-
1
-
-
33746377894
-
Protein misfolding, functional amyloid, and human disease
-
Chiti F., and Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75 (2006) 333-366
-
(2006)
Annu. Rev. Biochem.
, vol.75
, pp. 333-366
-
-
Chiti, F.1
Dobson, C.M.2
-
2
-
-
33750310849
-
Prions and their partners in crime
-
Caughey B., and Baron G.S. Prions and their partners in crime. Nature 443 (2006) 803-810
-
(2006)
Nature
, vol.443
, pp. 803-810
-
-
Caughey, B.1
Baron, G.S.2
-
3
-
-
19544363062
-
Prions as adaptive conduits of memory and inheritance
-
Shorter J., and Lindquist S. Prions as adaptive conduits of memory and inheritance. Nature Rev. Genet. 6 (2005) 435-450
-
(2005)
Nature Rev. Genet.
, vol.6
, pp. 435-450
-
-
Shorter, J.1
Lindquist, S.2
-
4
-
-
33644817188
-
Prion domains: sequences, structures and interactions
-
Ross E.D., Minton A., and Wickner R.B. Prion domains: sequences, structures and interactions. Nature Cell Biol. 7 (2005) 1039-1044
-
(2005)
Nature Cell Biol.
, vol.7
, pp. 1039-1044
-
-
Ross, E.D.1
Minton, A.2
Wickner, R.B.3
-
5
-
-
0034725747
-
Evidence for the prion hypothesis: induction of the yeast [PSI+] factor by in vitro- converted Sup35 protein
-
Sparrer H.E., Santoso A., Szoka Jr. F.C., and Weissman J.S. Evidence for the prion hypothesis: induction of the yeast [PSI+] factor by in vitro- converted Sup35 protein. Science 289 (2000) 595-599
-
(2000)
Science
, vol.289
, pp. 595-599
-
-
Sparrer, H.E.1
Santoso, A.2
Szoka Jr., F.C.3
Weissman, J.S.4
-
6
-
-
0037188506
-
Amyloid aggregates of the HET-s prion protein are infectious
-
Maddelein M.L., Dos Reis S., Duvezin-Caubet S., Coulary-Salin B., and Saupe S.J. Amyloid aggregates of the HET-s prion protein are infectious. Proc. Natl Acad. Sci. USA 99 (2002) 7402-7407
-
(2002)
Proc. Natl Acad. Sci. USA
, vol.99
, pp. 7402-7407
-
-
Maddelein, M.L.1
Dos Reis, S.2
Duvezin-Caubet, S.3
Coulary-Salin, B.4
Saupe, S.J.5
-
7
-
-
1642617641
-
Protein-only transmission of three yeast prion strains
-
King C.Y., and Diaz-Avalos R. Protein-only transmission of three yeast prion strains. Nature 428 (2004) 319-323
-
(2004)
Nature
, vol.428
, pp. 319-323
-
-
King, C.Y.1
Diaz-Avalos, R.2
-
8
-
-
1642633056
-
Conformational variations in an infectious protein determine prion strain differences
-
Tanaka M., Chien P., Naber N., Cooke R., and Weissman J.S. Conformational variations in an infectious protein determine prion strain differences. Nature 428 (2004) 323-328
-
(2004)
Nature
, vol.428
, pp. 323-328
-
-
Tanaka, M.1
Chien, P.2
Naber, N.3
Cooke, R.4
Weissman, J.S.5
-
9
-
-
27144451227
-
Prion generation in vitro: amyloid of Ure2p is infectious
-
Brachmann A., Baxa U., and Wickner R.B. Prion generation in vitro: amyloid of Ure2p is infectious. EMBO J. 24 (2005) 3082-3092
-
(2005)
EMBO J.
