-
1
-
-
33746377894
-
Protein misfolding, functional amyloid, and human disease
-
Chiti, F. and Dobson, C. M. (2006) Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75, 333-366
-
(2006)
Annu. Rev. Biochem.
, vol.75
, pp. 333-366
-
-
Chiti, F.1
Dobson, C.M.2
-
2
-
-
84857642949
-
The toxic Aβ oligomer and Alzheimers disease: An emperor in need of clothes
-
Benilova, I., Karran, E., and De Strooper, B. (2012) The toxic Aβ oligomer and Alzheimers disease: an emperor in need of clothes Nat. Neurosci. 15, 349-357
-
(2012)
Nat. Neurosci.
, vol.15
, pp. 349-357
-
-
Benilova, I.1
Karran, E.2
De Strooper, B.3
-
3
-
-
33847662852
-
Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimers amyloid β-peptide
-
Haass, C. and Selkoe, D. J. (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimers amyloid β-peptide Nat. Rev. Mol. Cell Biol. 8, 101-112
-
(2007)
Nat. Rev. Mol. Cell Biol.
, vol.8
, pp. 101-112
-
-
Haass, C.1
Selkoe, D.J.2
-
4
-
-
0037168655
-
A structural model for Alzheimers β-amyloid fibrils based on experimental constraints from solid state NMR
-
Petkova, A. T., Ishii, Y., Balbach, J. J., Antzutkin, O. N., Leapman, R. D., Delaglio, F., and Tycko, R. (2002) A structural model for Alzheimers β-amyloid fibrils based on experimental constraints from solid state NMR Proc. Natl. Acad. Sci. U. S. A. 99, 16742-16747
-
(2002)
Proc. Natl. Acad. Sci. U. S. A.
, vol.99
, pp. 16742-16747
-
-
Petkova, A.T.1
Ishii, Y.2
Balbach, J.J.3
Antzutkin, O.N.4
Leapman, R.D.5
Delaglio, F.6
Tycko, R.7
-
5
-
-
28444442999
-
3D structure of Alzheimers amyloid-β(1-42) fibrils
-
Luhrs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Dobeli, H., Schubert, D., and Riek, R. (2005) 3D structure of Alzheimers amyloid-β(1-42) fibrils Proc. Natl. Acad. Sci. U. S. A. 102, 17342-17347
-
(2005)
Proc. Natl. Acad. Sci. U. S. A.
, vol.102
, pp. 17342-17347
-
-
Luhrs, T.1
Ritter, C.2
Adrian, M.3
Riek-Loher, D.4
Bohrmann, B.5
Dobeli, H.6
Schubert, D.7
Riek, R.8
-
6
-
-
80053554845
-
A new structural model of Aβ40 fibrils
-
Bertini, I., Gonnelli, L., Luchinat, C., Mao, J., and Nesi, A. (2011) A new structural model of Aβ40 fibrils J. Am. Chem. Soc. 133, 16013-16022
-
(2011)
J. Am. Chem. Soc.
, vol.133
, pp. 16013-16022
-
-
Bertini, I.1
Gonnelli, L.2
Luchinat, C.3
Mao, J.4
Nesi, A.5
-
7
-
-
80054752317
-
Molecular basis for amyloid-β polymorphism
-
Colletier, J.-P., Laganowsky, A., Landau, M., Zhao, M., Soriaga, A. B., Goldschmidt, L., Flot, D., Cascio, D., Sawaya, M. R., and Eisenberg, D. (2011) Molecular basis for amyloid-β polymorphism Proc. Natl. Acad. Sci. U. S. A. 108, 16938-16943
-
(2011)
Proc. Natl. Acad. Sci. U. S. A.
