Cited by 118Alzheimer's disease research and treatmentsMass Spectrometry Techniques and ApplicationsAdvanced Proteomics Techniques and Applications

The DOI matches its Crossref record; 71 of the 71 references it cites were found in a registry or an index.

Pulsed hydrogen–deuterium exchange mass spectrometry probes conformational changes in amyloid beta (Aβ) peptide aggregation

Open access

Zhang, Ying, Rempel, Don L., Zhang, Jun, Sharma, Anuj K., Mirica, Liviu M., Gross, Michael L.·2013·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.1309175110PMC PMC3767558

Open this paper in CoChat — free account Open PDF

Abstract

Probing the conformational changes of amyloid beta (Aβ) peptide aggregation is challenging owing to the vast heterogeneity of the resulting soluble aggregates. To investigate the formation of these aggregates in solution, we designed an MS-based biophysical approach and applied it to the formation of soluble aggregates of the Aβ42 peptide, the proposed causative agent in Alzheimer's disease. The approach incorporates pulsed hydrogen-deuterium exchange coupled with MS analysis. The combined approach provides evidence for a self-catalyzed aggregation with a lag phase, as observed previously by fluorescence methods. Unlike those approaches, pulsed hydrogen-deuterium exchange does not require modified Aβ42 (e.g., labeling with a fluorophore). Furthermore, the approach reveals that the center region of Aβ42 is first to aggregate, followed by the C and N termini. We also found that the lag phase in the aggregation of soluble species is affected by temperature and Cu(2+) ions. This MS approach has sufficient structural resolution to allow interrogation of Aβ aggregation in physiologically relevant environments. This platform should be generally useful for investigating the aggregation of other amyloid-forming proteins and neurotoxic soluble peptide aggregates.

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 · 10.1073/pnas.1309175110

Cites

71 of 71 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.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

