Protein folding and misfolding

Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo

Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291 · see citing works

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064 · see citing works

Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein

Hartl, F. U., & Hayer-Hartl, M. K. (2002) · Science · doi:10.1126/science.1068408 · Cited by 3,335 · see citing works

The Hsp70 and Hsp60 Chaperone Machines

Bukau, B., & Horwich, A. L. (1998) · Cell · doi:10.1016/s0092-8674(00)80928-9 · Cited by 2,816 · see citing works

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434 · see citing works

From Levinthal to pathways to funnels

Dill, K. A., & Chan, H. S. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb0197-10 · Cited by 2,293 · see citing works

Impairment of the Ubiquitin-Proteasome System by Protein Aggregation

Bence, N., Sampat, R. M., & Kopito, R. R. (2001) · Science · doi:10.1126/science.292.5521.1552 · Cited by 2,192 · see citing works

Structure and Mechanism in Protein Science

Fersht, A. (2017) · WORLD SCIENTIFIC eBooks · doi:10.1142/10574 · Cited by 2,078 · see citing works

Protein misfolding, evolution and disease

Dobson, C. M. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01445-0 · Cited by 1,960 · see citing works

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 1,847 · see citing works

Structure and Mechanism in Protein Science. A guide to Enzyme Catalysis and Protein Folding

Howland, J. L. (2001) · Biochemistry and Molecular Biology Education · Cited by 1,823 · see citing works

P <scp>ROTOFIBRILS</scp> , P <scp>ORES</scp> , F <scp>IBRILS, AND</scp> N <scp>EURODEGENERATION</scp> : Separating the Responsible Protein Aggregates from The Innocent Bystanders

Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650 · see citing works

Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution

Stefani, M., & Dobson, C. M. (2003) · Journal of Molecular Medicine · doi:10.1007/s00109-003-0464-5 · Cited by 1,643 · see citing works

Rapid degradation of a large fraction of newly synthesized proteins by proteasomes

Schubert, U., Antón, L. C., Gibbs, J. S., Norbury, C. C., Yewdell, J. W., & Bennink, J. R. (2000) · Nature · doi:10.1038/35008096 · Cited by 1,536 · see citing works

Contact order, transition state placement and the refolding rates of single domain proteins 1 1Edited by P. E. Wright

Plaxco, K. W., Simons, K. T., & Baker, D. A. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1645 · Cited by 1,520 · see citing works

Amyloid pores from pathogenic mutations

Lashuel, H. A., Hartley, D. M., Petre, B. M., Walz, T., & Lansbury, P. T. (2002) · Nature · doi:10.1038/418291a · Cited by 1,291 · see citing works

Role of Escherichia coli Curli Operons in Directing Amyloid Fiber Formation

Chapman, M., Robinson, L. S., Pinkner, J., Roth, R., Heuser, J., Hammar, M., Normark, S., & Hultgren, S. (2002) · Science · doi:10.1126/science.1067484 · Cited by 1,282 · see citing works

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. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222681699 · Cited by 1,280 · see citing works

Toxic Proteins in Neurodegenerative Disease

Taylor, J. P., Hardy, J., & Fischbeck, K. H. (2002) · Science · doi:10.1126/science.1067122 · Cited by 1,251 · see citing works

Macromolecular crowding: an important but neglected aspect of the intracellular environment

Ellis, R. J. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00172-x · Cited by 1,153 · cited 1× · see citing works

Navigating the folding routes

Wolynes, P., Onuchic, J., & Thirumalai, D. (1995) · Science · doi:10.1126/science.7886447 · Cited by 1,080 · see citing works

Rationalization of the effects of mutations on peptide andprotein aggregation rates

Chiti, F., Stefani, M., Taddei, N., Ramponi, G., & Dobson, C. M. (2003) · Nature · doi:10.1038/nature01891 · Cited by 1,072 · see citing works

The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways

Kelly, J. W. (1998) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(98)80016-x · Cited by 998 · see citing works

Cellular Defenses against Unfolded Proteins

Sherman, M. Y., & Goldberg, A. L. (2001) · Neuron · doi:10.1016/s0896-6273(01)00177-5 · Cited by 984 · see citing works

Prion Diseases and the BSE Crisis

Prusiner, S. B. (1997) · Science · doi:10.1126/science.278.5336.245 · Cited by 958 · see citing works