, vol.108
, pp. 16938-16943
-
-
Colletier, J.-P.1
Laganowsky, A.2
Landau, M.3
Zhao, M.4
Soriaga, A.B.5
Goldschmidt, L.6
Flot, D.7
Cascio, D.8
Sawaya, M.R.9
Eisenberg, D.10
-
8
-
-
84862689606
-
An asymmetric dimer as the basic subunit in Alzheimers disease amyloid β fibrils
-
Lopez del Amo, J. M., Schmidt, M., Fink, U., Dasari, M., Fandrich, M., and Reif, B. (2012) An asymmetric dimer as the basic subunit in Alzheimers disease amyloid β fibrils Angew. Chem., Int. Ed. Engl. 51, 6136-6139
-
(2012)
Angew. Chem., Int. Ed. Engl.
, vol.51
, pp. 6136-6139
-
-
Lopez Del Amo, J.M.1
Schmidt, M.2
Fink, U.3
Dasari, M.4
Fandrich, M.5
Reif, B.6
-
9
-
-
84884217594
-
Molecular structure of β-amyloid fibrils in Alzheimers disease brain tissue
-
Lu, J. X., Qiang, W., Yau, W. M., Schwieters, C. D., Meredith, S. C., and Tycko, R. (2013) Molecular structure of β-amyloid fibrils in Alzheimers disease brain tissue Cell 154, 1257-1268
-
(2013)
Cell
, vol.154
, pp. 1257-1268
-
-
Lu, J.X.1
Qiang, W.2
Yau, W.M.3
Schwieters, C.D.4
Meredith, S.C.5
Tycko, R.6
-
10
-
-
82955169516
-
Zn++ binding disrupts the Asp23-Lys28 salt bridge without altering the hairpin-shaped cross-β structure of Aβ42 amyloid aggregates
-
Mithu, V. S., Sarkar, B., Bhowmik, D., Chandrakesan, M., Maiti, S., and Madhu, P. K. (2011) Zn++ binding disrupts the Asp23-Lys28 salt bridge without altering the hairpin-shaped cross-β structure of Aβ42 amyloid aggregates Biophys. J. 101, 2825-2832
-
(2011)
Biophys. J.
, vol.101
, pp. 2825-2832
-
-
Mithu, V.S.1
Sarkar, B.2
Bhowmik, D.3
Chandrakesan, M.4
Maiti, S.5
Madhu, P.K.6
-
11
-
-
36849084640
-
Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimers β-amyloid
-
Chimon, S., Shaibat, M. A., Jones, C. R., Calero, D. C., Aizezi, B., and Ishii, Y. (2007) Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimers β-amyloid Nat. Struct. Mol. Biol. 14, 1157-1164
-
(2007)
Nat. Struct. Mol. Biol.
, vol.14
, pp. 1157-1164
-
-
Chimon, S.1
Shaibat, M.A.2
Jones, C.R.3
Calero, D.C.4
Aizezi, B.5
Ishii, Y.6
-
12
-
-
77951975748
-
Structural conversion of neurotoxic amyloid-β1-42 oligomers to fibrils
-
Ahmed, M., Davis, J., Aucoin, D., Sato, T., Ahuja, S., Aimoto, S., Elliott, J. I., Van Nostrand, W. E., and Smith, S. O. (2010) Structural conversion of neurotoxic amyloid-β1-42 oligomers to fibrils Nat. Struct. Mol. Biol. 17, 561-567
-
(2010)
Nat. Struct. Mol. Biol.
, vol.17
, pp. 561-567
-
-
Ahmed, M.1
Davis, J.2
Aucoin, D.3
Sato, T.4
Ahuja, S.5
Aimoto, S.6
Elliott, J.I.7
Van Nostrand, W.E.8
Smith, S.O.9
-
13
-
-
84903267298
-
Significant structural differences between transient amyloid-β oligomers and less-toxic fibrils in regions known to harbor familial Alzheimers mutations
-
Sarkar, B., Mithu, V. S., Chandra, B., Mandal, A., Chandrakesan, M., Bhowmik, D., Madhu, P. K., and Maiti, S. (2014) Significant structural differences between transient amyloid-β oligomers and less-toxic fibrils in regions known to harbor familial Alzheimers mutations Angew. Chem., Int. Ed. Engl. 53, 6888-6892
-
(2014)
Angew. Chem., Int. Ed. Engl.
