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

An Introduction to the Bootstrap

Efron, B., & Tibshirani, R. J. (1994) · doi:10.1201/9780429246593 · Cited by 40,500 · see citing works

An Introduction to the Bootstrap

Efron, B., & Tibshirani, R. J. (1993) · doi:10.1007/978-1-4899-4541-9 · Cited by 21,230 · see citing works

Bootstrap methods: another look at the jackknife

Efron, B. (1979) · The Annals of Statistics · doi:10.1214/aos/1176344552 · Cited by 17,602 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 1,677 · see citing works

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 · see citing works

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 1,380 · see citing works

[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× · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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., Wyttenbach, T., Condron, M., Bitan, G., Teplow, D., Shea, J., Ruotolo, B., Robinson, C., et al. (2009) · Nature Chemistry · doi:10.1038/nchem.247 · Cited by 847 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 564 · see citing works

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 · see citing works

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 · see citing works

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 487 · see citing works

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 420 · see citing works

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 · see citing works

Aβ40 Inhibits Amyloid Deposition<i>In Vivo</i>

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 · see citing works

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 307 · see citing works

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 · see citing works

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 303 · see citing works

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 · see citing works

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 255 · see citing works

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 · see citing works

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 237 · see citing works

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 · see citing works

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× · see citing works

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 199 · see citing works

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 199 · see citing works

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 · see citing works

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 · see citing works

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 147 · see citing works

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 144 · see citing works

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 · see citing works

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 · see citing works

Ockham’s Razor

Garrett, A. J. M. (1991) · Springer eBooks · doi:10.1007/978-94-011-3460-6_36 · Cited by 129 · see citing works

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 · see citing works

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 · see citing works

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 108 · see citing works

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 107 · see citing works

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 104 · see citing works

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 · see citing works

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 · see citing works

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 85 · see citing works

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 · see citing works

Estimating error limits in parametric curve fitting

Caceci, M. S. (1989) · Analytical Chemistry · doi:10.1021/ac00195a023 · Cited by 84 · see citing works

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 · see citing works

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 77 · see citing works

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 73 · see citing works

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 69 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 35 · see citing works

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 · see citing works

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 · see citing works

[Amyloid beta protein].

Tamaoka, A. (1999) · PubMed · Cited by 25 · see citing works

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 · see citing works

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 11 · see citing works

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 969 · see citing works

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., Garcı́a, A. E., et al. (2015) · Chemical Reviews · doi:10.1021/cr500638n · Cited by 583 · see citing works

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 241 · see citing works

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 152 · see citing works

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 150 · see citing works

Applications of Hydrogen/Deuterium Exchange MS from 2012 to 2014

Pirrone, G. F., Iacob, R. E., & Engen, J. R. (2014) · Analytical Chemistry · doi:10.1021/ac5040242 · Cited by 148 · see citing works

Mass Spectrometry Methods for Studying Structure and Dynamics of Biological Macromolecules

Konermann, L., Vahidi, S., & Sowole, M. A. (2013) · Analytical Chemistry · doi:10.1021/ac4039306 · Cited by 136 · see citing works

Visualizing and trapping transient oligomers in amyloid assembly pathways

Cawood, E. E., Karamanos, T., Wilson, A. J., & Radford, S. (2020) · Biophysical Chemistry · doi:10.1016/j.bpc.2020.106505 · Cited by 109 · see citing works

Bridging protein structure, dynamics, and function using hydrogen/deuterium‐exchange mass spectrometry

Hodge, E. A., Benhaim, M. A., & Lee, K. K. (2019) · Protein Science · doi:10.1002/pro.3790 · Cited by 127 · see citing works

Cu and Zn interactions with Aβ peptides: consequence of coordination on aggregation and formation of neurotoxic soluble Aβ oligomers

Rana, M., & Sharma, A. K. (2018) · Metallomics · doi:10.1039/c8mt00203g · Cited by 113 · see citing works

Transient dynamics of Aβ contribute to toxicity in Alzheimer’s disease

Hubin, E., van Nuland, N. V., Broersen, K., & Pauwels, K. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1634-z · Cited by 94 · see citing works