, vol.24
, pp. 3082-3092
-
-
Brachmann, A.1
Baxa, U.2
Wickner, R.B.3
-
10
-
-
33845605514
-
"Prion-proof" for [PIN(+)]: infection with in vitro-made amyloid aggregates of Rnq1p-(132-405) Induces [PIN(+)]
-
Patel B.K., and Liebman S.W. "Prion-proof" for [PIN(+)]: infection with in vitro-made amyloid aggregates of Rnq1p-(132-405) Induces [PIN(+)]. J. Mol. Biol. 365 (2006) 775-782
-
(2006)
J. Mol. Biol.
, vol.365
, pp. 775-782
-
-
Patel, B.K.1
Liebman, S.W.2
-
11
-
-
28244446220
-
Aspects on human amyloid forms and their fibril polypeptides
-
Westermark P. Aspects on human amyloid forms and their fibril polypeptides. FEBS J. 272 (2005) 5942-5949
-
(2005)
FEBS J.
, vol.272
, pp. 5942-5949
-
-
Westermark, P.1
-
12
-
-
33751352055
-
Cell biology: infectious Alzheimer's disease?
-
Riek R. Cell biology: infectious Alzheimer's disease?. Nature 444 (2006) 429-431
-
(2006)
Nature
, vol.444
, pp. 429-431
-
-
Riek, R.1
-
13
-
-
33746698975
-
The physical basis of how prion conformations determine strain phenotypes
-
Tanaka M., Collins S.R., Toyama B.H., and Weissman J.S. The physical basis of how prion conformations determine strain phenotypes. Nature 442 (2006) 585-589
-
(2006)
Nature
, vol.442
, pp. 585-589
-
-
Tanaka, M.1
Collins, S.R.2
Toyama, B.H.3
Weissman, J.S.4
-
14
-
-
1342324027
-
Progress towards a molecular-level structural understanding of amyloid fibrils
-
Tycko R. Progress towards a molecular-level structural understanding of amyloid fibrils. Curr. Opin. Struct. Biol. 14 (2004) 96-103
-
(2004)
Curr. Opin. Struct. Biol.
, vol.14
, pp. 96-103
-
-
Tycko, R.1
-
15
-
-
33645995764
-
Recent atomic models of amyloid fibril structure
-
Nelson R., and Eisenberg D. Recent atomic models of amyloid fibril structure. Curr. Opin. Struct. Biol. 16 (2006) 260-265
-
(2006)
Curr. Opin. Struct. Biol.
, vol.16
, pp. 260-265
-
-
Nelson, R.1
Eisenberg, D.2
-
16
-
-
27644518721
-
Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR
-
Heise H., Hoyer W., Becker S., Andronesi O.C., Riedel D., and Baldus M. Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR. Proc. Natl Acad. Sci. USA 102 (2005) 15871-15876
-
(2005)
Proc. Natl Acad. Sci. USA
, vol.102
, pp. 15871-15876
-
-
Heise, H.1
Hoyer, W.2
Becker, S.3
Andronesi, O.C.4
Riedel, D.5
Baldus, M.6
-
17
-
-
12244249201
-
Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils
-
Petkova A.T., Leapman R.D., Guo Z., Yau W.M., Mattson M.P., and Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 307 (2005) 262-265
-
(2005)
Science
, vol.307
, pp. 262-265
-
-
Petkova, A.T.1
Leapman, R.D.2
Guo, Z.3
Yau, W.M.4
Mattson, M.P.5
Tycko, R.6
-
18
-
-
17044381327
-
Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids
-
Jones E.M., and Surewicz W.K. Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids. Cell 121 (2005) 63-72
-
(2005)
Cell
, vol.121
, pp. 63-72
-
-
Jones, E.M.1
Surewicz, W.K.2
-
19
-
-
2542542833
-
A model for Ure2p prion filaments and other amyloids: the parallel superpleated beta-structure
-
Kajava A.V., Baxa U., Wickner R.B., and Steven A.C. A model for Ure2p prion filaments and other amyloids: the parallel superpleated beta-structure. Proc. Natl Acad. Sci. USA 101 (2004) 7885-7890