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

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

1 retracted

RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769
Retracted
An Introduction to the Bootstrap
Efron, B., & Tibshirani, R. J. (1994) · doi:10.1201/9780429246593 · Cited by 40,500
An Introduction to the Bootstrap
Efron, B., & Tibshirani, R. J. (1993) · doi:10.1007/978-1-4899-4541-9 · Cited by 21,230
Bootstrap methods: another look at the jackknife
Efron, B. (1979) · The Annals of Statistics · doi:10.1214/aos/1176344552 · Cited by 17,602
Atomic structures of amyloid cross-β spines reveal varied steric zippers
Sawaya, M. R., Sambashivan, S., Nelson, R. A., 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 2,279
The carboxy terminus of the .beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022
3D structure of Alzheimer's amyloid-β(1–42) fibrils
Lührs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Döbeli, H., Schubert, D. A., & Riek, R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506723102 · Cited by 2,001
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,722
Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability
Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., & LaDu, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201750200 · Cited by 1,452
Mutation of the Alzheimer's Disease Amyloid Gene in Hereditary Cerebral Hemorrhage, Dutch Type
Levy, E., Carman, M. D., Fernandez-Madrid, I. J., Power, M. D., Lieberburg, I. M., van Duinen, S. G., Bots, G. T. A. M., Luyendijk, W., & Frangione, B. (1990) · Science · doi:10.1126/science.2111584 · Cited by 1,399
[18] Quantification of β-sheet amyloid fibril structures with thioflavin T
LeVine, H. (1999) · Methods in Enzymology · doi:10.1016/s0076-6879(99)09020-5 · Cited by 1,365 · cited 6×
“Studies of amyloid fibrils invoke X-ray crystallography (22–24), EM (19, 25, 26), and thioflavin T fluorescence (19, 27), revealing the polypeptide’s global behavior, whereas NMR studies provide residue-level information for the fibrils (28–30).”
Influential
The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation
Nilsberth, C., Westlind-Danielsson, A., Eckman, C. B., Condron, M. M., Axelman, K., Forsell, C., Stenh, C., Luthman, J., Teplow, D. B., Younkin, S. G., et al. (2001) · Nature Neuroscience · doi:10.1038/nn0901-887 · Cited by 1,209
Alzheimer's disease-affected brain: Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss
Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E., Krafft, G. A., & Klein, W. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1834302100 · Cited by 1,061
Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
Zhang, Z., & Smith, D. L. (1993) · Protein Science · doi:10.1002/pro.5560020404 · Cited by 1,017
In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
Stine, W. B., Dahlgren, K. N., Krafft, G. A., & LaDu, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210207200 · Cited by 1,015
Dramatic Aggregation of Alzheimer Aβ by Cu(II) Is Induced by Conditions Representing Physiological Acidosis
Atwood, C. S., Moir, R. D., Huang, X., Scarpa, R. C., Bacarra, N. M. E., Romano, D. M., Hartshorn, M. A., Tanzi, R. E., & Bush, A. I. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.12817 · Cited by 1,009
Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
Bernstein, S. L., Dupuis, N., Lazo, N. D., Wyttenbach, T., Condron, M. M., Bitan, G., Teplow, D. B., Shea, J., Ruotolo, B. T., Robinson, C. V., et al. (2009) · Nature Chemistry · doi:10.1038/nchem.247 · Cited by 943
Hydrogen exchange mass spectrometry for the analysis of protein dynamics
Wales, T. E., & Engen, J. R. (2005) · Mass Spectrometry Reviews · doi:10.1002/mas.20064 · Cited by 864
Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR
Röder, H., Elöve, G. A., & Englander, S. W. (1988) · Nature · doi:10.1038/335700a0 · Cited by 815
beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease.
Roher, A. E., Lowenson, J. D., Clarke, S., Woods, A. S., Cotter, R. J., Gowing, E., & Ball, M. J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.22.10836 · Cited by 740