Mass Spectrometry Methods for Measuring Protein Stability

Vallejo, D. D., Ramírez, C. R., Parson, K. F., Han, Y., Gadkari, V. V., & Ruotolo, B. T. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00857 · Cited by 82 · see citing works

Dynamic diversity of synthetic supramolecular polymers in water as revealed by hydrogen/deuterium exchange

Lou, X., Lafleur, R. P. M., Leenders, C. M. A., Schoenmakers, S. M. C., Matsumoto, N. M., Baker, M. B., van Dongen, J. L. J., Palmans, A. R. A., & Meijer, E. W. (2017) · Nature Communications · doi:10.1038/ncomms15420 · Cited by 81 · see citing works

Atomic and Dynamic Insights into the Beneficial Effect of the 1,4-Naphthoquinon-2-yl- l -tryptophan Inhibitor on Alzheimer’s Aβ1–42 Dimer in Terms of Aggregation and Toxicity

Zhang, T., Xu, W., Mu, Y., & Derreumaux, P. (2013) · ACS Chemical Neuroscience · doi:10.1021/cn400197x · Cited by 77 · see citing works

Proteomics beyond large-scale protein expression analysis

Boersema, P. J., Kahraman, A., & Picotti, P. (2015) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2015.01.005 · Cited by 74 · see citing works

Conformational-Sensitive Fast Photochemical Oxidation of Proteins and Mass Spectrometry Characterize Amyloid Beta 1–42 Aggregation

Li, K. S., Rempel, D. L., & Gross, M. L. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b07543 · Cited by 73 · see citing works

Advanced Techniques for Detecting Protein Misfolding and Aggregation in Cellular Environments

Bai, Y., Zhang, S., Dong, H. Y., Liu, Y., Liu, C., & Zhang, X. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00494 · Cited by 71 · see citing works

Familial Alzheimer A2 V Mutation Reduces the Intrinsic Disorder and Completely Changes the Free Energy Landscape of the Aβ1–28 Monomer

Nguyen, P. H., Tarus, B., & Derreumaux, P. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp4115404 · Cited by 67 · see citing works

Insights into the Molecular Mechanisms of Alzheimer’s and Parkinson’s Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology

Coskuner‐Weber, O., & Uversky, V. N. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020336 · Cited by 66 · see citing works

Strain-Stiffening in Dynamic Supramolecular Fiber Networks

Romera, M. F., Lou, X., Schill, J., ter Huurne, G. M., Fransen, P.-P. K. H., Voets, I. K., Storm, C., & Sijbesma, R. P. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b09289 · Cited by 62 · see citing works

Mass Determination of Entire Amyloid Fibrils by Using Mass Spectrometry

Doussineau, T., Mathevon, C., Altamura, L., Vendrely, C., Dugourd, P., Forge, V., & Antoine, R. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201508995 · Cited by 61 · see citing works

Coordination Chemistry of Bifunctional Chemical Agents Designed for Applications in 64Cu PET Imaging for Alzheimer’s Disease

Sharma, A. K., Schultz, J. W., Prior, J. T., Rath, N. P., & Mirica, L. M. (2017) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.7b01883 · Cited by 60 · see citing works

Metal-chelating benzothiazole multifunctional compounds for the modulation and 64 Cu PET imaging of Aβ aggregation

Huang, Y., Cho, H.-J., Bandara, N., Sun, L., Tran, D., Rogers, B. E., & Mirica, L. M. (2020) · Chemical Science · doi:10.1039/d0sc02641g · Cited by 58 · see citing works

A Multifunctional Chemical Agent as an Attenuator of Amyloid Burden and Neuroinflammation in Alzheimer’s Disease

Cho, H., Sharma, A. K., Zhang, Y., Gross, M. L., & Mirica, L. M. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00114 · Cited by 53 · see citing works

Probing the dynamic regulation of peripheral membrane proteins using hydrogen deuterium exchange–MS (HDX–MS)

Vadas, O., & Burke, J. E. (2015) · Biochemical Society Transactions · doi:10.1042/bst20150065 · Cited by 51 · see citing works

Self-Assembly Pathways of β-Sheet-Rich Amyloid-β(1–40) Dimers: Markov State Model Analysis on Millisecond Hybrid-Resolution Simulations