-
(2004)
Proc. Natl Acad. Sci. USA
, vol.101
, pp. 7885-7890
-
-
Kajava, A.V.1
Baxa, U.2
Wickner, R.B.3
Steven, A.C.4
-
20
-
-
33845938549
-
Amyloid of the prion domain of Sup35p has an in-register parallel {beta}-sheet structure
-
Shewmaker F., Wickner R.B., and Tycko R. Amyloid of the prion domain of Sup35p has an in-register parallel {beta}-sheet structure. Proc. Natl Acad. Sci. USA 103 (2006) 19754-19759
-
(2006)
Proc. Natl Acad. Sci. USA
, vol.103
, pp. 19754-19759
-
-
Shewmaker, F.1
Wickner, R.B.2
Tycko, R.3
-
21
-
-
0030885650
-
The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog
-
Coustou V., Deleu C., Saupe S., and Begueret J. The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc. Natl Acad. Sci. USA 94 (1997) 9773-9778
-
(1997)
Proc. Natl Acad. Sci. USA
, vol.94
, pp. 9773-9778
-
-
Coustou, V.1
Deleu, C.2
Saupe, S.3
Begueret, J.4
-
22
-
-
0038219626
-
Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina
-
Balguerie A., Dos Reis S., Ritter C., Chaignepain S., Coulary-Salin B., Forge V., et al. Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina. EMBO J. 22 (2003) 2071-2081
-
(2003)
EMBO J.
, vol.22
, pp. 2071-2081
-
-
Balguerie, A.1
Dos Reis, S.2
Ritter, C.3
Chaignepain, S.4
Coulary-Salin, B.5
Forge, V.6
-
23
-
-
0041345995
-
Conformational transition occurring upon amyloid aggregation of the HET-s prion protein of Podospora anserina analyzed by hydrogen/deuterium exchange and mass spectrometry
-
Nazabal A., Dos Reis S., Bonneu M., Saupe S.J., and Schmitter J.M. Conformational transition occurring upon amyloid aggregation of the HET-s prion protein of Podospora anserina analyzed by hydrogen/deuterium exchange and mass spectrometry. Biochemistry 42 (2003) 8852-8861
-
(2003)
Biochemistry
, vol.42
, pp. 8852-8861
-
-
Nazabal, A.1
Dos Reis, S.2
Bonneu, M.3
Saupe, S.J.4
Schmitter, J.M.5
-
24
-
-
20444458341
-
Correlation of structural elements and infectivity of the HET-s prion
-
Ritter C., Maddelein M.L., Siemer A.B., Luhrs T., Ernst M., Meier B.H., et al. Correlation of structural elements and infectivity of the HET-s prion. Nature 435 (2005) 844-848
-
(2005)
Nature
, vol.435
, pp. 844-848
-
-
Ritter, C.1
Maddelein, M.L.2
Siemer, A.B.3
Luhrs, T.4
Ernst, M.5
Meier, B.H.6
-
25
-
-
34247093347
-
Mass analysis by scanning transmission electron microscopy and electron diffraction validate predictions of the stacked beta -solenoid model of HET-s prion fibrils
-
Sen A., Baxa U., Simon M.N., Wall J.S., Sabate R., Saupe S.J., and Steven A.C. Mass analysis by scanning transmission electron microscopy and electron diffraction validate predictions of the stacked beta -solenoid model of HET-s prion fibrils. J. Biol. Chem. 282 (2007) 5545-5550
-
(2007)
J. Biol. Chem.
, vol.282
, pp. 5545-5550
-
-
Sen, A.1
Baxa, U.2
Simon, M.N.3
Wall, J.S.4
Sabate, R.5
Saupe, S.J.6
Steven, A.C.7
-
26
-
-
18044391103
-
High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation
-
Siemer A.B., Ritter C., Ernst M., Riek R., and Meier B.H. High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation. Angew Chem. Int. Ed. Engl. 44 (2005) 2441-2444
-
(2005)
Angew Chem. Int. Ed. Engl.