The structural basis of protein folding and its links with human disease

Dobson, C. M. (2001) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2000.0758 · Cited by 927 · see citing works

Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy

Schuler, B., Lipman, E. A., & Eaton, W. A. (2002) · Nature · doi:10.1038/nature01060 · Cited by 921 · see citing works

Protein Folding: A Perspective from Theory and Experiment

Dobson, C. M., Šali, A., & Karplus, M. (1998) · Angewandte Chemie International Edition · doi:10.1002/(sici)1521-3773(19980420)37:7 · Cited by 859 · see citing works

A surprising simplicity to protein folding

Baker, D. A. (2000) · Nature · doi:10.1038/35011000 · Cited by 778 · see citing works

The Structure of Amyloid Fibrils by Electron Microscopy and X-Ray Diffraction

Sunde, M., & BLAKE, C. (1997) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60320-4 · Cited by 768 · see citing works

Absolute comparison of simulated and experimental protein-folding dynamics

Snow, C. D., Nguyen, H., Pande, V. S., & Gruebele, M. (2002) · Nature · doi:10.1038/nature01160 · Cited by 701 · see citing works

A yeast prion provides a mechanism for genetic variation and phenotypic diversity

True, H. L., & Lindquist, S. L. (2000) · Nature · doi:10.1038/35035005 · Cited by 672 · see citing works

Quality control in the secretory pathway

Hammond, C., & Helenius, A. (1995) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(95)80009-3 · Cited by 672 · see citing works

Hsp70 and Hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils

Muchowski, P. J., Schaffar, G., Sittler, A., Wanker, E. E., Hayer-Hartl, M. K., & Hartl, F. U. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.140202897 · Cited by 668 · see citing works

The unfolded protein response in nutrient sensing and differentiation

Kaufman, R. J., Scheuner, D. L., Schröder, M., Shen, X., Lee, K., Liu, C. Y., & Arnold, S. M. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm829 · Cited by 607 · see citing works

Rescuing the function of mutant p53

Bullock, A. N., & Fersht, A. R. (2001) · Nature reviews. Cancer · doi:10.1038/35094077 · Cited by 565 · see citing works

Defective protein folding as a basis of human disease

Thomas, P., Qu, B.-H., & Pedersen, P. L. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)89100-8 · Cited by 531 · see citing works

The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation

Fändrich, M., & Dobson, C. M. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf573 · Cited by 526 · see citing works

Protein folding mediated by solvation: Water expulsion and formation of the hydrophobic core occur after the structural collapse

Cheung, M. S., Garcı́a, A. E., & Onuchic, J. N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.022387699 · Cited by 513 · see citing works

Cryo‐electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing

Jiménez, J. L., Guijarro, J. I., Orlova, E. V., Zurdo, J., Dobson, C. M., Sunde, M., & Saibil, H. R. (1999) · The EMBO Journal · doi:10.1093/emboj/18.4.815 · Cited by 503 · see citing works

Understanding protein folding via free-energy surfaces from theory and experiment

Dinner, A. R., Šali, A., Smith, L. J., Dobson, C. M., & Karplus, M. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01610-8 · Cited by 496 · see citing works

Protein Folding and Unfolding at Atomic Resolution

Fersht, A. R., & Daggett, V. (2002) · Cell · doi:10.1016/s0092-8674(02)00620-7 · Cited by 495 · see citing works

F<scp>ROM</scp>F<scp>OLDING</scp>T<scp>HEORIES TO</scp>F<scp>OLDING</scp>P<scp>ROTEINS</scp>: A Review and Assessment of Simulation Studies of Protein Folding and Unfolding

Shea, J.-E., & Brooks III, C. L. (2001) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.52.1.499 · Cited by 481 · see citing works

The complete folding pathway of a protein from nanoseconds to microseconds

Mayor, U., Guydosh, N. R., Johnson, C. M., Grossmann, J. G., Sato, S., Jas, G. S., Freund, S. M. V., Alonso, D. O. V., Daggett, V., & Fersht, A. R. (2003) · Nature · doi:10.1038/nature01428 · Cited by 458 · see citing works

Three key residues form a critical contact network in a protein folding transition state

Vendruscolo, M., Paci, E., Dobson, C. M., & Karplus, M. (2001) · Nature · doi:10.1038/35054591 · Cited by 429 · see citing works