Cao, Y., Jiang, X., & Han, W. (2017) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.7b00803 · Cited by 51 · see citing works

Effects of Cu(II) on the aggregation of amyloid-β

Weibull, M. G. M., Simonsen, S., Oksbjerg, C. R., Tiwari, M. K., & Hemmingsen, L. (2019) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-019-01727-5 · Cited by 50 · see citing works

Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity

Sharma, A. K., Kim, J., Prior, J. T., Hawco, N. J., Rath, N. P., Kim, J., & Mirica, L. M. (2014) · Inorganic Chemistry · doi:10.1021/ic500926c · Cited by 48 · see citing works

Structural Proteomics Methods to Interrogate the Conformations and Dynamics of Intrinsically Disordered Proteins

Beveridge, R., & Calabrese, A. N. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.603639 · Cited by 47 · see citing works

Polyphenolic Biflavonoids Inhibit Amyloid-Beta Fibrillation and Disaggregate Preformed Amyloid-Beta Fibrils

Choi, E. Y., Kang, S. S., Lee, S. K., & Han, B. H. (2019) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2019.113 · Cited by 45 · see citing works

Amentoflavone: A Bifunctional Metal Chelator that Controls the Formation of Neurotoxic Soluble Aβ 42 Oligomers

Sun, L., Sharma, A. K., Han, B.-H., & Mirica, L. M. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00376 · Cited by 45 · see citing works

One of the possible mechanisms of amyloid fibrils formation based on the sizes of primary and secondary folding nuclei of Aβ40 and Aβ42

Dovidchenko, N. V., Glyakina, A. V., Selivanova, O. M., Grigorashvili, E. I., Suvorina, M. Y., Dzhus, U. F., Mikhaylina, A. O., Shiliaev, N. G., Marchenkov, V. V., Surin, A. K., et al. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.03.020 · Cited by 42 · see citing works

Interrogating amyloid aggregation with aggregation-induced emission fluorescence probes

Zhou, Y., Jin, H., Ding, D., & Tang, Y. (2022) · Biomaterials · doi:10.1016/j.biomaterials.2022.121605 · Cited by 42 · see citing works

Paper-based electrochemiluminescence sensor for highly sensitive detection of amyloid-β oligomerization: Toward potential diagnosis of Alzheimer's disease

Liu, H., Zhou, X., Shen, Q. P., & Xing, D. (2018) · Theranostics · doi:10.7150/thno.23483 · Cited by 40 · see citing works

Azo-dyes based small bifunctional molecules for metal chelation and controlling amyloid formation

Rana, M., Cho, H., Roy, T. K., Mirica, L. M., & Sharma, A. K. (2017) · Inorganica Chimica Acta · doi:10.1016/j.ica.2017.11.029 · Cited by 40 · see citing works

Hydrogen–Deuterium Exchange and Mass Spectrometry Reveal the pH-Dependent Conformational Changes of Diphtheria Toxin T Domain

Li, J., Rodnin, M. V., Ladokhin, A. S., & Gross, M. L. (2014) · Biochemistry · doi:10.1021/bi500893y · Cited by 37 · see citing works

Protein Footprinting and X-ray Crystallography Reveal the Interaction of PD-L1 and a Macrocyclic Peptide

Niu, B., Appleby, T. C., Wang, R., Morar, M., Voight, J., Villaseñor, A. G., Clancy, S., Wise, S. J., Belzile, J.-P., Papalia, G. A., et al. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00822 · Cited by 37 · see citing works

An Improved Fast Photochemical Oxidation of Proteins (FPOP) Platform for Protein Therapeutics

Zhang, Y., Rempel, D. L., Zhang, H., & Gross, M. L. (2014) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-014-1055-0 · Cited by 35 · see citing works

Biological and methodological complexities of beta‐amyloid peptide: Implications for Alzheimer’s disease research

Matuszyk, M. M., Garwood, C. J., Ferraiuolo, L., Simpson, J. E., Staniforth, R. A., & Wharton, S. B. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15538 · Cited by 35 · see citing works

Using mass spectrometry‐based methods to understand amyloid formation and inhibition of alpha‐synuclein and amyloid beta

