Cited by 578

The DOI matches its Crossref record; 94 of the 94 references it cites were found in a registry or an index.

Peptide Conformation and Supramolecular Organization in Amylin Fibrils: Constraints from Solid-State NMR

Open access

Luca, Sorin, Yau, Wai-Ming, Leapman, Richard, Tycko, Robert·2007·Biochemistry

Open this paper in CoChat — free account

Abstract

The 37-residue amylin peptide, also known as islet amyloid polypeptide, forms fibrils that are the main peptide or protein component of amyloid that develops in the pancreas of type 2 diabetes patients. Amylin also readily forms amyloid fibrils in vitro that are highly polymorphic under typical experimental conditions. We describe a protocol for the preparation of synthetic amylin fibrils that exhibit a single predominant morphology, which we call a striated ribbon, in electron microscopy and atomic force microscopy images. Solid-state nuclear magnetic resonance (NMR) measurements on a series of isotopically labeled samples indicate a single molecular structure within the striated ribbons. We use scanning transmission electron microscopy and several types of one- and two-dimensional solid-state NMR techniques to obtain constraints on the peptide conformation and supramolecular structure in these amylin fibrils and to derive molecular structural models that are consistent with the experimental data. The basic structural unit in amylin striated ribbons, which we call the protofilament, contains four layers of parallel beta-sheets, formed by two symmetric layers of amylin molecules. The molecular structure of amylin protofilaments in striated ribbons closely resembles the protofilament in amyloid fibrils with a similar morphology formed by the 40-residue beta-amyloid peptide that is associated with Alzheimer's disease.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1021/bi701427q