, vol.53
, pp. 6888-6892
-
-
Sarkar, B.1
Mithu, V.S.2
Chandra, B.3
Mandal, A.4
Chandrakesan, M.5
Bhowmik, D.6
Madhu, P.K.7
Maiti, S.8
-
14
-
-
84908211476
-
Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity
-
Mannini, B., Mulvihill, E., Sgromo, C., Cascella, R., Khodarahmi, R., Ramazzotti, M., Dobson, C. M., Cecchi, C., and Chiti, F. (2014) Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity ACS Chem. Biol. 9, 2309-2317
-
(2014)
ACS Chem. Biol.
, vol.9
, pp. 2309-2317
-
-
Mannini, B.1
Mulvihill, E.2
Sgromo, C.3
Cascella, R.4
Khodarahmi, R.5
Ramazzotti, M.6
Dobson, C.M.7
Cecchi, C.8
Chiti, F.9
-
15
-
-
34848887507
-
Soluble oligomers from a non-disease related protein mimic Aβ-induced tau hyperphosphorylation and neurodegeneration
-
Vieira, M. N., Forny-Germano, L., Saraiva, L. M., Sebollela, A., Martinez, A. M., Houzel, J. C., De Felice, F. G., and Ferreira, S. T. (2007) Soluble oligomers from a non-disease related protein mimic Aβ-induced tau hyperphosphorylation and neurodegeneration J. Neurochem. 103, 736-748
-
(2007)
J. Neurochem.
, vol.103
, pp. 736-748
-
-
Vieira, M.N.1
Forny-Germano, L.2
Saraiva, L.M.3
Sebollela, A.4
Martinez, A.M.5
Houzel, J.C.6
De Felice, F.G.7
Ferreira, S.T.8
-
16
-
-
0344944630
-
Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
-
Stefani, M. and Dobson, C. M. (2003) Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution J. Mol. Med. 81, 678-699
-
(2003)
J. Mol. Med.
, vol.81
, pp. 678-699
-
-
Stefani, M.1
Dobson, C.M.2
-
17
-
-
0037041420
-
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
-
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., and Stefani, M. (2002) Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases Nature 416, 507-511
-
(2002)
Nature
, vol.416
, pp. 507-511
-
-
Bucciantini, M.1
Giannoni, E.2
Chiti, F.3
Baroni, F.4
Formigli, L.5
Zurdo, J.6
Taddei, N.7
Ramponi, G.8
Dobson, C.M.9
Stefani, M.10
-
18
-
-
84886788712
-
A folding transition underlies the emergence of membrane affinity in amyloid-β
-
Nag, S., Sarkar, B., Chandrakesan, M., Abhyanakar, R., Bhowmik, D., Kombrabail, M., Dandekar, S., Lerner, E., Haas, E., and Maiti, S. (2013) A folding transition underlies the emergence of membrane affinity in amyloid-β Phys. Chem. Chem. Phys. 15, 19129-19133
-
(2013)
Phys. Chem. Chem. Phys.
, vol.15
, pp. 19129-19133
-
-
Nag, S.1
Sarkar, B.2
Chandrakesan, M.3
Abhyanakar, R.4
Bhowmik, D.5
Kombrabail, M.6
Dandekar, S.7
Lerner, E.8
Haas, E.9
Maiti, S.10
-
19
-
-
84864471159
-
A mutation in APP protects against Alzheimers disease and age-related cognitive decline
-
Jonsson, T., Atwal, J. K., Steinberg, S., Snaedal, J., Jonsson, P. V., Bjornsson, S., Stefansson, H., Sulem, P., Gudbjartsson, D., Maloney, J., Hoyte, K., Gustafson, A., Liu, Y., Lu, Y., Bhangale, T., Graham, R. R., Huttenlocher, J., Bjornsdottir, G., Andreassen, O. A., Jonsson, E. G., Palotie, A., Behrens, T. W., Magnusson, O. T., Kong, A., Thorsteinsdottir, U., Watts, R. J., and Stefansson, K. (2012) A mutation in APP protects against Alzheimers disease and age-related cognitive decline Nature 488, 96-99
-
(2012)
Nature
, vol.488
, pp. 96-99
-
-
Jonsson, T.1
Atwal, J.K.2
Steinberg, S.3
Snaedal, J.4
Jonsson, P.V.5
Bjornsson, S.6
Stefansson, H.7
Sulem, P.8
Gudbjartsson, D.9
Maloney, J.10
Hoyte, K.11
Gustafson, A.12
Liu, Y.13
Lu, Y.14
Bhangale, T.15
Graham, R.R.16
Huttenlocher, J.17
Bjornsdottir, G.18
Andreassen, O.A.19
Jonsson, E.G.20
Palotie, A.21
Behrens, T.W.22
Magnusson, O.T.23
Kong, A.24
Thorsteinsdottir, U.25
Watts, R.J.26
Stefansson, K.27
more..