Wagner, W. J., & Gross, M. L. (2022) · Mass Spectrometry Reviews · doi:10.1002/mas.21814 · Cited by 35 · see citing works

Characterizing the Structure and Oligomerization of Major Royal Jelly Protein 1 (MRJP1) by Mass Spectrometry and Complementary Biophysical Tools

Mandacaru, S. C., do Vale, L. H. F., Vahidi, S., Xiao, Y., Skinner, O. S., Ricart, C. A. O., Kelleher, N. L., de Sousa, M. V., & Konermann, L. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00020 · Cited by 33 · see citing works

Does deamidation cause protein unfolding? A top‐down tandem mass spectrometry study

Soulby, A., Heal, J. W., Barrow, M. P., Römer, R. A., & O’Connor, P. B. (2015) · Protein Science · doi:10.1002/pro.2659 · Cited by 33 · see citing works

Mechanism of Protein Aggregation Inhibition by Arginine: Blockage of Anionic Side Chains Favors Unproductive Encounter Complexes

Ng, Y. K., & Konermann, L. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c14180 · Cited by 32 · see citing works

Pulsed Hydrogen–Deuterium Exchange Illuminates the Aggregation Kinetics of α-Synuclein, the Causative Agent for Parkinson’s Disease

Illes‐Toth, E., Rempel, D. L., & Gross, M. L. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00052 · Cited by 31 · see citing works

Mechanism of Thermal Protein Aggregation: Experiments and Molecular Dynamics Simulations on the High-Temperature Behavior of Myoglobin

Ng, Y. K., Tajoddin, N. N., Scrosati, P. M., & Konermann, L. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c07210 · Cited by 30 · see citing works

A Synchrotron-Based Hydroxyl Radical Footprinting Analysis of Amyloid Fibrils and Prefibrillar Intermediates with Residue-Specific Resolution

Klinger, A. L., Kiselar, J., Ilchenko, S., Komatsu, H., Chance, M. R., & Axelsen, P. H. (2014) · Biochemistry · doi:10.1021/bi5010409 · Cited by 30 · see citing works

Illuminating Intrinsically Disordered Proteins with Integrative Structural Biology

Evans, R., Ramisetty, S. K., Kulkarni, P., & Weninger, K. (2023) · Biomolecules · doi:10.3390/biom13010124 · Cited by 27 · see citing works

Structural Transitions and Interactions in the Early Stages of Human Glucagon Amyloid Fibrillation

Moorthy, B. S., Ghomi, H. T., Lill, M. A., & Topp, E. M. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.01.004 · Cited by 27 · see citing works

Native MS and ECD Characterization of a Fab–Antigen Complex May Facilitate Crystallization for X-ray Diffraction

Zhang, Y., Cui, W., Wecksler, A. T., Zhang, H., Molina, P., Deperalta, G., & Gross, M. L. (2016) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1398-9 · Cited by 27 · see citing works

The Aggregation Pattern of Aβ1–40 is Altered by the Presence of N‐Truncated Aβ4–40 and/or CuII in a Similar Way through Ionic Interactions

Stefaniak, E., Atrián‐Blasco, E., Goch, W., Sabater, L., Hureau, C., & Bal, W. (2020) · Chemistry - A European Journal · doi:10.1002/chem.202004484 · Cited by 26 · see citing works

Exploration of Resveratrol as a Potent Modulator of α-Synuclein Fibril Formation

Illes‐Toth, E., Rempel, D. L., & Gross, M. L. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00571 · Cited by 25 · see citing works

Neurodegenerative Proteinopathies in the Proteoform Spectrum—Tools and Challenges

Noor, A., Zafar, S., & Zerr, I. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031085 · Cited by 24 · see citing works

Self-assembly of stable oligomeric and fibrillar aggregates of Aβ peptides relevant to Alzheimer's disease: morphology dependent Cu/heme toxicity and inhibition of PROS generation

Sengupta, K., Chatterjee, S., Pramanik, D., Dey, S. G., & Dey, A. (2014) · Dalton Transactions · doi:10.1039/c4dt01991a · Cited by 24 · see citing works