Cites

94 of 94 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

VMD: visual molecular dynamics
Humphrey, W., Dalke, A., & Schulten, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00018-5 · Cited by 66,952
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,965
The Amber biomolecular simulation programs
Case, D. A., Cheatham, T. E., Darden, T., Gohlke, H., Luo, R., Merz, K. M., Onufriev, A., Simmerling, C., Wang, B., & Woods, R. J. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20290 · Cited by 9,535
Comparison of multiple Amber force fields and development of improved protein backbone parameters
Hornak, V., Abel, R., Okur, A., Strockbine, B., Roitberg, A., & Simmerling, C. (2006) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.21123 · Cited by 6,914
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
Protein backbone angle restraints from searching a database for chemical shift and sequence homology
Cornilescu, G., Delaglio, F., & Bax, A. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008392405740 · Cited by 2,957
Proton-enhanced NMR of dilute spins in solids
Pines, A., Gibby, M. G., & Waugh, J. S. (1973) · The Journal of Chemical Physics · doi:10.1063/1.1680061 · Cited by 2,493
Atomic structures of amyloid cross-β spines reveal varied steric zippers
Sawaya, M. R., Sambashivan, S., Nelson, R., Ivanova, M. I., Sievers, S. A., Apostol, M. I., Thompson, M. J., Balbirnie, M., Wiltzius, J. J. W., McFarlane, H. T., et al. (2007) · Nature · doi:10.1038/nature05695 · Cited by 2,271
Structure of the cross-β spine of amyloid-like fibrils
Nelson, R., Sawaya, M. R., Balbirnie, M., Madsen, A. Ø., Riekel, C., Grothe, R., & Eisenberg, D. (2005) · Nature · doi:10.1038/nature03680 · Cited by 2,202
The relative contributions of insulin resistance and beta-cell dysfunction to the pathophysiology of type 2 diabetes
Kahn, S. E. (2003) · Diabetologia · doi:10.1007/s00125-002-1009-0 · Cited by 2,166
Heteronuclear decoupling in rotating solids
Bennett, A. E., Rienstra, C. M., Auger, M., Lakshmi, K. V., & Griffin, R. G. (1995) · The Journal of Chemical Physics · doi:10.1063/1.470372 · Cited by 2,124
A structural model for Alzheimer's 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., & Tycko, R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.262663499 · Cited by 1,845
Self-citation
Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils
Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W.-M., Mattson, M. P., & Tycko, R. (2005) · Science · doi:10.1126/science.1105850 · Cited by 1,687
Self-citation
1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S., & Sykes, B. D. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00227471 · Cited by 1,628
SIMPSON: A general simulation program for solid-state NMR spectroscopy
Bak, M., Rasmussen, J. T., & Nielsen, N. C. (2011) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2011.09.008 · Cited by 1,459
Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients.
Cooper, G. J., Willis, A. C., Clark, A., Turner, R. C., Sim, R. B., & Reid, K. B. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.23.8628 · Cited by 1,299
Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways
Bitan, G., Kirkitadze, M. D., Lomakin, A., Vollers, S. S., Benedek, G. B., & Teplow, D. B. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222681699 · Cited by 1,287
Langevin dynamics of peptides: The frictional dependence of isomerization rates of N‐acetylalanyl‐N′‐methylamide
Loncharich, R. J., Brooks, B. R., & Pastor, R. W. (1992) · Biopolymers · doi:10.1002/bip.360320508 · Cited by 1,180
Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid Fibrils
Petkova, A. T., Yau, W.-M., & Tycko, R. (2006) · Biochemistry · doi:10.1021/bi051952q · Cited by 1,044
Self-citation
1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S., & Sykes, B. D. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00211764 · Cited by 1,012
– dipolar-assisted rotational resonance in magic-angle spinning NMR
Takegoshi, K., Nakamura, S., & Terao, T. (2001) · Chemical Physics Letters · doi:10.1016/s0009-2614(01)00791-6 · Cited by 1,012
Theory and applications of the generalized born solvation model in macromolecular simulations
Tsui, V., & Case, D. A. (2000) · Biopolymers · doi:10.1002/1097-0282(2000)56:4<275::aid-bip10024>3.0.co;2-e · Cited by 977
Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells.
Westermark, P., Wernstedt, C., Wilander, E., Hayden, D. W., O'Brien, T. D., & Johnson, K. H. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.11.3881 · Cited by 976
The protofilament structure of insulin amyloid fibrils
Jiménez, J. L., Nettleton, E. J., Bouchard, M., Robinson, C. V., Dobson, C. M., & Saibil, H. R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.142459399 · Cited by 834
X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS
EANES, E. D., & GLENNER, G. G. (1968) · Journal of Histochemistry & Cytochemistry · doi:10.1177/16.11.673 · Cited by 823
Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus
Lorenzo, A., Razzaboni, B., Weir, G. C., & Yankner, B. A. (1994) · Nature · doi:10.1038/368756a0 · Cited by 820
Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation.
Westermark, P., Engström, U., Johnson, K. H., Westermark, G. T., & Betsholtz, C. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.13.5036 · Cited by 807
Amyloid Fibril Formation by Aβ16-22, a Seven-Residue Fragment of the Alzheimer's β-Amyloid Peptide, and Structural Characterization by Solid State NMR