-
20
-
-
84909583532
-
Molecular mechanisms of Alzheimer disease protection by the A673T allele of amyloid precursor protein
-
Maloney, J. A., Bainbridge, T., Gustafson, A., Zhang, S., Kyauk, R., Steiner, P., van der Brug, M., Liu, Y., Ernst, J. A., Watts, R. J., and Atwal, J. K. (2014) Molecular mechanisms of Alzheimer disease protection by the A673T allele of amyloid precursor protein J. Biol. Chem. 289, 30990-31000
-
(2014)
J. Biol. Chem.
, vol.289
, pp. 30990-31000
-
-
Maloney, J.A.1
Bainbridge, T.2
Gustafson, A.3
Zhang, S.4
Kyauk, R.5
Steiner, P.6
Van Der Brug, M.7
Liu, Y.8
Ernst, J.A.9
Watts, R.J.10
Atwal, J.K.11
-
21
-
-
84869878607
-
Good gene, bad gene: New APP variant may be both
-
Di Fede, G., Catania, M., Morbin, M., Giaccone, G., Moro, M. L., Ghidoni, R., Colombo, L., Messa, M., Cagnotto, A., Romeo, M., Stravalaci, M., Diomede, L., Gobbi, M., Salmona, M., and Tagliavini, F. (2012) Good gene, bad gene: new APP variant may be both Prog. Neurobiol. 99, 281-292
-
(2012)
Prog. Neurobiol.
, vol.99
, pp. 281-292
-
-
Di Fede, G.1
Catania, M.2
Morbin, M.3
Giaccone, G.4
Moro, M.L.5
Ghidoni, R.6
Colombo, L.7
Messa, M.8
Cagnotto, A.9
Romeo, M.10
Stravalaci, M.11
Diomede, L.12
Gobbi, M.13
Salmona, M.14
Tagliavini, F.15
-
22
-
-
62449330486
-
A recessive mutation in the APP gene with dominant-negative effect on amyloidogenesis
-
Di Fede, G., Catania, M., Morbin, M., Rossi, G., Suardi, S., Mazzoleni, G., Merlin, M., Giovagnoli, A. R., Prioni, S., Erbetta, A., Falcone, C., Gobbi, M., Colombo, L., Bastone, A., Beeg, M., Manzoni, C., Francescucci, B., Spagnoli, A., Cantu, L., Del Favero, E., Levy, E., Salmona, M., and Tagliavini, F. (2009) A recessive mutation in the APP gene with dominant-negative effect on amyloidogenesis Science 323, 1473-1477
-
(2009)
Science
, vol.323
, pp. 1473-1477
-
-
Di Fede, G.1
Catania, M.2
Morbin, M.3
Rossi, G.4
Suardi, S.5
Mazzoleni, G.6
Merlin, M.7
Giovagnoli, A.R.8
Prioni, S.9
Erbetta, A.10
Falcone, C.11
Gobbi, M.12
Colombo, L.13
Bastone, A.14
Beeg, M.15
Manzoni, C.16
Francescucci, B.17
Spagnoli, A.18
Cantu, L.19
Del Favero, E.20
Levy, E.21
Salmona, M.22
Tagliavini, F.23
more..