Atomic View of a Toxic Amyloid Small Oligomer
Laganowsky, A. D., Liu, C., Sawaya, M. R., Whitelegge, J. P., Park, J., Zhao, M., Pensalfini, A., Soriaga, A. B., Landau, M., Teng, P. K., et al. (2012) · Science · doi:10.1126/science.1213151 · Cited by 572
Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice
McGowan, E., Pickford, F., Kim, J., Onstead, L., Eriksen, J., Yu, C., Skipper, L., Murphy, M. P., Beard, J., Das, P., et al. (2005) · Neuron · doi:10.1016/j.neuron.2005.06.030 · Cited by 565
Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy
Grabowski, T. J., Cho, H. S., Vonsattel, J. P. G., Rebeck, G. W., & Greenberg, S. M. (2001) · Annals of Neurology · doi:10.1002/ana.1009 · Cited by 523
A universal algorithm for fast and automated charge state deconvolution of electrospray mass-to-charge ratio spectra
Zhang, Z., & Marshall, A. G. (1998) · Journal of the American Society for Mass Spectrometry · doi:10.1016/s1044-0305(97)00284-5 · Cited by 511
Small assemblies of unmodified amyloid $beta;-protein are the proximate neurotoxin in Alzheimer?s disease
Klein, W. L., Stine, W. B., & Teplow, D. B. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.02.010 · Cited by 494
Atomic-resolution dynamics on the surface of amyloid-β protofibrils probed by solution NMR
Fawzi, N. L., Ying, J., Ghirlando, R., Torchia, D. A., & Clore, G. M. (2011) · Nature · doi:10.1038/nature10577 · Cited by 426
Copper Mediates Dityrosine Cross-Linking of Alzheimer's Amyloid-β
Atwood, C., Perry, G. L., Zeng, H., Kato, Y., Jones, W. D., Ling, K.-Q., Huang, X., Moir, R. D., Wang, D., Sayre, L. M., et al. (2003) · Biochemistry · doi:10.1021/bi0358824 · Cited by 371
Aβ40 Inhibits Amyloid Deposition In Vivo
Kim, J., Onstead, L., Randle, S., Price, R., Smithson, L., Zwizinski, C., Dickson, D. W., Golde, T., & McGowan, E. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4849-06.2007 · Cited by 359
Fitting Neurological Protein Aggregation Kinetic Data via a 2-Step, Minimal/“Ockham's Razor” Model: The Finke−Watzky Mechanism of Nucleation Followed by Autocatalytic Surface Growth
Morris, A. M., Watzky, M. A., Agar, J. N., & Finke, R. G. (2008) · Biochemistry · doi:10.1021/bi701899y · Cited by 312
Intracellular Copper Transport in Mammals
Prohaska, J. R., & Gybina, A. A. (2004) · Journal of Nutrition · doi:10.1093/jn/134.5.1003 · Cited by 307
Toxic fibrillar oligomers of amyloid-β have cross-β structure
Stroud, J. C., Liu, C., Teng, P. K., & Eisenberg, D. S. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1203193109 · Cited by 306
Probing Protein Ligand Interactions by Automated Hydrogen/Deuterium Exchange Mass Spectrometry
Chalmers, M. J., Busby, S. A., Pascal, B. D., He, Y., Hendrickson, C. L., Marshall, A. G., & Griffin, P. R. (2006) · Analytical Chemistry · doi:10.1021/ac051294f · Cited by 301
Differential hydrogen/deuterium exchange mass spectrometry analysis of protein–ligand interactions
Chalmers, M. J., Busby, S. A., Pascal, B. D., West, G. M., & Griffin, P. R. (2011) · Expert Review of Proteomics · doi:10.1586/epr.10.109 · Cited by 256
Structural Basis for Increased Toxicity of Pathological Aβ42:Aβ40 Ratios in Alzheimer Disease
Pauwels, K., Williams, T. L., Morris, K. L., Jonckheere, W., Vandersteen, A., Kelly, G., Schymkowitz, J., Rousseau, F., Pastore, A., Serpell, L. C., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.264473 · Cited by 253
Elucidation of Amyloid β-Protein Oligomerization Mechanisms: Discrete Molecular Dynamics Study
Urbanc, B., Betnel, M., Cruz, L., Bitan, G., & Teplow, D. B. (2010) · Journal of the American Chemical Society · doi:10.1021/ja9096303 · Cited by 234
In vitro formation of amyloid fibrils from two synthetic peptides of different lengths homologous to alzheimer's disease β-protein
Castaño, E. M., Ghiso, J. A., Prelli, F. C., Gorevic, P. D., Migheli, A., & Frangione, B. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(86)80241-8 · Cited by 225
Haploinsufficiency of Human APOE Reduces Amyloid Deposition in a Mouse Model of Amyloid-β Amyloidosis