, vol.44
, pp. 2441-2444
-
-
Siemer, A.B.1
Ritter, C.2
Ernst, M.3
Riek, R.4
Meier, B.H.5
-
27
-
-
1842562406
-
The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll
-
Nummelin H., Merckel M.C., Leo J.C., Lankinen H., Skurnik M., and Goldman A. The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll. EMBO J. 23 (2004) 701-711
-
(2004)
EMBO J.
, vol.23
, pp. 701-711
-
-
Nummelin, H.1
Merckel, M.C.2
Leo, J.C.3
Lankinen, H.4
Skurnik, M.5
Goldman, A.6
-
28
-
-
0030712145
-
Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae
-
Glover J.R., Kowal A.S., Schirmer E.C., Patino M.M., Liu J.J., and Lindquist S. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell 89 (1997) 811-819
-
(1997)
Cell
, vol.89
, pp. 811-819
-
-
Glover, J.R.1
Kowal, A.S.2
Schirmer, E.C.3
Patino, M.M.4
Liu, J.J.5
Lindquist, S.6
-
29
-
-
17144398382
-
Probing the structure of the infectious amyloid form of the prion-forming domain of HET-s using high resolution hydrogen/deuterium exchange monitored by mass spectrometry
-
Nazabal A., Maddelein M.L., Bonneu M., Saupe S.J., and Schmitter J.M. Probing the structure of the infectious amyloid form of the prion-forming domain of HET-s using high resolution hydrogen/deuterium exchange monitored by mass spectrometry. J. Biol. Chem. 280 (2005) 13220-23228
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 13220-23228
-
-
Nazabal, A.1
Maddelein, M.L.2
Bonneu, M.3
Saupe, S.J.4
Schmitter, J.M.5
-
30
-
-
33745622856
-
Methods for the in vivo and in vitro analysis of [Het-s] prion infectivity
-
Benkemoun L., Sabate R., Malato L., Dos Reis S., Dalstra H., Saupe S.J., and Maddelein M.L. Methods for the in vivo and in vitro analysis of [Het-s] prion infectivity. Methods 39 (2006) 61-67
-
(2006)
Methods
, vol.39
, pp. 61-67
-
-
Benkemoun, L.1
Sabate, R.2
Malato, L.3
Dos Reis, S.4
Dalstra, H.5
Saupe, S.J.6
Maddelein, M.L.7
-
31
-
-
9344243513
-
FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils
-
Zandomeneghi G., Krebs M.R., McCammon M.G., and Fandrich M. FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils. Protein Sci. 13 (2004) 3314-3321
-
(2004)
Protein Sci.
, vol.13
, pp. 3314-3321
-
-
Zandomeneghi, G.1
Krebs, M.R.2
McCammon, M.G.3
Fandrich, M.4
-
32
-
-
0028569153
-
Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions
-
Monera O.D., Kay C.M., and Hodges R.S. Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions. Protein Sci. 3 (1994) 1984-1991
-
(1994)
Protein Sci.
, vol.3
, pp. 1984-1991
-
-
Monera, O.D.1
Kay, C.M.2
Hodges, R.S.3
-
33
-
-
11144222595
-
The binding of thioflavin-T to amyloid fibrils: localisation and implications
-
Krebs M.R., Bromley E.H., and Donald A.M. The binding of thioflavin-T to amyloid fibrils: localisation and implications. J. Struct. Biol. 149 (2005) 30-37
-
(2005)
J. Struct. Biol.
, vol.149
, pp. 30-37
-
-
Krebs, M.R.1
Bromley, E.H.2
Donald, A.M.3
-
34
-
-
0029058159
-
An analysis of side chain interactions and pair correlations within antiparallel beta-sheets: the differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs
-
Wouters M.A., and Curmi P.M. An analysis of side chain interactions and pair correlations within antiparallel beta-sheets: the differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs. Proteins: Struct. Funct. Genet. 22 (1995) 119-131
-
(1995)
Proteins: Struct. Funct. Genet.