-
23
-
-
78651100067
-
Neuropathology of the recessive A673V APP mutation: Alzheimer disease with distinctive features
-
Giaccone, G., Morbin, M., Moda, F., Botta, M., Mazzoleni, G., Uggetti, A., Catania, M., Moro, M. L., Redaelli, V., Spagnoli, A., Rossi, R. S., Salmona, M., Di Fede, G., and Tagliavini, F. (2010) Neuropathology of the recessive A673V APP mutation: Alzheimer disease with distinctive features Acta Neuropathol. 120, 803-812
-
(2010)
Acta Neuropathol.
, vol.120
, pp. 803-812
-
-
Giaccone, G.1
Morbin, M.2
Moda, F.3
Botta, M.4
Mazzoleni, G.5
Uggetti, A.6
Catania, M.7
Moro, M.L.8
Redaelli, V.9
Spagnoli, A.10
Rossi, R.S.11
Salmona, M.12
Di Fede, G.13
Tagliavini, F.14
-
24
-
-
57449091884
-
Molecular structural basis for polymorphism in Alzheimers β-amyloid fibrils
-
Paravastu, A. K., Leapman, R. D., Yau, W. M., and Tycko, R. (2008) Molecular structural basis for polymorphism in Alzheimers β-amyloid fibrils Proc. Natl. Acad. Sci. U. S. A. 105, 18349-18354
-
(2008)
Proc. Natl. Acad. Sci. U. S. A.
, vol.105
, pp. 18349-18354
-
-
Paravastu, A.K.1
Leapman, R.D.2
Yau, W.M.3
Tycko, R.4
-
25
-
-
84885654189
-
The basic structural motif and major biophysical properties of amyloid-β are encoded in the fragment 18-35
-
Chandrakesan, M., Sarkar, B., Mithu, V. S., Abhyankar, R., Bhowmik, D., Nag, S., Sahoo, B., Shah, R., Gurav, S., Banerjee, R., Dandekar, S., Jose, J. C., Sengupta, N., Madhu, P. K., and Maiti, S. (2013) The basic structural motif and major biophysical properties of amyloid-β are encoded in the fragment 18-35 Chem. Phys. 422, 80-87
-
(2013)
Chem. Phys.
, vol.422
, pp. 80-87
-
-
Chandrakesan, M.1
Sarkar, B.2
Mithu, V.S.3
Abhyankar, R.4
Bhowmik, D.5
Nag, S.6
Sahoo, B.7
Shah, R.8
Gurav, S.9
Banerjee, R.10
Dandekar, S.11
Jose, J.C.12
Sengupta, N.13
Madhu, P.K.14
Maiti, S.15
-
26
-
-
79952498441
-
Solid-state NMR spectroscopic investigation of Aβ protofibrils: Implication of a β-sheet remodeling upon maturation into terminal amyloid fibrils
-
Scheidt, H. A., Morgado, I., Rothemund, S., Huster, D., and Fandrich, M. (2011) Solid-state NMR spectroscopic investigation of Aβ protofibrils: implication of a β-sheet remodeling upon maturation into terminal amyloid fibrils Angew. Chem., Int. Ed. Engl. 50, 2837-2840
-
(2011)
Angew. Chem., Int. Ed. Engl.
, vol.50
, pp. 2837-2840
-
-
Scheidt, H.A.1
Morgado, I.2
Rothemund, S.3
Huster, D.4
Fandrich, M.5
-
27
-
-
70349295278
-
Structure-neurotoxicity relationships of amyloid β-protein oligomers
-
Ono, K., Condron, M. M., and Teplow, D. B. (2009) Structure-neurotoxicity relationships of amyloid β-protein oligomers Proc. Natl. Acad. Sci. U. S. A. 106, 14745-14750
-
(2009)
Proc. Natl. Acad. Sci. U. S. A.
, vol.106
, pp. 14745-14750
-
-
Ono, K.1
Condron, M.M.2
Teplow, D.B.3
-
28
-
-
79251631002
-
Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation
-
Bleiholder, C., Dupuis, N. F., Wyttenbach, T., and Bowers, M. T. (2011) Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation Nat. Chem. 3, 172-177
-
(2011)
Nat. Chem.