Balbach, J. J., Ishii, Y., Antzutkin, O. N., Leapman, R. D., Rizzo, N. W., Dyda, F., Reed, J., & Tycko, R. (2000) · Biochemistry · doi:10.1021/bi0011330 · Cited by 703
Self-citation
Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR
Heise, H., Hoyer, W., Becker, S., Andronesi, O. C., Riedel, D., & Baldus, M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506109102 · Cited by 647
Molecular structure of amyloid fibrils: insights from solid-state NMR
Tycko, R. (2006) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583506004173 · Cited by 527
Self-citation
High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy
Jaroniec, C. P., MacPhee, C. E., Bajaj, V. S., McMahon, M. T., Dobson, C. M., & Griffin, R. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0304849101 · Cited by 515
Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
Jiménez, J. L., Guijarro, J. I., Orlova, E., Zurdo, J., Dobson, C. M., Sunde, M., & Saibil, H. R. (1999) · The EMBO Journal · doi:10.1093/emboj/18.4.815 · Cited by 503
Islet amyloid: a long-recognized but underappreciated pathological feature of type 2 diabetes.
Kahn, S. E., Andrikopoulos, S., & Verchere, C. B. (1999) · Diabetes · doi:10.2337/diabetes.48.2.241 · Cited by 488
From the globular to the fibrous state: protein structure and structural conversion in amyloid formation
SUNDE, M., & BLAKE, C. C. F. (1998) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583598003400 · Cited by 457
Correlation of structural elements and infectivity of the HET-s prion
Ritter, C., Maddelein, M.-L., Siemer, A. B., Lührs, T., Ernst, M., Meier, B. H., Saupe, S. J., & Riek, R. (2005) · Nature · doi:10.1038/nature03793 · Cited by 437
Seeding Specificity in Amyloid Growth Induced by Heterologous Fibrils
O'Nuallain, B., Williams, A. D., Westermark, P., & Wetzel, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311300200 · Cited by 423
Analysis of the Minimal Amyloid-forming Fragment of the Islet Amyloid Polypeptide
Azriel, R., & Gazit, E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102883200 · Cited by 420
Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide
Lansbury, P. T., Costa, P. R., Griffiths, J. M., Simon, E. J., Auger, M., Halverson, K. J., Kocisko, D. A., Hendsch, Z. S., Ashburn, T. T., Spencer, R. G. S., et al. (1995) · Nature Structural & Molecular Biology · doi:10.1038/nsb1195-990 · Cited by 396
Conformation‐dependent 13C chemical shifts: A new means of conformational characterization as obtained by high‐resolution solid‐state 13C NMR
Saitô, H. (1986) · Magnetic Resonance in Chemistry · doi:10.1002/mrc.1260241002 · Cited by 390
Propagating structure of Alzheimer’s β-amyloid (10–35) is parallel β-sheet with residues in exact register
Benzinger, T. L. S., Gregory, D. M., Burkoth, T. S., Miller-Auer, H., Lynn, D. G., Botto, R. E., & Meredith, S. C. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13407 · Cited by 389
Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimer's β-amyloid fibrils
Antzutkin, O. N., Balbach, J. J., Leapman, R. D., Rizzo, N. W., Reed, J., & Tycko, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.230315097 · Cited by 383
Self-citation
Mapping Aβ Amyloid Fibril Secondary Structure Using Scanning Proline Mutagenesis
Williams, A. D., Portelius, E., Kheterpal, I., Guo, J.-T., Cook, K. D., Xu, Y., & Wetzel, R. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.11.008 · Cited by 378
Structural and Dynamic Features of Alzheimer's Aβ Peptide in Amyloid Fibrils Studied by Site-directed Spin Labeling
Török, M., Milton, S., Kayed, R., Wu, P., McIntire, T., Glabe, C. G., & Langen, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205659200 · Cited by 373
Spontaneous diabetes mellitus in transgenic mice expressing human islet amyloid polypeptide.
Janson, J., Soeller, W. C., Roche, P. C., Nelson, R. T., Torchia, A. J., Kreutter, D. K., & Butler, P. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.14.7283 · Cited by 342
Structural Organization of α-Synuclein Fibrils Studied by Site-directed Spin Labeling
Der-Sarkissian, A., Jao, C. C., Chen, J., & Langen, R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305266200 · Cited by 329
Watching amyloid fibrils grow by time-lapse atomic force microscopy 1 1Edited by W. Baumeister
Goldsbury, C., Kistler, J., Aebi, U., Arvinte, T., & Cooper, G. J. S. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2299 · Cited by 326
Amyloid Fibril Formation from Full-Length and Fragments of Amylin
Goldsbury, C., Goldie, K., Pellaud, J., Seelig, J., Frey, P., Müller, S. A., Kistler, J., Cooper, G. J. S., & Aebi, U. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4268 · Cited by 316
Solid State NMR Reveals a pH-dependent Antiparallel β-Sheet Registry in Fibrils Formed by a β-Amyloid Peptide
Petkova, A. T., Buntkowsky, G., Dyda, F., Leapman, R. D., Yau, W.-M., & Tycko, R. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.10.044 · Cited by 314
Self-citation
Supramolecular Structure in Full-Length Alzheimer's β-Amyloid Fibrils: Evidence for a Parallel β-Sheet Organization from Solid-State Nuclear Magnetic Resonance
Balbach, J. J., Petkova, A. T., Oyler, N. A., Antzutkin, O. N., Gordon, D. J., Meredith, S. C., & Tycko, R. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)75244-2 · Cited by 314
Self-citation
Polymorphic Fibrillar Assembly of Human Amylin
