-
1
-
-
84907500655
-
Effect of the interaction of the amyloid β (1–42) peptide with short single-stranded synthetic nucleotide sequences: Morphological characterization of the inhibition of fibrils formation and fibrils disassembly
-
Abraham, J. N., Kedracki, D., Prado, E., Gourmel, C., Maroni, P., & Nardin, C., (2014). Effect of the interaction of the amyloid β (1–42) peptide with short single-stranded synthetic nucleotide sequences:Morphological characterization of the inhibition of fibrils formation and fibrils disassembly. Biomacromolecules, 15, 3253–3258. doi:10.1021/bm501004q
-
(2014)
Biomacromolecules
, vol.15
, pp. 3253-3258
-
-
Abraham, J.N.1
Kedracki, D.2
Prado, E.3
Gourmel, C.4
Maroni, P.5
Nardin, C.6
-
2
-
-
84867722125
-
Alzheimer's disease amyloid peptides interact with DNA, as proved by surface plasmon resonance
-
Barrantes, A., Camero, S., Garcia-Lucas, A., Navarro, P. J., Benitez, M. J., & Jimenez, J. S., (2012). Alzheimer's disease amyloid peptides interact with DNA, as proved by surface plasmon resonance. Current Alzheimer Research, 9, 924–934. doi:10.2174/156720512803251101
-
(2012)
Current Alzheimer Research
, vol.9
, pp. 924-934
-
-
Barrantes, A.1
Camero, S.2
Garcia-Lucas, A.3
Navarro, P.J.4
Benitez, M.J.5
Jimenez, J.S.6
-
3
-
-
84928602022
-
Atomistic mechanism of polyphenol amyloid aggregation inhibitors: Molecular dynamics study of Curcumin, Exifone, and Myricetin interaction with the segment of tau peptide oligomer
-
Berhanu, W. M., & Masunov, A. E., (2015). Atomistic mechanism of polyphenol amyloid aggregation inhibitors:Molecular dynamics study of Curcumin, Exifone, and Myricetin interaction with the segment of tau peptide oligomer. Journal of Biomolecular Structure and Dynamics, 33, 1399–1411. doi:10.1080/07391102.2014.951689
-
(2015)
Journal of Biomolecular Structure and Dynamics
, vol.33
, pp. 1399-1411
-
-
Berhanu, W.M.1
Masunov, A.E.2
-
4
-
-
0031214736
-
Teflon-coated peptides
-
Bhattacharjya, S., & Balaram, P., (1997). Teflon-coated peptides. Biopolymers, 42, 125–128. doi:10.1002/(SICI)1097-0282(199708)42:2<125:AID-BIP1>3.0
-
(1997)
Biopolymers
, vol.42
, pp. 125-128
-
-
Bhattacharjya, S.1
Balaram, P.2
-
5
-
-
84920165153
-
Inhibition of protein aggregation and amyloid formation by small molecules
-
Doig, A. J., & Derreumaux, P., (2015). Inhibition of protein aggregation and amyloid formation by small molecules. Current Opinion in Structural Biology, 30, 50–56. doi:10.1016/j.sbi.2014.12.004
-
(2015)
Current Opinion in Structural Biology
, vol.30
, pp. 50-56
-
-
Doig, A.J.1
Derreumaux, P.2
-
6
-
-
84923638331
-
Copper (II) directs formation of toxic amorphous aggregates resulting in inhibition of hen egg white lysozyme fibrillation under alkaline salt-mediated conditions
-
Ghosh, S., Pandey, N. K., Banerjee, P., Chaudhury, K., Nagy, N. V., & Dasgupta, S., (2015). Copper (II) directs formation of toxic amorphous aggregates resulting in inhibition of hen egg white lysozyme fibrillation under alkaline salt-mediated conditions. Journal of Biomolecular Structure and Dynamics, 33, 991–1007. doi:10.1080/07391102.2014.921864
-
(2015)
Journal of Biomolecular Structure and Dynamics
, vol.33
, pp. 991-1007
-
-
Ghosh, S.1
Pandey, N.K.2
Banerjee, P.3
Chaudhury, K.4
Nagy, N.V.5
Dasgupta, S.6
-
7
-
-
84858374665
-
The amyloid state of proteins in human diseases
-
Jucker, M., (2012). The amyloid state of proteins in human diseases. Cell, 148, 1188–1203. doi:10.1016/j.cell.2012.02.022
-
(2012)
Cell
, vol.148
, pp. 1188-1203
-
-
Jucker, M.1
-
8
-
-
84867256112
-
Discovery and structure activity relationship of small molecule inhibitors of toxic β-amyloid-42 fibril formation
-
Kroth, H., Ansaloni, A., Varisco, Y., Jan, A., Sreenivasachary, N., Rezaei-Ghaleh, N., & Pihlgren, M., (2012). Discovery and structure activity relationship of small molecule inhibitors of toxic β-amyloid-42 fibril formation. Journal of Biological Chemistry, 287, 34786–34800. doi:10.1074/jbc.M112.357665
-
(2012)
Journal of Biological Chemistry
, vol.287