N-Terminus Binding Preference for Either Tanshinone or Analogue in Both Inhibition of Amyloid Aggregation and Disaggregation of Preformed Amyloid Fibrils—Toward Introducing a Kind of Novel Anti-Alzheimer Compounds

Dong, M., Zhao, W., Hu, D., Ai, H., & Kang, B. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00080 · Cited by 24 · see citing works

Collagen hydrogel confinement of Amyloid-β (Aβ) accelerates aggregation and reduces cytotoxic effects

Simpson, L. W., Szeto, G. L., Boukari, H., Good, T. A., & Leach, J. B. (2019) · Acta Biomaterialia · doi:10.1016/j.actbio.2020.05.030 · Cited by 24 · see citing works

Applications of Mass Spectrometry in the Onset of Amyloid Fibril Formation: Focus on the Analysis of Early-Stage Oligomers

Hu, J., & Zheng, Q. (2020) · Frontiers in Chemistry · doi:10.3389/fchem.2020.00324 · Cited by 23 · see citing works

Developments in Trapped Ion Mobility Mass Spectrometry to Probe the Early Stages of Peptide Aggregation

Depland, A. D., Stroganova, I., Wootton, C. A., & Rijs, A. M. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.2c00253 · Cited by 23 · see citing works

Ultrasensitive label-free photoelectrochemical immunosensor for the detection of amyloid β-protein based on Zn:SnO2/SnS2-Au nanocomposites

Gao, N., Zhang, Y., Gao, K., Xie, J., Liu, L., Li, Y., Qiu, L., Wei, Q. L., Ma, H., & Pang, X. (2019) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2019.127576 · Cited by 23 · see citing works

Hydrogen/Deuterium Exchange-Protected Oligomers Populated during Aβ Fibril Formation Correlate with Neuronal Cell Death

Serra-Vidal, B., Pujadas, L., Rossi, D. P., Soriano, E., Madurga, S., & Carulla, N. (2014) · ACS Chemical Biology · doi:10.1021/cb500621x · Cited by 22 · see citing works

Tracking Higher Order Protein Structure by Hydrogen-Deuterium Exchange Mass Spectrometry

Benhaim, M. A., Lee, K. K., & Guttman, M. (2018) · Protein and Peptide Letters · doi:10.2174/0929866526666181212165037 · Cited by 22 · see citing works

Evidence for a Partially Stalled γ Rotor in F1-ATPase from Hydrogen–Deuterium Exchange Experiments and Molecular Dynamics Simulations

Rios, A. M. M., Vahidi, S., Dunn, S. D., & Konermann, L. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b08692 · Cited by 21 · see citing works

Immunosensor incorporating half-antibody fragment for electrochemical monitoring of amyloid-β fibrils in artificial blood plasma

Gopal, P., Malecka, K., Dehaen, W., Radecki, J., & Radecka, H. (2020) · Bioelectrochemistry · doi:10.1016/j.bioelechem.2020.107643 · Cited by 21 · see citing works

Fibrillation of Human Calcitonin and Its Analogs: Effects of Phosphorylation and Disulfide Reduction

Renawala, H., Chandrababu, K. B., & Topp, E. M. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.11.009 · Cited by 21 · see citing works

Mass Spectrometry-Based Protein Footprinting for Protein Structure Characterization

Cheng, M., & Gross, M. L. (2025) · Accounts of Chemical Research · doi:10.1021/acs.accounts.4c00545 · Cited by 20 · see citing works

Mass spectrometric insights into protein aggregation

Pukala, T. L. (2023) · Essays in Biochemistry · doi:10.1042/ebc20220103 · Cited by 19 · see citing works

Mass Spectrometry-Based Structural Proteomics for Metal Ion/Protein Binding Studies

Lin, Y., & Gross, M. L. (2022) · Biomolecules · doi:10.3390/biom12010135 · Cited by 18 · see citing works

Semax, a Synthetic Regulatory Peptide, Affects Copper-Induced Abeta Aggregation and Amyloid Formation in Artificial Membrane Models

Sciacca, M. F. M., Николаевна, Н. И., Giuffrida, M. L., & Attanasio, F. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00707 · Cited by 18 · see citing works

Detection of conformation types of cyclosporin retaining intramolecular hydrogen bonds by mass spectrometry