Goldsbury, C. S., Cooper, G. J. S., Goldie, K. N., Müller, S. A., Saafi, E. L., Gruijters, W. T. M., Misur, M. P., Engel, A., Aebi, U., & Kistler, J. (1997) · Journal of Structural Biology · doi:10.1006/jsbi.1997.3858 · Cited by 293
Amyloid of the prion domain of Sup35p has an in-register parallel β-sheet structure
Shewmaker, F., Wickner, R. B., & Tycko, R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609638103 · Cited by 284
Self-citation
C 13 – C 13 dipolar recoupling under very fast magic angle spinning in solid-state nuclear magnetic resonance: Applications to distance measurements, spectral assignments, and high-throughput secondary-structure determination
Ishii, Y. (2001) · The Journal of Chemical Physics · doi:10.1063/1.1359445 · Cited by 281
Studies on the in Vitro Assembly of Aβ 1–40: Implications for the Search for Aβ Fibril Formation Inhibitors
Goldsbury, C. S., Wirtz, S., Müller, S. A., Sunderji, S., Wicki, P., Aebi, U., & Frey, P. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4259 · Cited by 274
Multiple Assembly Pathways Underlie Amyloid-β Fibril Polymorphisms
Goldsbury, C., Frey, P., Olivieri, V., Aebi, U., & Müller, S. A. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.07.029 · Cited by 273
Supramolecular Structural Constraints on Alzheimer's β-Amyloid Fibrils from Electron Microscopy and Solid-State Nuclear Magnetic Resonance
Antzutkin, O. N., Leapman, R. D., Balbach, J. J., & Tycko, R. (2002) · Biochemistry · doi:10.1021/bi0204185 · Cited by 263
Self-citation
Frequency Selective Heteronuclear Dipolar Recoupling in Rotating Solids: Accurate13C−15N Distance Measurements in Uniformly13C,15N-labeled Peptides
Jaroniec, C. P., Tounge, B. A., Herzfeld, J., & Griffin, R. G. (2001) · Journal of the American Chemical Society · doi:10.1021/ja003266e · Cited by 255
MASS MAPPING WITH THE SCANNING TRANSMISSION ELECTRON MICROSCOPE
Wall, J. S., & Hainfeld, J. F. (1986) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.15.060186.002035 · Cited by 236
3D structure of amyloid protofilaments of β 2 -microglobulin fragment probed by solid-state NMR
Iwata, K., Fujiwara, T., Matsuki, Y., Akutsu, H., Takahashi, S., Naiki, H., & Goto, Y. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607180103 · Cited by 226
Inhibition of Islet Amyloid Polypeptide Fibril Formation: A Potential Role for Heteroaromatic Interactions
Porat, Y., Mazor, Y., Efrat, S., & Gazit, E. (2004) · Biochemistry · doi:10.1021/bi048582a · Cited by 226
Diluting Abundant Spins by Isotope Edited Radio Frequency Field Assisted Diffusion
Morcombe, C. R., Gaponenko, V., Byrd, R. A., & Zilm, K. W. (2004) · Journal of the American Chemical Society · doi:10.1021/ja047919t · Cited by 223
Direct detection of transient α‐helical states in islet amyloid polypeptide
Williamson, J. A., & Miranker, A. D. (2007) · Protein Science · doi:10.1110/ps.062486907 · Cited by 215
Polymorphic Fibril Formation by Residues 10–40 of the Alzheimer’s β-Amyloid Peptide
Paravastu, A. K., Petkova, A. T., & Tycko, R. (2006) · Biophysical Journal · doi:10.1529/biophysj.105.076927 · Cited by 207
Self-citation
The Parallel Superpleated Beta-structure as a Model for Amyloid Fibrils of Human Amylin
Kajava, A. V., Aebi, U., & Steven, A. C. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.02.029 · Cited by 191
General structural motifs of amyloid protofilaments
Ferguson, N., Becker, J., Tidow, H., Tremmel, S., Sharpe, T. D., Krause, G., Flinders, J., Petrovich, M., Berriman, J., Oschkinat, H., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607815103 · Cited by 177
Direct visualisation of the β-sheet structure of synthetic Alzheimer’s amyloid 1 1Edited by F. E. Cohen
Serpell, L. C., & Smith, J. M. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3650 · Cited by 176
Inhibition of human IAPP fibril formation does not prevent β-cell death: evidence for distinct actions of oligomers and fibrils of human IAPP
Meier, J. J., Kayed, R., Lin, C.-Y., Gurlo, T., Haataja, L., Jayasinghe, S., Langen, R., Glabe, C. G., & Butler, P. C. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00082.2006 · Cited by 166
Exploring amyloid formation by a de novo design
Kammerer, R. A., Kostrewa, D., Zurdo, J., Detken, A., García-Echeverría, C., Green, J. D., Müller, S. A., Meier, B. H., Winkler, F. K., Dobson, C. M., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0306786101 · Cited by 164
Extensive islet amyloid formation is induced by development of Type II diabetes mellitus and contributes to its progression: pathogenesis of diabetes in a mouse model
Höppener, J. W. M., Oosterwijk, C., Nieuwenhuis, M. G., Posthuma, G., Thijssen, J. H. H., Vroom, T. M., Ahrén, B., & Lips, C. J. M. (1999) · Diabetologia · doi:10.1007/s001250051175 · Cited by 153
Identifying Structural Features of Fibrillar Islet Amyloid Polypeptide Using Site-directed Spin Labeling
Jayasinghe, S. A., & Langen, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406853200 · Cited by 153
Role of islet amyloid in type 2 diabetes mellitus
Höppener, J. W. M., & Lips, C. J. M. (2006) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.12.009 · Cited by 148
Structural Characterisation of Islet Amyloid Polypeptide Fibrils
Makin, O. S., & Serpell, L. C. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.11.048 · Cited by 147
Amyloid fibrils formed from a segment of the pancreatic islet amyloid protein
Glenner, G. G., Eanes, E. D., & Wiley, C. A. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(88)80538-2 · Cited by 145