, vol.22
, pp. 119-131
-
-
Wouters, M.A.1
Curmi, P.M.2
-
35
-
-
33744807442
-
Sequence and structure analysis of parallel beta helices: implication for constructing amyloid structural models
-
Tsai H.H., Gunasekaran K., and Nussinov R. Sequence and structure analysis of parallel beta helices: implication for constructing amyloid structural models. Structure 14 (2006) 1059-1072
-
(2006)
Structure
, vol.14
, pp. 1059-1072
-
-
Tsai, H.H.1
Gunasekaran, K.2
Nussinov, R.3
-
36
-
-
0032568793
-
A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion
-
DePace A.H., Santoso A., Hillner P., and Weissman J.S. A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell 93 (1998) 1241-1252
-
(1998)
Cell
, vol.93
, pp. 1241-1252
-
-
DePace, A.H.1
Santoso, A.2
Hillner, P.3
Weissman, J.S.4
-
37
-
-
23244449092
-
Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p
-
Chan J.C., Oyler N.A., Yau W.M., and Tycko R. Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p. Biochemistry 44 (2005) 10669-10680
-
(2005)
Biochemistry
, vol.44
, pp. 10669-10680
-
-
Chan, J.C.1
Oyler, N.A.2
Yau, W.M.3
Tycko, R.4
-
38
-
-
0037168655
-
A structural model for Alzheimer's beta -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. A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR. Proc. Natl Acad. Sci. USA 99 (2002) 16742-16747
-
(2002)
Proc. Natl Acad. Sci. USA
, 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
-
39
-
-
28444442999
-
3D structure of Alzheimer's amyloid-beta(1-42) fibrils
-
Luhrs T., Ritter C., Adrian M., Riek-Loher D., Bohrmann B., Dobeli H., et al. 3D structure of Alzheimer's amyloid-beta(1-42) fibrils. Proc. Natl Acad. Sci. USA 102 (2005) 17342-17347
-
(2005)
Proc. Natl Acad. Sci. USA
, vol.102
, pp. 17342-17347
-
-
Luhrs, T.1
Ritter, C.2
Adrian, M.3
Riek-Loher, D.4
Bohrmann, B.5
Dobeli, H.6
-
40
-
-
33750826280
-
General structural motifs of amyloid protofilaments
-
Ferguson N., Becker J., Tidow H., Tremmel S., Sharpe T.D., Krause G., et al. General structural motifs of amyloid protofilaments. Proc. Natl Acad. Sci. USA 103 (2006) 16248-16253
-
(2006)
Proc. Natl Acad. Sci. USA
, vol.103
, pp. 16248-16253
-
-
Ferguson, N.1
Becker, J.2
Tidow, H.3
Tremmel, S.4
Sharpe, T.D.5
Krause, G.6
-
41
-
-
17644397372
-
Abeta40-Lactam(D23/K28) models a conformation highly favorable for nucleation of amyloid
-
Sciarretta K.L., Gordon D.J., Petkova A.T., Tycko R., and Meredith S.C. Abeta40-Lactam(D23/K28) models a conformation highly favorable for nucleation of amyloid. Biochemistry 44 (2005) 6003-6014
-
(2005)
Biochemistry
, vol.44
, pp. 6003-6014
-
-
Sciarretta, K.L.1
Gordon, D.J.2
Petkova, A.T.3
Tycko, R.4
Meredith, S.C.5
-
42
-
-
0344255649
-
Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide
-
Petkova A.T., Buntkowsky G., Dyda F., Leapman R.D., Yau W.M., and Tycko R. Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide. J. Mol. Biol. 335 (2004) 247-260
-
(2004)