Hyung, S., Feng, X., Che, Y., Stroh, J. G., & Shapiro, M. J. (2014) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-014-8023-1 · Cited by 18 · see citing works

Mass Determination of Entire Amyloid Fibrils by Using Mass Spectrometry

Doussineau, T., Mathevon, C., Altamura, L., Vendrely, C., Dugourd, P., Forge, V., & Antoine, R. (2015) · Angewandte Chemie · doi:10.1002/ange.201508995 · Cited by 18 · see citing works

Continuous and Pulsed Hydrogen–Deuterium Exchange and Mass Spectrometry Characterize CsgE Oligomerization

Wang, H., Shu, Q., Rempel, D. L., Frieden, C., & Gross, M. L. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00871 · Cited by 18 · see citing works

Side-chain moieties from the N-terminal region of Aβ are Involved in an oligomer-stabilizing network of interactions

Przygońska, K., Poznański, J. T., Mistarz, U. H., Rand, K. D., & Dadlez, M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0201761 · Cited by 18 · see citing works

Chemical Penetration Enhancers Increase Hydrogen Peroxide Uptake in C. elegans for In Vivo Fast Photochemical Oxidation of Proteins

Espino, J. A., Zhang, Z., & Jones, L. M. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00245 · Cited by 16 · see citing works

Understanding curli amyloid-protein aggregation by hydrogen–deuterium exchange and mass spectrometry

Wang, H., Shu, Q., Rempel, D. L., Frieden, C., & Gross, M. L. (2016) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2016.10.006 · Cited by 16 · see citing works

MS ‐Based Hydroxyl Radical Footprinting: Methodology and Application of Fast Photochemical Oxidation of Proteins ( FPOP )

Niu, B., & Gross, M. L. (2019) · Wiley eBooks · doi:10.1002/9781118970195.ch15 · Cited by 16 · see citing works

The effects of fluorescent labels on Aβ 42 aggregation detected by fluorescence correlation spectroscopy

Zheng, Y.-P., Xu, L., Yang, J., Peng, X.-L., Wang, H., Yu, N., Hua, Y., Zhao, J., He, J., & Hong, T. (2018) · Biopolymers · doi:10.1002/bip.23237 · Cited by 15 · see citing works

Pulsed Hydrogen–Deuterium Exchange Reveals Altered Structures and Mechanisms in the Aggregation of Familial Alzheimer’s Disease Mutants

Illes‐Toth, E., Meisl, G., Rempel, D. L., Knowles, T. P. J., & Gross, M. L. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00072 · Cited by 15 · see citing works

Effect of pH on Aβ 42 Monomer and Fibril‐like Oligomers—Decoding in Silico of the Roles of p K Values of Charged Residues

Zhao, W., & Ai, H. (2018) · ChemPhysChem · doi:10.1002/cphc.201701384 · Cited by 15 · see citing works

Proteolysis of Amyloid β by Lysosomal Enzymes as a Function of Fibril Morphology

Lambeth, T. R., & Julian, R. R. (2021) · ACS Omega · doi:10.1021/acsomega.1c03915 · Cited by 14 · see citing works

A label-free electrochemical immunosensor based on PtCoCu PNPs/NB-rGO as a dual signal amplification platform for sensitive detection of β-Amyloid1-42

Wang, Y., Wang, P., Zhao, Z., Ye, S., Wang, W., Liu, Q., Yang, L., Zhang, D., & Li, Y. (2023) · Bioelectrochemistry · doi:10.1016/j.bioelechem.2023.108405 · Cited by 14 · see citing works

Determination of regions involved in amyloid fibril formation for Aβ(1-40) peptide

Surin, A. K., Grigorashvili, E. I., Suvorina, M. Y., Selivanova, O. M., & Galzitskaya, O. V. (2016) · Biochemistry (Moscow) · doi:10.1134/s0006297916070130 · Cited by 14 · see citing works

Combination of circular dichroism spectroscopy and size-exclusion chromatography coupled with HDX-MS for studying global conformational structures of peptides in solution

Schiavone, N. M., Pirrone, G. F., Guetschow, E. D., Mangion, I. K., & Makarov, A. A. (2018) · Talanta · doi:10.1016/j.talanta.2018.09.077 · Cited by 13 · see citing works