Design of Peptide-based Inhibitors of Human Islet Amyloid Polypeptide Fibrillogenesis
Scrocchi, L. A., Chen, Y., Waschuk, S., Wang, F., Cheung, S., Darabie, A. A., McLaurin, J., & Fraser, P. E. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00164-x · Cited by 145
Capturing Intermediate Structures of Alzheimer's β-Amyloid, Aβ(1−40), by Solid-State NMR Spectroscopy
Chimon, S., & Ishii, Y. (2005) · Journal of the American Chemical Society · doi:10.1021/ja054039l · Cited by 143
Aromatic Interactions Are Not Required for Amyloid Fibril Formation by Islet Amyloid Polypeptide but Do Influence the Rate of Fibril Formation and Fibril Morphology
Marek, P., Abedini, A., Song, B., Kanungo, M., Johnson, M. E., Gupta, R., Zaman, W., Wong, S. S., & Raleigh, D. P. (2007) · Biochemistry · doi:10.1021/bi0621967 · Cited by 142
Parallel β-Sheets and Polar Zippers in Amyloid Fibrils Formed by Residues 10−39 of the Yeast Prion Protein Ure2p
Chan, J. C. C., Oyler, N. A., Yau, W., & Tycko, R. (2005) · Biochemistry · doi:10.1021/bi050724t · Cited by 141
Self-citation
Full-length Rat Amylin Forms Fibrils Following Substitution of Single Residues from Human Amylin
Green, J., Goldsbury, C. S., Mini, T., Sunderji, S., Frey, P., Kistler, J., Cooper, G. J. S., & Aebi, U. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01377-3 · Cited by 132
Conservation of the sequence of islet amyloid polypeptide in five mammals is consistent with its putative role as an islet hormone.
Nishi, M., Chan, S. J., Nagamatsu, S., Bell, G. I., & Steiner, D. F. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.15.5738 · Cited by 128
Hydrogen−Deuterium (H/D) Exchange Mapping of Aβ1-40 Amyloid Fibril Secondary Structure Using Nuclear Magnetic Resonance Spectroscopy
Whittemore, N. A., Mishra, R., Kheterpal, I., Williams, A. D., Wetzel, R. B., & SERPERSU, E. H. (2005) · Biochemistry · doi:10.1021/bi048292u · Cited by 124
Aβ Protofibrils Possess a Stable Core Structure Resistant to Hydrogen Exchange
Kheterpal, I., Lashuel, H. A., Hartley, D. M., Walz, T., Lansbury, P. T., & Wetzel, R. B. (2003) · Biochemistry · doi:10.1021/bi0357816 · Cited by 122
Islet amyloid polypeptide: identification of long-range contacts and local order on the fibrillogenesis pathway 1 1Edited by F. Cohen
Padrick, S. B., & Miranker, A. D. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4608 · Cited by 119
Rat amylin: cloning and tissue-specific expression in pancreatic islets.
Leffert, J. D., Newgard, C. B., Okamoto, H., Milburn, J. L., & Luskey, K. L. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.9.3127 · Cited by 118
Incorporation of Pseudoproline Derivatives Allows the Facile Synthesis of Human IAPP, a Highly Amyloidogenic and Aggregation-Prone Polypeptide
Abedini, A., & Raleigh, D. P. (2005) · Organic Letters · doi:10.1021/ol047480+ · Cited by 114
Destabilization of Human IAPP Amyloid Fibrils by Proline Mutations Outside of the Putative Amyloidogenic Domain: Is There a Critical Amyloidogenic Domain in Human IAPP?
Abedini, A., & Raleigh, D. P. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.10.052 · Cited by 108
Core and Heterogeneity of β2-Microglobulin Amyloid Fibrils as Revealed by H/D Exchange
Yamaguchi, K., Katou, H., Hoshino, M., Hasegawa, K., Naiki, H., & Goto, Y. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.067 · Cited by 102
Structural diversity of amyloid fibril formed in human calcitonin as revealed by site‐directed 13C solid‐state NMR spectroscopy
Naito, A., Kamihira, M., Inoue, R., & Saitô, H. (2004) · Magnetic Resonance in Chemistry · doi:10.1002/mrc.1323 · Cited by 94
Rifampicin inhibits the toxicity of pre-aggregated amyloid peptides by binding to peptide fibrils and preventing amyloid-cell interaction
Tomiyama, T., Kaneko, H., Kataoka, K.-I., Asano, S., & Endo, N. (1997) · Biochemical Journal · doi:10.1042/bj3220859 · Cited by 91
Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy
Ippel, H., Olofsson, A., Schleucher, J., Lundgren, E., & Wijmenga, S. S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.132098999 · Cited by 86
Role of endogenous amylin in glucagon secretion and gastric emptying in rats demonstrated with the selective antagonist, AC187
Gedulin, B. R., Jodka, C. M., Herrmann, K., & Young, A. A. (2006) · Regulatory Peptides · doi:10.1016/j.regpep.2006.06.004 · Cited by 81
Islet Amyloid Develops Diffusely Throughout the Pancreas Before Becoming Severe and Replacing Endocrine Cells
Wang, F., Hull, R. L., Vidal, J., Cnop, M., & Kahn, S. E. (2001) · Diabetes · doi:10.2337/diabetes.50.11.2514 · Cited by 77
Dipolar recoupling NMR of biomolecular self-assemblies: determining inter- and intrastrand distances in fibrilized Alzheimer's β-amyloid peptide
Gregory, D. M., Benzinger, T. L. S., Burkoth, T. S., Miller-Auer, H., Lynn, D. G., Meredith, S. C., & Botto, R. E. (1998) · Solid State Nuclear Magnetic Resonance · doi:10.1016/s0926-2040(98)00086-1 · Cited by 75
An Intersheet Packing Interaction in Aβ Fibrils Mapped by Disulfide Cross-Linking
Shivaprasad, S., & Wetzel, R. B. (2004) · Biochemistry · doi:10.1021/bi048019s · Cited by 59
Molecular Alignment within β-Sheets in Aβ14-23 Fibrils: Solid-State NMR Experiments and Theoretical Predictions
Bu, Z., Shi, Y., Callaway, D. J. E., et al. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.091017 · Cited by 50
Islet Amyloid Polypeptide
Abedini, A., & Raleigh, D. P. (2010) · Wiley eBooks · doi:10.1002/9780470572702.ch23 · Cited by 5

Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629
Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
Paravastu, A. K., Leapman, R. D., Yau, W.-M., & Tycko, R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806270105 · Cited by 1,160
Self-citation
Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus
Westermark, P., Andersson, A., & Westermark, G. T. (2011) · Physiological Reviews · doi:10.1152/physrev.00042.2009 · Cited by 1,044
Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer’s Disease, Parkinson’s Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis
Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Dominguez, L., Shea, J.-E., Dokholyan, N. V., De Simone, A., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 678
Amyloid Polymorphism: Structural Basis and Neurobiological Relevance
Tycko, R. (2015) · Neuron · doi:10.1016/j.neuron.2015.03.017 · Cited by 440
Self-citation

See all 578

Authors: Luca, S., Yau, W.-M., Leapman, R., & Tycko, R.
Venue: Biochemistry
Publisher: American Chemical Society (ACS)
Published: 2007-11-01
Volume: 46
Issue: 47
Pages: 13505-13522
ISSN: 0006-2960 (ISSN-L)
1520-4995
DOI: 10.1021/bi701427q
OpenAlex: W1964727310
Cited by: 578
References: 94
FWCI: 19.58
Type: journal article
Language: en
Open access: green

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.

Peptide Conformation and Supramolecular Organization in Amylin Fibrils: Constraints from Solid-State NMR

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Self-check

Citations

Cites

Cited by

Metadata

Record

About these checks

Data sources