Kinetic partitioning of protein folding and aggregation

Chiti, F., Taddei, N., Baroni, F., Capanni, C., Stefani, M., Ramponi, G., & Dobson, C. M. (2002) · Nature Structural Biology · doi:10.1038/nsb752 · Cited by 423 · see citing works

Folding at the speed limit

Yang, W. Y., & Gruebele, M. (2003) · Nature · doi:10.1038/nature01609 · Cited by 405 · see citing works

Clusterin is a secreted mammalian chaperone

Wilson, M. R., & Easterbrook‐Smith, S. B. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01534-0 · Cited by 380 · see citing works

Protein-misfolding diseases: Getting out of shape

Dobson, C. M. (2002) · Nature · doi:10.1038/418729a · Cited by 341 · see citing works

Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism

Fersht, A. R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.4.1525 · Cited by 323 · see citing works

Kinetic role of early intermediates in protein folding

Röder, H., & Colón, W. (1997) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(97)80004-8 · Cited by 316 · see citing works

Oligomer Formation By 3D Domain Swapping: A Model For Protein Assembly And Misassembly

Schlunegger, M. P., Bennett, M. D., & Eisenberg, D. S. (1997) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60319-8 · Cited by 286 · see citing works

Evidence for Sequential Barriers and Obligatory Intermediates in Apparent Two-state Protein Folding

Sanchez, I. E., & Kiefhaber, T. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01230-5 · Cited by 249 · see citing works

A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme

Dumoulin, M., Last, A. M., Desmyter, A., Decanniere, K., Canet, D., Larsson, G., Spencer, A. G., Archer, D. B., Sasse, J., Muyldermans, S., et al. (2003) · Nature · doi:10.1038/nature01870 · Cited by 245 · see citing works

Amyloidosis

Tan, S., & Pepys, M. B. (1994) · Histopathology · doi:10.1111/j.1365-2559.1994.tb00001.x · Cited by 231 · see citing works

A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro

Ramı́rez-Alvarado, M., Merkel, J. S., & Regan, L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.150091797 · Cited by 229 · see citing works

Protein aggregation in disease: a role for folding intermediates forming specific multimeric interactions

Horwich, A. L. (2002) · Journal of Clinical Investigation · doi:10.1172/jci16781 · Cited by 197 · see citing works

Enzymes that catalyse the restructuring of proteins

Schiene, C., & Fischer, G. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00046-9 · Cited by 188 · see citing works

Protein aggregation in disease: a role for folding intermediates forming specific multimeric interactions

Horwich, A. L. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216781 · Cited by 185 · see citing works

The topomer search model: A simple, quantitative theory of two‐state protein folding kinetics

Makarov, D. E., & Plaxco, K. W. (2003) · Protein Science · doi:10.1110/ps.0220003 · Cited by 182 · see citing works

Nature disfavors sequences of alternating polar and non-polar amino acids: implications for amyloidogenesis 1 1Edited by F. E. Cohen

Broome, B. M., & Hecht, M. H. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3514 · Cited by 169 · see citing works

Kinetics and Dynamics of Loops, α-Helices, β-Hairpins, and Fast-Folding Proteins

Eaton, W. A., Muñoz, V., Thompson, P. A., Henry, E. R., & Hofrichter, J. (1998) · Accounts of Chemical Research · doi:10.1021/ar9700825 · Cited by 156 · see citing works

Protein Folding and Disease: a view from the first Horizon Symposium

Dobson, C. M. (2003) · Nature Reviews Drug Discovery · doi:10.1038/nrd1013 · Cited by 144 · see citing works

Protein folding and misfolding: a paradigm of self–assembly and regulation in complex biological systems

Vendruscolo, M., Zurdo, J., MacPhee, C. E., & Dobson, C. M. (2003) · Philosophical Transactions of the Royal Society A Mathematical Physical and Engineering Sciences · doi:10.1098/rsta.2003.1194 · Cited by 140 · see citing works

From Computer Simulations to Human Disease

Radford, S. E., & Dobson, C. M. (1999) · Cell · doi:10.1016/s0092-8674(00)80739-4 · Cited by 136 · see citing works

Matching speed and stability

Baldwin, R. L. (1994) · Nature · doi:10.1038/369183a0 · Cited by 130 · see citing works

Low levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: Implications for the study of amyloid formation

Nilsson, M. R., Driscoll, M., & Raleigh, D. P. (2002) · Protein Science · doi:10.1110/ps.48702 · Cited by 124 · see citing works