THE MAKING OF A FOOTPRINT IN PROTEIN FOOTPRINTING: A REVIEW IN HONOR OF MICHAEL L. GROSS

McKenzie-Coe, A., Shortt, R. L., & Jones, L. (2020) · Mass spectrometry reviews (Print) · doi:10.1002/mas.21632 · Cited by 11 · see citing works

Molecular Insights into Cu/Zn Metal Response to the Amyloid β-Peptide (1–42)

Sunda, A. P., & Sharma, A. K. (2023) · ACS Physical Chemistry Au · doi:10.1021/acsphyschemau.3c00041 · Cited by 10 · see citing works

Bifunctional Copper Chelators Capable of Reducing Aβ Aggregation and Aβ-Induced Oxidative Stress

Krasnovskaya, O. O., Abramchuk, D., Vaneev, A. N., Gorelkin, P. V., Abakumov, M. A., Timoshenko, R. V., Kuzmichev, I., Chmelyuk, N. S., Vadekhina, V. V., Kuanaeva, R. M., et al. (2024) · ACS Omega · doi:10.1021/acsomega.4c03152 · Cited by 10 · see citing works

Trifluoroethanol Partially Unfolds G93A SOD1 Leading to Protein Aggregation: A Study by Native Mass Spectrometry and FPOP Protein Footprinting

Niu, B., Mackness, B. C., Zitzewitz, J. A., Matthews, C. R., & Gross, M. L. (2020) · Biochemistry · doi:10.1021/acs.biochem.0c00425 · Cited by 10 · see citing works

Evaluation of Anti‐Alzheimer's Potential of Azo‐Stilbene‐Thioflavin‐T derived Multifunctional Molecules: Synthesis, Metal and Aβ Species Binding and Cholinesterase Activity

Rana, M., Terpstra, K., GUTIERREZ, C. G., Xu, K., Arya, H., Bhatt, T. K., Mirica, L. M., & Sharma, A. K. (2024) · Chemistry - A European Journal · doi:10.1002/chem.202402748 · Cited by 8 · see citing works

An Original Monomer Sampling from a Ready‐Made Aβ42 NMR Fibril Suggests a Turn‐β‐Strand Synergetic Seeding Mechanism

Liu, C., Zhao, W., Xing, X., Shi, H., Kang, B., Liu, H., Li, P., & Ai, H. (2019) · ChemPhysChem · doi:10.1002/cphc.201801137 · Cited by 8 · see citing works

Probing of Amyloid Aβ (14-23) Trimers by Single-Molecule Force Spectroscopy.

Maity, S., & Lyubchenko, Y. L. (2016) · PubMed · Cited by 8 · see citing works

Folding dynamics of Aβ42 monomer at pH 4.0–7.5 with and without physiological salt conditions – does the β1 or β2 region fold first?

Xing, X., Liu, C., Yang, H., Nouman, M. F., & Ai, H. (2020) · New Journal of Chemistry · doi:10.1039/d0nj01090a · Cited by 8 · see citing works

Turn-on fluorescent sensors for Cu-rich amyloid β peptide aggregates

Huang, Y., Sun, L., & Mirica, L. M. (2022) · Sensors & Diagnostics · doi:10.1039/d2sd00028h · Cited by 7 · see citing works

Origin of stronger binding of ionic pair (IP) inhibitor to Aβ42 than the equimolar neutral counterparts: synergy mechanism of IP in disrupting Aβ42 protofibril and inhibiting Aβ42 aggregation under two pH conditions

Xu, W. W., Mei, J., Wang, C., Yang, H., Ma, X., Gao, W., Ahmad, S., & Ai, H. (2023) · Physical Chemistry Chemical Physics · doi:10.1039/d3cp01683h · Cited by 7 · see citing works

Aggregation Dynamics Characteristics of Seven Different Aβ Oligomeric Isoforms-Dependence on the Interfacial Interaction

Guan, Y., Li, Y., Gao, W., Mei, J., Xu, W. W., Wang, C., & Ai, H. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00585 · Cited by 7 · see citing works