Kim, J., Jiang, H., Park, S., Eltorai, A. E. M., Stewart, F. R., Yoon, H., Basak, J. M., Finn, M. B., & Holtzman, D. M. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.3773-11.2011 · Cited by 204
Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide
Sharma, A. K., Pavlova, S. T., Kim, J., Finkelstein, D., Hawco, N. J., Rath, N. P., Kim, J., & Mirica, L. M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja210588m · Cited by 202 · cited 5×
“One factor of high interest to us is that of Cu 2 + , which has been previously implicated in A β 42 aggregation (14, 18, 19).”
InfluentialSelf-citation
Molecular-Level Examination of Cu2+ Binding Structure for Amyloid Fibrils of 40-Residue Alzheimer’s β by Solid-State NMR Spectroscopy
Parthasarathy, S., Long, F., Miller, Y., Xiao, Y., McElheny, D., Thurber, K. R., Ma, B., Nussinov, R., & Ishii, Y. (2011) · Journal of the American Chemical Society · doi:10.1021/ja1072178 · Cited by 200
Zn(II)‐ and Cu(II)‐induced non‐fibrillar aggregates of amyloid‐β (1–42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators
Tõugu, V., Karafin, A., Zovo, K., Chung, R. S., Howells, C., West, A. K., & Palumaa, P. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06269.x · Cited by 181
Aβ amyloid fibrils possess a core structure highly resistant to hydrogen exchange
Kheterpal, I., Zhou, S., Cook, K. D., & Wetzel, R. B. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250288897 · Cited by 168
Aβ aggregation and possible implications in Alzheimer's disease pathogenesis
Bharadwaj, P. R., Dubey, A. K., Masters, C. L., Martins, R. N., & Macreadie, I. G. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00609.x · Cited by 155
Synthesis, aggregation, neurotoxicity, and secondary structure of various Aβ1–42 mutants of familial Alzheimer's disease at positions 21–23
Murakami, K., Irie, K., Morimoto, A., Ohigashi, H., Shindo, M., Nagao, M., Shimizu, T., & Shirasawa, T. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00430-8 · Cited by 146
H/D Exchange and Mass Spectrometry in the Studies of Protein Conformation and Dynamics: Is There a Need for a Top-Down Approach?
Kaltashov, I. A., Bobst, C. E., & Abzalimov, R. R. (2009) · Analytical Chemistry · doi:10.1021/ac901366n · Cited by 138
Quantitative analysis of the time course of Aβ oligomerization and subsequent growth steps using tetramethylrhodamine-labeled Aβ
Garai, K., & Frieden, C. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1222478110 · Cited by 138
Ockham’s Razor
Garrett, A. J. M. (1991) · Springer eBooks · doi:10.1007/978-94-011-3460-6_36 · Cited by 129
Amyloid β Protein: Aβ40 Inhibits Aβ42 Oligomerization
Murray, M. M., Bernstein, S. L., Nyugen, V., Condron, M. M., Teplow, D. B., & Bowers, M. T. (2009) · Journal of the American Chemical Society · doi:10.1021/ja8092604 · Cited by 128
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
Identification of Physiological and Toxic Conformations in Aβ42 Aggregates
Masuda, Y., Uemura, S., Ohashi, R., Nakanishi, A., Takegoshi, K., Shimizu, T., Shirasawa, T., & Irie, K. (2008) · ChemBioChem · doi:10.1002/cbic.200800411 · Cited by 109
Hydrogen/Deuterium Exchange Reveals Distinct Agonist/Partial Agonist Receptor Dynamics within Vitamin D Receptor/Retinoid X Receptor Heterodimer
Zhang, J., Chalmers, M. J., Stayrook, K. R., Burris, L. L., Garcia-Ordoñez, R. D., Pascal, B. D., Burris, T. P., Dodge, J. A., & Griffin, P. R. (2010) · Structure · doi:10.1016/j.str.2010.07.007 · Cited by 109
Self-citation
Aβ40 and Aβ42 Amyloid Fibrils Exhibit Distinct Molecular Recycling Properties
Sánchez, L., Madurga, S., Pukala, T. L., Vilaseca, M., López‐Iglesias, C., Robinson, C. V., Giralt, E., & Carulla, N. (2011) · Journal of the American Chemical Society · doi:10.1021/ja1117123 · Cited by 108
Aβ40 Protects Non-toxic Aβ42 Monomer from Aggregation
Yan, Y., & Wang, C. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.04.014 · Cited by 99
Hydrogen/deuterium exchange and electron-transfer dissociation mass spectrometry determine the interface and dynamics of apolipoprotein E oligomerization
Huang, R. Y.-C., Garai, K., Frieden, C., & Gross, M. L. (2011) · Biochemistry · doi:10.1021/bi2010027 · Cited by 97