Amyloid as a natural product

Kelly, J. W., & Balch, W. E. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200304074 · Cited by 116 · see citing works

Folding of a nascent peptide on the ribosome

Hardesty, B., & Kramer, G. (2000) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(00)66026-9 · Cited by 115 · see citing works

Chaperone overload is a possible contributor to ‘civilization diseases’

Csermely, P. (2001) · Trends in Genetics · doi:10.1016/s0168-9525(01)02495-7 · Cited by 100 · see citing works

The Kinetic Pathway of Folding of Barnase

Khan, F., Chuang, J. I., Gianni, S., et al. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.08.024 · Cited by 83 · see citing works

Sick chaperones and ageing: a perspective

Macario, A. J. L. (2002) · Ageing Research Reviews · doi:10.1016/s1568-1637(01)00005-8 · Cited by 81 · see citing works

Structures and relative free energies of partially folded states of proteins

Vendruscolo, M., Paci, E., Karplus, M., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2036516100 · Cited by 80 · see citing works

Aggregation-Induced Emission: Together We Shine, United We Soar!

Mei, J., Leung, N. L. C., Kwok, R. T. K., Lam, J. W. Y., & Tang, B. Z. (2015) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00263 · Cited by 8,270 · see citing works

Mechanisms of Diabetic Complications

Forbes, J. M., & Cooper, M. E. (2013) · Physiological Reviews · doi:10.1152/physrev.00045.2011 · Cited by 2,890 · see citing works

Exploring and Engineering the Cell Surface Interface

Stevens, M. M., & George, J. H. (2005) · Science · doi:10.1126/science.1106587 · Cited by 2,607 · see citing works

The amyloid state and its association with protein misfolding diseases.

Knowles, T. P. J., Vendruscolo, M., & Dobson, C. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3810 · Cited by 2,382 · see citing works

Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels

Kato, M., Han, T. W., Xie, S., Shi, K., Du, X., Wu, L. C., Mirzaei, H., Goldsmith, E. J., Longgood, J., Pei, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.017 · Cited by 2,012 · see citing works

The Protein-Folding Problem, 50 Years On

Dill, K. A., & MacCallum, J. L. (2012) · Science · doi:10.1126/science.1219021 · Cited by 1,699 · see citing works

Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases

Guo, J. L., & Lee, V. M. Y. (2014) · Nature Medicine · doi:10.1038/nm.3457 · Cited by 641 · see citing works

Prions as adaptive conduits of memory and inheritance

Shorter, J., & Lindquist, S. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1616 · Cited by 558 · see citing works

The CamSol method of rational design of protein mutants with enhanced solubility

Sormanni, P., Aprile, F. A., & Vendruscolo, M. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.09.026 · Cited by 494 · see citing works

Protein Quality Control in the Cytosol and the Endoplasmic Reticulum: Brothers in Arms

Buchberger, A., Bukau, B., & Sommer, T. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.001 · Cited by 483 · see citing works

Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell

Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436 · see citing works

Biology and Genetics of Prions Causing Neurodegeneration

Prusiner, S. B. (2013) · Annual Review of Genetics · doi:10.1146/annurev-genet-110711-155524 · Cited by 455 · see citing works

Prebiotic Peptides: Molecular Hubs in the Origin of Life

Frenkel-Pinter, M., Samanta, M., Ashkenasy, G., & Leman, L. J. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00664 · Cited by 354 · see citing works

Tau Post-translational Modifications: Dynamic Transformers of Tau Function, Degradation, and Aggregation

Alquezar, C., Arya, S., & Kao, A. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.595532 · Cited by 367 · see citing works

Physical limits of cells and proteomes

Dill, K. A., Ghosh, K., & Schmit, J. D. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1114477108 · Cited by 298 · see citing works

Soluble protein oligomers as emerging toxins in Alzheimer’s and other amyloid diseases

Ferreira, S. T., Vieira, M. N. N., & De Felice, F. G. (2007) · IUBMB Life · doi:10.1080/15216540701283882 · Cited by 335 · see citing works

Reducing the RNA binding protein TIA1 protects against tau-mediated neurodegeneration in vivo

Apicco, D. J., Ash, P. E. A., Maziuk, B., LeBlang, C., Medalla, M., Al Abdullatif, A., Ferragud, A., Botelho, E., Ballance, H. I., Dhawan, U., et al. (2018) · Nature Neuroscience · doi:10.1038/s41593-017-0022-z · Cited by 281 · see citing works

Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins

Ciryam, P., Tartaglia, G. G., Morimoto, R. I., Dobson, C. M., & Vendruscolo, M. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.09.043 · Cited by 270 · see citing works

Firefly luciferase mutants as sensors of proteome stress

Gupta, R., Kasturi, P., Bracher, A., Loew, C., Zheng, M., Villella, A., Garza, D., Hartl, F. U., & Raychaudhuri, S. (2011) · Nature Methods · doi:10.1038/nmeth.1697 · Cited by 219 · see citing works

Consensus protein design

Porebski, B. T., & Buckle, A. M. (2016) · Protein Engineering Design and Selection · doi:10.1093/protein/gzw015 · Cited by 215 · see citing works

The <i>Silver</i> locus product Pmel17/gp100/Silv/ME20: controversial in name and in function

Theos, A. C., Truschel, S. T., Raposo, G., & Marks, M. S. (2005) · Pigment Cell Research · doi:10.1111/j.1600-0749.2005.00269.x · Cited by 224 · see citing works

Potential aggregation prone regions in biotherapeutics: A survey of commercial monoclonal antibodies

Wang, X., Das, T. K., Singh, S. K., & Kumar, S. (2009) · mAbs · doi:10.4161/mabs.1.3.8035 · Cited by 198 · see citing works

AlphaFold, Artificial Intelligence (AI), and Allostery

Nussinov, R., Zhang, M., Liu, Y., & Jang, H. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c04346 · Cited by 190 · see citing works

Single-molecule fluorescence spectroscopy maps the folding landscape of a large protein

Pirchi, M., Ziv, G., Riven, I., Cohen, S. S., Zohar, N., Barak, Y., & Haran, G. (2011) · Nature Communications · doi:10.1038/ncomms1504 · Cited by 179 · see citing works

The art of building multifunctional metal-binding agents from basic molecular scaffolds for the potential application in neurodegenerative diseases

Rodríguez-Rodríguez, C., Telpoukhovskaia, M., & Orvig, C. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.008 · Cited by 151 · see citing works

Targeting the Intrinsically Disordered Structural Ensemble of α-Synuclein by Small Molecules as a Potential Therapeutic Strategy for Parkinson’s Disease

Tóth, G., Gardai, S. J., Zago, W., Bertoncini, C. W., Cremades, N., Roy, S. L., Tambe, M. A., Rochet, J.-C., Galvagnion, C., Skibinski, G., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087133 · Cited by 151 · see citing works

Clusterin facilitates in vivo clearance of extracellular misfolded proteins

Wyatt, A. R., Yerbury, J. J., Berghofer, P., Greguric, I., Katsifis, A., Dobson, C. M., & Wilson, M. R. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0684-8 · Cited by 145 · see citing works

A Review on Origami Simulations: From Kinematics, To Mechanics, Toward Multiphysics

Zhu, Y., Schenk, M., & Filipov, E. T. (2022) · Applied Mechanics Reviews · doi:10.1115/1.4055031 · Cited by 137 · see citing works

Biophysical Insights into How Surfaces, Including Lipid Membranes, Modulate Protein Aggregation Related to Neurodegeneration

Burke, K. A., Yates, E. A., & Legleiter, J. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00017 · Cited by 127 · see citing works

HacA-Independent Functions of the ER Stress Sensor IreA Synergize with the Canonical UPR to Influence Virulence Traits in Aspergillus fumigatus

Feng, X., Krishnan, K., Richie, D. L., Aimanianda, V., Hartl, L., Grahl, N., Powers-Fletcher, M. V., Zhang, M., Fuller, K. K., Nierman, W. C., et al. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002330 · Cited by 112 · see citing works

Amino-terminal domain stability mediates apolipoprotein E aggregation into neurotoxic fibrils

Hatters, D. M., Zhong, N., Rutenber, E., & Weisgraber, K. H. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.06.080 · Cited by 105 · see citing works

Effects of Ammonium Bicarbonate on the Electrospray Mass Spectra of Proteins: Evidence for Bubble-Induced Unfolding

Hedges, J. B., Vahidi, S., Yue, X., & Konermann, L. (2013) · Analytical Chemistry · doi:10.1021/ac401020s · Cited by 109 · see citing works

Hot-spot analysis for drug discovery targeting protein-protein interactions

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