J. Mol. Biol.
, vol.335
, pp. 247-260
-
-
Petkova, A.T.1
Buntkowsky, G.2
Dyda, F.3
Leapman, R.D.4
Yau, W.M.5
Tycko, R.6
-
43
-
-
22544450457
-
Strain-specific morphologies of yeast prion amyloid fibrils
-
Diaz-Avalos R., King C.Y., Wall J., Simon M., and Caspar D.L. Strain-specific morphologies of yeast prion amyloid fibrils. Proc. Natl Acad. Sci. USA 102 (2005) 10165-10170
-
(2005)
Proc. Natl Acad. Sci. USA
, vol.102
, pp. 10165-10170
-
-
Diaz-Avalos, R.1
King, C.Y.2
Wall, J.3
Simon, M.4
Caspar, D.L.5
-
44
-
-
15744371668
-
Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids
-
Salnikova A.B., Kryndushkin D.S., Smirnov V.N., Kushnirov V.V., and Ter-Avanesyan M.D. Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids. J. Biol. Chem. 280 (2005) 8808-8812
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 8808-8812
-
-
Salnikova, A.B.1
Kryndushkin, D.S.2
Smirnov, V.N.3
Kushnirov, V.V.4
Ter-Avanesyan, M.D.5
-
45
-
-
33846446694
-
The reconstitution of mammalian prion infectivity de novo
-
Baskakov I.V. The reconstitution of mammalian prion infectivity de novo. FEBS J. 274 (2007) 576-587
-
(2007)
FEBS J.
, vol.274
, pp. 576-587
-
-
Baskakov, I.V.1
-
46
-
-
3042774002
-
The sequences appended to the amyloid core region of the HET-s prion protein determine higher-order aggregate organization in vivo
-
Balguerie A., Dos Reis S., Coulary-Salin B., Chaignepain S., Sabourin M., Schmitter J.M., and Saupe S.J. The sequences appended to the amyloid core region of the HET-s prion protein determine higher-order aggregate organization in vivo. J. Cell Sci. 117 (2004) 2599-2610
-
(2004)
J. Cell Sci.
, vol.117
, pp. 2599-2610
-
-
Balguerie, A.1
Dos Reis, S.2
Coulary-Salin, B.3
Chaignepain, S.4
Sabourin, M.5
Schmitter, J.M.6
Saupe, S.J.7
-
48
-
-
0038795608
-
An autocatalytic reaction as a model for the kinetics of the aggregation of beta-amyloid
-
Sabate R., Gallardo M., and Estelrich J. An autocatalytic reaction as a model for the kinetics of the aggregation of beta-amyloid. Biopolymers 71 (2003) 190-195
-
(2003)
Biopolymers
, vol.71
, pp. 190-195
-
-
Sabate, R.1
Gallardo, M.2
Estelrich, J.3
-
49
-
-
0035783171
-
Bsoft: image and molecular processing in electron microscopy
-
Heymann J.B. Bsoft: image and molecular processing in electron microscopy. J. Struct. Biol. 133 (2001) 156-169
-
(2001)
J. Struct. Biol.
, vol.133
, pp. 156-169
-
-
Heymann, J.B.1
-
50
-
-
33845336533
-
Bsoft: Image processing and molecular modeling for electron microscopy
-
Heymann J.B., and Belnap D.M. Bsoft: Image processing and molecular modeling for electron microscopy. J. Struct. Biol. 157 (2007) 3-18
-
(2007)
J. Struct. Biol.
, vol.157
, pp. 3-18
-
-
Heymann, J.B.1
Belnap, D.M.2
-
51
-
-
4444221565
-
UCSF Chimera-a visualization system for exploratory research and analysis
-
Pettersen E.F., Goddard T.D., Huang C.C., Couch G.S., Greenblatt D.M., Meng E.C., and Ferrin T.E. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25 (2004) 1605-1612
-
(2004)
J. Comput. Chem.
, vol.25
, pp. 1605-1612
-
-
Pettersen, E.F.1
Goddard, T.D.2
Huang, C.C.3
Couch, G.S.4
Greenblatt, D.M.5
Meng, E.C.6
Ferrin, T.E.7
|