, pp. 34786-34800
-
-
Kroth, H.1
Ansaloni, A.2
Varisco, Y.3
Jan, A.4
Sreenivasachary, N.5
Rezaei-Ghaleh, N.6
Pihlgren, M.7
-
9
-
-
84975862390
-
Molecular insight into amyloid oligomer destabilizing mechanism of flavonoid derivative 2-(4′ benzyloxyphenyl)-3-hydroxy-chromen-4-one through docking and molecular dynamics simulations
-
Kumar, A., Srivastava, S., Tripathi, S., Singh, S. K., Srikrishna, S., & Sharma, A., (2015). Molecular insight into amyloid oligomer destabilizing mechanism of flavonoid derivative 2-(4′ benzyloxyphenyl)-3-hydroxy-chromen-4-one through docking and molecular dynamics simulations. Journal of Biomolecular Structure and Dynamics, 34(6), 1–12, doi:10.1080/07391102.2015.1074943
-
(2015)
Journal of Biomolecular Structure and Dynamics
, vol.34
, Issue.6
, pp. 1-12
-
-
Kumar, A.1
Srivastava, S.2
Tripathi, S.3
Singh, S.K.4
Srikrishna, S.5
Sharma, A.6
-
10
-
-
80051673604
-
Amyloid-like fibrils from a domain-swapping protein feature a parallel, in-register conformation without native-like interactions
-
Li, J., Hoop, C. L., Kodali, R., Sivanandam, V. N., & van der Wel, P. C., (2011). Amyloid-like fibrils from a domain-swapping protein feature a parallel, in-register conformation without native-like interactions. Journal of Biological Chemistry, 286, 28988–28995. doi:10.1074/jbc.M111.261750
-
(2011)
Journal of Biological Chemistry
, vol.286
, pp. 28988-28995
-
-
Li, J.1
Hoop, C.L.2
Kodali, R.3
Sivanandam, V.N.4
van der Wel, P.C.5
-
11
-
-
85016634606
-
Amyloid misfolding, aggregation, and the early onset of protein deposition diseases: Insights from AFM experiments and computational analyses
-
Lyubchenko, Y. L., (2015). Amyloid misfolding, aggregation, and the early onset of protein deposition diseases:Insights from AFM experiments and computational analyses. AIMS Molecular Science, 2, 190–210. doi:10.3934/molsci.2015.3.190
-
(2015)
AIMS Molecular Science
, vol.2
, pp. 190-210
-
-
Lyubchenko, Y.L.1
-
12
-
-
84863755561
-
Nonspecific prion protein–nucleic acid interactions lead to different aggregates and cytotoxic species
-
Macedo, B., Millen, T. A., Braga, C. A., Gomes, M. P., Ferreira, P. S., Kraineva, J., & Cordeiro, Y., (2012). Nonspecific prion protein–nucleic acid interactions lead to different aggregates and cytotoxic species. Biochemistry, 51, 5402–5413. doi:10.1021/bi300440e
-
(2012)
Biochemistry
, vol.51
, pp. 5402-5413
-
-
Macedo, B.1
Millen, T.A.2
Braga, C.A.3
Gomes, M.P.4
Ferreira, P.S.5
Kraineva, J.6
Cordeiro, Y.7
-
13
-
-
77955790562
-
Comparing the folding free-energy landscapes of Aβ42 variants with different aggregation properties
-
Mitternacht, S., Staneva, I., Härd, T., & Irbäck, A., (2010). Comparing the folding free-energy landscapes of Aβ42 variants with different aggregation properties. Proteins:Structure, Function, and Bioinformatics, 78, 2600–2608. doi:10.1002/prot.22775
-
(2010)
Proteins: Structure, Function, and Bioinformatics
, vol.78
, pp. 2600-2608
-
-
Mitternacht, S.1
Staneva, I.2
Härd, T.3
Irbäck, A.4
-
14
-
-
84955646477
-
The role of the acidic domain of α-synuclein in amyloid fibril formation: a molecular dynamics study
-
Park, S., Yoon, J., Jang, S., Lee, K., & Shin, S., (2015). The role of the acidic domain of α-synuclein in amyloid fibril formation:a molecular dynamics study. Journal of Biomolecular Structure and Dynamics, 34(2), 1–8, doi:10.1080/07391102.2015.1033016
-
(2015)
Journal of Biomolecular Structure and Dynamics
, vol.34
, Issue.2
, pp. 1-8
-
-
Park, S.1
Yoon, J.2
Jang, S.3
Lee, K.4
Shin, S.5
-
15
-
-
84904036284
-
Amyloid fibrils nucleated and organized by DNA origami constructions
-
Udomprasert, A., Bongiovanni, M. N., Sha, R., Sherman, W. B., Wang, T., Arora, P. S., & Seeman, N. C., (2014). Amyloid fibrils nucleated and organized by DNA origami constructions. Nature Nanotechnology, 9, 537–541. doi:10.1038/nnano.2014.102
-
(2014)
Nature Nanotechnology
, vol.9
, pp. 537-541
-
-
Udomprasert, A.1
Bongiovanni, M.N.2
Sha, R.3
Sherman, W.B.4
Wang, T.5
Arora, P.S.6
Seeman, N.C.7
|