Self-citation
Cerebrospinal Fluid Biomarkers of Alzheimer's Disease
Fagan, A. M., & Holtzman, D. M. (2010) · Biomarkers in Medicine · doi:10.2217/bmm.09.83 · Cited by 88
Hollow core of Alzheimer’s Aβ42 amyloid observed by cryoEM is relevant at physiological pH
Miller, Y., Ma, B., Tsai, C.-J., & Nussinov, R. (2010) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1004704107 · Cited by 84
Estimating error limits in parametric curve fitting
Caceci, M. S. (1989) · Analytical Chemistry · doi:10.1021/ac00195a023 · Cited by 84
Structure and Intermolecular Dynamics of Aggregates Populated during Amyloid Fibril Formation Studied by Hydrogen/Deuterium Exchange
Carulla, N., Zhou, M., Giralt, E., Robinson, C. V., & Dobson, C. M. (2010) · Accounts of Chemical Research · doi:10.1021/ar9002784 · Cited by 81
Aβ(39–42) Modulates Aβ Oligomerization but Not Fibril Formation
Gessel, M. M., Wu, C. F., Li, H., Bitan, G., Shea, J., & Bowers, M. T. (2011) · Biochemistry · doi:10.1021/bi201520b · Cited by 80
High‐molecular weight Aβ oligomers and protofibrils are the predominant Aβ species in the native soluble protein fraction of the AD brain
Upadhaya, A. R., Lungrin, I., Yamaguchi, H., Fändrich, M., & Thal, D. R. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2011.01306.x · Cited by 75
Structure and Dynamics of Small Soluble Aβ(1–40) Oligomers Studied by Top-Down Hydrogen Exchange Mass Spectrometry
Pan, J., Han, J., Borchers, C. H., & Konermann, L. (2012) · Biochemistry · doi:10.1021/bi3002049 · Cited by 71
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., & Konermann, L. (2011) · Analytical Chemistry · doi:10.1021/ac200906v · Cited by 69
Three Dimensional Models of Cu 2+ -Aβ(1–16) Complexes from Computational Approaches
Alí‐Torres, J., Maréchal, J., Rodrı́guez-Santiago, L., & Sodupe, M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja203407v · Cited by 60
In Vitro Studies of Flemish, Dutch, and Wild-Type β-Amyloid Provide Evidence for Two-Staged Neurotoxicity
Kumar‐Singh, S., Julliams, A., Nuydens, R., Ceuterick, C., Labeur, C., Serneels, S., Vennekens, K., Osta, P. V., Geerts, H., Strooper, B. D., et al. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0529 · Cited by 52
Pulsed Hydrogen Exchange and Electrospray Charge-State Distribution as Complementary Probes of Protein Structure in Kinetic Experiments: Implications for Ubiquitin Folding
Pan, J., Wilson, D. J., & Konermann, L. (2005) · Biochemistry · doi:10.1021/bi050575e · Cited by 45
Pulsed hydrogen/deuterium exchange mass spectrometry for time‐resolved membrane protein folding studies
Khanal, A., Pan, Y., Brown, L. S., & Konermann, L. (2012) · Journal of Mass Spectrometry · doi:10.1002/jms.3127 · Cited by 38
Z-Phe-Ala-diazomethylketone (PADK) Disrupts and Remodels Early Oligomer States of the Alzheimer Disease Aβ42 Protein
Zheng, X., Gessel, M. M., Wisniewski, M. L., Viswanathan, K., Wright, D. L., Bahr, B. A., & Bowers, M. T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.c111.328575 · Cited by 36
H/D Exchange Centroid Monitoring is Insufficient to Show Differences in the Behavior of Protein States
Zhang, J., Ramachandran, P. L., Kumar, R., & Gross, M. L. (2013) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-012-0555-z · Cited by 34
Self-citation
Dynamics of Metastable β-Hairpin Structures in the Folding Nucleus of Amyloid β-Protein
Cruz, L., Rao, J. S., Teplow, D. B., & Urbanc, B. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp301619v · Cited by 29
[Amyloid beta protein].
Tamaoka, A. (1999) · PubMed · Cited by 25
Structural Dynamics of the Amyloid β-Protein Monomer Folding Nucleus
Roychaudhuri, R., Yang, M., Condron, M. M., & Teplow, D. B. (2012) · Biochemistry · doi:10.1021/bi300350p · Cited by 16
Dual role of Cu2+ ions on the aggregation and degradation of soluble Aβ oligomers and protofibrils investigated by fluorescence spectroscopy and AFM
García, S. P., Cuscó, C., Brissos, R. F., Torrents, E., Caubet, A., & Gámez, P. (2012) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2012.07.007 · Cited by 12