Amyloid β Hypothesis in the Development of Therapeutic Agents for Alzheimer’s Disease

Adeniji, A. O., Adams, P. W., & Mody, V. V. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802810-0.00007-6 · Cited by 7 · see citing works

Biophysical Dissection of Isolated GPCRs: The Adenosine A2A Receptor under the Bistouries

Banères, J., Botzanowski, T., Boutin, J. A., Calamini, B., Castel, J.-G., Catoire, L. J., Cianférani, S., Demesmay, C., Ferguson, G., Ferry, G., et al. (2023) · Receptors · doi:10.3390/receptors2010004 · Cited by 5 · see citing works

Hydrogen Exchange Mass Spectrometry for the Analysis of Ligand Binding and Protein Aggregation

Zhang, Y., Rempel, D. L., & Gross, M. L. (2016) · Wiley eBooks · doi:10.1002/9781118703748.ch11 · Cited by 5 · see citing works

A Model Study to Assess Fibrillation and Product Stability to Support Peptide Drug Design

Renawala, H., Chandrababu, K. B., Smith, K. J., D’Addio, S. M., & Topp, E. M. (2024) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.3c00996 · Cited by 4 · see citing works

Mass-Spectrometry-Based GEE Footprinting Characterizes Kinetic Mechanisms and Sites of Conformational Change in Amyloid β 1–42 Aggregation

Kuang, X. C., Rempel, D. L., Lin, Y., & Gross, M. L. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00033 · Cited by 4 · see citing works

Molecular mechanisms of direct and indirect interplay between amyloid β42 oligomer and characteristic lipids

Mei, J., Liu, C., Yang, H., Ma, X., & Ai, H. (2022) · ChemPhysMater · doi:10.1016/j.chphma.2021.12.002 · Cited by 4 · see citing works

Toxicity Mechanism of Aβ42 Oligomer in the Binding between the GABABR1a sushi1 Domain and Amyloid Precursor Protein 9mer: A Mechanism like Substitution Reaction

Mei, J., Yang, H., Ahmad, S., Ma, X., Xu, W. W., Gao, W., Li, Y., Wang, C., & Ai, H. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00311 · Cited by 4 · see citing works

Identification of Crocin as a New hIAPP Amyloid Inhibitor via a Simple Yet Highly Biospecific Screening System

Lu, J., Lu, Z., Liu, L., Li, X., Yu, W., & Lu, X. (2021) · Chemistry & Biodiversity · doi:10.1002/cbdv.202100270 · Cited by 4 · see citing works

Pulsed Hydrogen–Deuterium Exchange Reveals Altered Structures and Mechanisms in the Aggregation of Familial Alzheimer’s Disease Mutants

Illes‐Toth, E., Meisl, G., Rempel, D. L., Knowles, T. P. J., & Gross, M. L. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00072 · Cited by 15 · see citing works

Simultaneous monitoring of peptide aggregate distributions, structure, and kinetics using amide hydrogen exchange: Application to Aβ(1‐40) fibrillogenesis

Qi, W., Zhang, A., Patel, D. A., Lee, S., Harrington, J. L., Zhao, L., Schaefer, D., Good, T. A., & Fernández, E. (2008) · Biotechnology and Bioengineering · doi:10.1002/bit.21846 · Cited by 31 · see citing works

Hydrogen exchange studies on Alzheimer's amyloid‐β peptides by mass spectrometry using matrix‐assisted laser desorption/ionization and electrospray ionization

Kraus, M., Bienert, M., & Krause, E. (2002) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.901 · Cited by 29 · see citing works

Hydrogen/Deuterium Exchange-Protected Oligomers Populated during Aβ Fibril Formation Correlate with Neuronal Cell Death

Serra-Vidal, B., Pujadas, L., Rossi, D. P., Soriano, E., Madurga, S., & Carulla, N. (2014) · ACS Chemical Biology · doi:10.1021/cb500621x · Cited by 22 · see citing works

Hydrogen Exchange-Mass Spectrometry Analysis of β-Amyloid Peptide Structure

Wang, S. S. ‐., Tobler, S. A., Good, T. A., & Fernández, E. (2003) · Biochemistry · doi:10.1021/bi0342766 · Cited by 53 · see citing works