, vol.3
, pp. 172-177
-
-
Bleiholder, C.1
Dupuis, N.F.2
Wyttenbach, T.3
Bowers, M.T.4
-
29
-
-
79960003359
-
Conformer-specific hydrogen exchange analysis of Aβ(1-42) oligomers by top-down electron capture dissociation mass spectrometry
-
Pan, J., Han, J., Borchers, C. H., and Konermann, L. (2011) Conformer-specific hydrogen exchange analysis of Aβ(1-42) oligomers by top-down electron capture dissociation mass spectrometry Anal. Chem. 83, 5386-5393
-
(2011)
Anal. Chem.
, vol.83
, pp. 5386-5393
-
-
Pan, J.1
Han, J.2
Borchers, C.H.3
Konermann, L.4
-
30
-
-
0025779179
-
Solution structures of β peptide and its constituent fragments: Relation to amyloid deposition
-
Barrow, C. J. and Zagorski, M. G. (1991) Solution structures of β peptide and its constituent fragments: relation to amyloid deposition Science 253, 179-182
-
(1991)
Science
, vol.253
, pp. 179-182
-
-
Barrow, C.J.1
Zagorski, M.G.2
-
31
-
-
84858612961
-
Solid-support electron paramagnetic resonance (EPR) studies of Aβ40 monomers reveal a structured state with three ordered segments
-
Gu, L., Ngo, S., and Guo, Z. (2012) Solid-support electron paramagnetic resonance (EPR) studies of Aβ40 monomers reveal a structured state with three ordered segments J. Biol. Chem. 287, 9081-9089
-
(2012)
J. Biol. Chem.
, vol.287
, pp. 9081-9089
-
-
Gu, L.1
Ngo, S.2
Guo, Z.3
-
32
-
-
33644526613
-
Amyloid β-protein monomer structure: A computational and experimental study
-
Baumketner, A., Bernstein, S. L., Wyttenbach, T., Bitan, G., Teplow, D. B., Bowers, M. T., and Shea, J. E. (2006) Amyloid β-protein monomer structure: a computational and experimental study Protein Sci. 15, 420-428
-
(2006)
Protein Sci.
, vol.15
, pp. 420-428
-
-
Baumketner, A.1
Bernstein, S.L.2
Wyttenbach, T.3
Bitan, G.4
Teplow, D.B.5
Bowers, M.T.6
Shea, J.E.7
-
33
-
-
84883751849
-
Thermodynamically stable amyloid-β monomers have much lower membrane affinity than the small oligomers
-
Sarkar, B., Das, A. K., and Maiti, S. (2013) Thermodynamically stable amyloid-β monomers have much lower membrane affinity than the small oligomers Front. Physiol. 4, 84 10.3389/fphys.2013.00084
-
(2013)
Front. Physiol.
, vol.4
, pp. 84
-
-
Sarkar, B.1
Das, A.K.2
Maiti, S.3
-
34
-
-
84873809834
-
Single molecule characterization of the interactions between amyloid-β peptides and the membranes of hippocampal cells
-
Narayan, P., Ganzinger, K. A., McColl, J., Weimann, L., Meehan, S., Qamar, S., Carver, J. A., Wilson, M. R., St George-Hyslop, P., Dobson, C. M., and Klenerman, D. (2013) Single molecule characterization of the interactions between amyloid-β peptides and the membranes of hippocampal cells J. Am. Chem. Soc. 135, 1491-1498
-
(2013)