Sorted by citations

A new era for understanding amyloid structures and disease
Iadanza, M. G., Jackson, M. P., Hewitt, E. W., Ranson, N. A., & Radford, S. E. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0060-8 · Cited by 1,002
Amyloid β Protein and Alzheimer’s Disease: When Computer Simulations Complement Experimental Studies
Nasica-Labouze, J., Nguyen, P. H., Sterpone, F., Berthoumieu, O., Buchete, N., Côté, S., Simone, A. D., Doig, A. J., Faller, P., García, A. E., et al. (2015) · Chemical Reviews · doi:10.1021/cr500638n · Cited by 591
Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications
Liu, X. R., Zhang, M. M., & Gross, M. L. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00815 · Cited by 245
Self-citation
Mass spectrometry for the biophysical characterization of therapeutic monoclonal antibodies
Zhang, H., Cui, W., & Gross, M. L. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.11.027 · Cited by 158
Self-citation
The OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systems
Sterpone, F., Melchionna, S., Tufféry, P., Pasquali, S., Mousseau, N., Cragnolini, T., Chebaro, Y., St‐Pierre, J., Kalimeri, M., Barducci, A., et al. (2014) · Chemical Society Reviews · doi:10.1039/c4cs00048j · Cited by 156

See all 118

Authors: Zhang, Y., Rempel, D. L., Zhang, J., Sharma, A. K., Mirica, L. M., & Gross, M. L.
Affiliations: California Institute of Technology (US)
ORCID: Zhang, Ying
Rempel, Don L.
Zhang, Jun
Sharma, Anuj K.
Mirica, Liviu M.
Gross, Michael L.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2013-08-19
Volume: 110
Issue: 36
Pages: 14604-14609
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.1309175110
PMC: PMC3767558
OpenAlex: W2165610594
Cited by: 118
References: 71
Citations by year: 2026: 1 · 2025: 5 · 2024: 4 · 2023: 12 · 2022: 10 · 2021: 7 · 2020: 14 · 2019: 9 · 2018: 12 · 2017: 7 · 2016: 8 · 2015: 12 · 2014: 13 · 2013: 4
FWCI: 8.59
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Alzheimer's Association (AG05681, NIRP-12-259199, 12-259199)
Oak Ridge Associated Universities
National Institutes of Health (GM103422, AG05681)
Charles F. and Joanne Knight Alzheimer Disease Research Center, Washington University in St. Louis (P50 AG0568 1)
National Institute on Aging (P 50 AG05681, P50AG005681)
National Institute of General Medical Sciences (GM103422, P41GM103422)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
Keywords: amyloid-beta, amyloid-beta 42, peptide aggregation, hydrogen-deuterium exchange, conformational change, lag phase, Alzheimer's disease, copper ions, temperature effects
MeSH terms: Alzheimer Disease, Amyloid, Copper, Deuterium, Humans, Hydrogen, Peptide Fragments, Protein Conformation, Mass Spectrometry, Temperature, Blotting, Western, Amyloid beta-Peptides, Deuterium Exchange Measurement, Microscopy, Electron, Transmission

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

Pulsed hydrogen–deuterium exchange mass spectrometry probes conformational changes in amyloid beta (Aβ) peptide aggregation

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks