,
Riek, R.: 3D structure of Alzheimer's amyloid-“(1-42) fibrils. Proc. Natl. Acad. Sci. U. S. A.
102 (48), 17342-17347 (2005)
34. Sgourakis, N.G., Yan, Y.L., McCallum, S.A., Wang, C.Y., Garcia, A.E.: The Alzheimer's
peptides A“40 and 42 adopt distinct conformations in water: a combined MD/NMR study.
J. Mol. Biol. 368 (5), 1448-1457 (2007)
35. Sgourakis, N.G., Merced-Serrano, M., Boutsidis, C., Drineas, P., Du, Z.M., Wang, C.Y.,
Garcia, A.E.: Atomic-level characterization of the ensemble of the A“(1-42) monomer in water
using unbiased molecular dynamics simulations and spectral algorithms. J. Mol. Biol. 405 (2),
570-583 (2011)
36. Zhuang, W., Sgourakis, N.G., Li, Z.Y., Garcia, A.E., Mukamel, S.: Discriminating early stage
A“42 monomer structures using chirality-induced 2DIR spectroscopy in a simulation study.
Proc.Natl.Acad.Sci.U.S.A. 107 (36), 15687-15692 (2010)
37. Wu, C., Murray, M.M., Bernstein, S.L., Condron, M.M., Bitan, G., Shea J.E., Bowers,
M.T.: The structure of A“42 C-terminal fragments probed by a combined experimental and
theoretical study. J. Mol. Biol. 387 (2), 492-501 (2009)
38. Fradinger, E.A., Monien, B.H., Urbanc, B., Lomakin, A., Tan, M., Li, H., Spring, S.M., Con-
dron, M.M., Cruz, L., Xie, C.W., Benedek, G.B., Bitan, G.: C-terminal peptides coassemble
into A“42 oligomers and protect neurons against A“42-induced neurotoxicity. Proc. Natl.
Acad. Sci. U. S. A. 105 (37), 14175-14180 (2008)
39. Van Nostrand, W.E., Melchor, J.P., Cho, H.S., Greenberg, S.M., Rebeck, G.W.: Pathogenic
effects of D23N Iowa mutant amyloid “-protein. J. Biol. Chem. 276 (35), 32860-32866 (2001)
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