J. Am. Chem. Soc.
, vol.135
, pp. 1491-1498
-
-
Narayan, P.1
Ganzinger, K.A.2
McColl, J.3
Weimann, L.4
Meehan, S.5
Qamar, S.6
Carver, J.A.7
Wilson, M.R.8
St George-Hyslop, P.9
Dobson, C.M.10
Klenerman, D.11
-
35
-
-
84927726715
-
Rapid, cell-free assay for membrane-active forms of amyloid-β
-
Bhowmik, D., Das, A. K., and Maiti, S. (2015) Rapid, cell-free assay for membrane-active forms of amyloid-β Langmuir 31, 4049-4053
-
(2015)
Langmuir
, vol.31
, pp. 4049-4053
-
-
Bhowmik, D.1
Das, A.K.2
Maiti, S.3
-
36
-
-
84897063460
-
Local interactions influence the fibrillation kinetics, structure and dynamics of Aβ(1-40) but leave the general fibril structure unchanged
-
Adler, J., Scheidt, H. A., Kruger, M., Thomas, L., and Huster, D. (2014) Local interactions influence the fibrillation kinetics, structure and dynamics of Aβ(1-40) but leave the general fibril structure unchanged Phys. Chem. Chem. Phys. 16, 7461-7471
-
(2014)
Phys. Chem. Chem. Phys.
, vol.16
, pp. 7461-7471
-
-
Adler, J.1
Scheidt, H.A.2
Kruger, M.3
Thomas, L.4
Huster, D.5
-
37
-
-
79954609552
-
Nature of the amyloid-β monomer and the monomer-oligomer equilibrium
-
Nag, S., Sarkar, B., Bandyopadhyay, A., Sahoo, B., Sreenivasan, V. K., Kombrabail, M., Muralidharan, C., and Maiti, S. (2011) Nature of the amyloid-β monomer and the monomer-oligomer equilibrium J. Biol. Chem. 286, 13827-13833
-
(2011)
J. Biol. Chem.
, vol.286
, pp. 13827-13833
-
-
Nag, S.1
Sarkar, B.2
Bandyopadhyay, A.3
Sahoo, B.4
Sreenivasan, V.K.5
Kombrabail, M.6
Muralidharan, C.7
Maiti, S.8
-
38
-
-
38849136693
-
Quasihomogeneous nucleation of amyloid beta yields numerical bounds for the critical radius, the surface tension, and the free energy barrier for nucleus formation
-
Garai, K., Sahoo, B., Sengupta, P., and Maiti, S. (2008) Quasihomogeneous nucleation of amyloid beta yields numerical bounds for the critical radius, the surface tension, and the free energy barrier for nucleus formation J. Chem. Phys. 128, 045102
-
(2008)
J. Chem. Phys.
, vol.128
, pp. 045102
-
-
Garai, K.1
Sahoo, B.2
Sengupta, P.3
Maiti, S.4
-
39
-
-
70349587461
-
On the stability of the soluble amyloid aggregates
-
Sahoo, B., Nag, S., Sengupta, P., and Maiti, S. (2009) On the stability of the soluble amyloid aggregates Biophys. J. 97, 1454-1460
-
(2009)
Biophys. J.
, vol.97
, pp. 1454-1460
-
-
Sahoo, B.1
Nag, S.2
Sengupta, P.3
Maiti, S.4
-
40
-
-
0036384366
-
Measuring diffusion in cell membranes by fluorescence correlation spectroscopy
-
Sengupta, P., Balaji, J., and Maiti, S. (2002) Measuring diffusion in cell membranes by fluorescence correlation spectroscopy Methods 27, 374-387
-
(2002)
Methods
, vol.27
, pp. 374-387
-
-
Sengupta, P.1
Balaji, J.2
Maiti, S.3
-
41
-
-
0041817542
-
The amyloid β peptide (Aβ1-40) is thermodynamically soluble at physiological concentrations
-
Sengupta, P., Garai, K., Sahoo, B., Shi, Y., Callaway, D. J., and Maiti, S. (2003) The amyloid β peptide (Aβ1-40) is thermodynamically soluble at physiological concentrations Biochemistry 42, 10506-10513
-
(2003)
Biochemistry
, vol.42
, pp. 10506-10513
-
-
Sengupta, P.1
Garai, K.2
Sahoo, B.3
Shi, Y.4
Callaway, D.J.5
Maiti, S.6
-
42
-
-
0032797389
-
Amyloid β-peptide polymerization studied using fluorescence correlation spectroscopy
-
Tjernberg, L. O., Pramanik, A., Bjorling, S., Thyberg, P., Thyberg, J., Nordstedt, C., Berndt, K. D., Terenius, L., and Rigler, R. (1999) Amyloid β-peptide polymerization studied using fluorescence correlation spectroscopy Chem. Biol. 6, 53-62
-
(1999)
Chem. Biol.
, vol.6
, pp. 53-62
-
-
Tjernberg, L.O.1
Pramanik, A.2
Bjorling, S.3
Thyberg, P.4
Thyberg, J.5
Nordstedt, C.6
Berndt, K.D.7
Terenius, L.8
Rigler, R.9
-
43
-
-
34047197671
-
Detecting amyloid-β aggregation with fiber-based fluorescence correlation spectroscopy
-
Garai, K., Sureka, R., and Maiti, S. (2007) Detecting amyloid-β aggregation with fiber-based fluorescence correlation spectroscopy Biophys. J. 92, L55-L57
-
(2007)
Biophys. J.
, vol.92
, pp. 55-L57
-
-
Garai, K.1
Sureka, R.2
Maiti, S.3
-
44
-
-
50249169901
-
Protein aggregation probed by two-photon fluorescence correlation spectroscopy of native tryptophan
-
Sahoo, B., Balaji, J., Nag, S., Kaushalya, S. K., and Maiti, S. (2008) Protein aggregation probed by two-photon fluorescence correlation spectroscopy of native tryptophan J. Chem. Phys. 129, 075103
-
(2008)
J. Chem. Phys.
, vol.129
, pp. 075103
-
-
Sahoo, B.1
Balaji, J.2
Nag, S.3
Kaushalya, S.K.4
Maiti, S.5
-
45
-
-
0037060136
-
Diffusion coefficient measurements in microfluidic devices
-
Culbertson, C. T., Jacobson, S. C., and Michael Ramsey, J. (2002) Diffusion coefficient measurements in microfluidic devices Talanta 56, 365-373
-
(2002)
Talanta
, vol.56
, pp. 365-373
-
-
Culbertson, C.T.1
Jacobson, S.C.2
Michael Ramsey, J.3
-
46
-
-
0037342671
-
Measuring size distribution in highly heterogeneous systems with fluorescence correlation spectroscopy
-
Sengupta, P., Garai, K., Balaji, J., Periasamy, N., and Maiti, S. (2003) Measuring size distribution in highly heterogeneous systems with fluorescence correlation spectroscopy Biophys. J. 84, 1977-1984
-
(2003)
Biophys. J.
, vol.84
, pp. 1977-1984
-
-
Sengupta, P.1
Garai, K.2
Balaji, J.3
Periasamy, N.4
Maiti, S.5
-
47
-
-
84890287943
-
PH changes the aggregation propensity of amyloid-β without altering the monomer conformation
-
Bhowmik, D., Maclaughlin, C. M., Chandrakesan, M., Ramesh, P., Venkatramani, R., Walker, G. C., and Maiti, S. (2014) pH changes the aggregation propensity of amyloid-β without altering the monomer conformation Phys. Chem. Chem. Phys. 16, 885-889
-
(2014)
Phys. Chem. Chem. Phys.
, vol.16
, pp. 885-889
-
-
Bhowmik, D.1
Maclaughlin, C.M.2
Chandrakesan, M.3
Ramesh, P.4
Venkatramani, R.5
Walker, G.C.6
Maiti, S.7
-
48
-
-
20444440728
-
Structure of the cross-β spine of amyloid-like fibrils
-
Nelson, R., Sawaya, M. R., Balbirnie, M., Madsen, A. O., Riekel, C., Grothe, R., and Eisenberg, D. (2005) Structure of the cross-β spine of amyloid-like fibrils Nature 435, 773-778
-
(2005)
Nature
, vol.435
, pp. 773-778
-
-
Nelson, R.1
Sawaya, M.R.2
Balbirnie, M.3
Madsen, A.O.4
Riekel, C.5
Grothe, R.6
Eisenberg, D.7
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