A capillary zone electrophoresis method to investigate the oligomerization of the human Islet Amyloid Polypeptide involved in Type 2 Diabetes

Global aetiology and epidemiology of type 2 diabetes mellitus and its complications

Zheng, Y., Ley, S. H., & Hu, F. B. (2018) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2017.151 · Cited by 5,697 · see citing works

Global estimates of diabetes prevalence for 2013 and projections for 2035

Guariguata, L., Whiting, D. R., Hambleton, I., Beagley, J., Linnenkamp, U., & Shaw, J. E. (2014) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2013.11.002 · Cited by 4,642 · see citing works

Molecular mechanism of Thioflavin-T binding to amyloid fibrils

Biancalana, M., & Koide, S. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.04.001 · Cited by 2,203 · see citing works

Clinical review of antidiabetic drugs: implications for type 2 diabetes mellitus management

Chaudhury, A., Duvoor, C., Reddy Dendi, V. S., Kraleti, S., Chada, A., Ravilla, R., Marco, A., Shekhawat, N. S., Montales, M. T., Kuriakose, K., et al. (2017) · Frontiers in Endocrinology · doi:10.3389/fendo.2017.00006 · Cited by 1,500 · see citing works

Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus

Westermark, P., Andersson, A., & Westermark, G. T. (2011) · Physiological Reviews · doi:10.1152/physrev.00042.2009 · Cited by 1,044 · see citing works

Mechanism of thioflavin T binding to amyloid fibrils

Khurana, R., Coleman, C., Ionescu‐Zanetti, C., Carter, S. A., Krishna, V., Grover, R. K., Roy, R., & Singh, S. S. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.06.006 · Cited by 833 · see citing works

Islet Amyloid in Type 2 Diabetes, and the Toxic Oligomer Hypothesis

Haataja, L., Gurlo, T., Huang, C. J., & Butler, P. C. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0037 · Cited by 612 · see citing works

Type 2 diabetes as a protein misfolding disease

Mukherjee, A., Morales‐Scheihing, D., Butler, P. C., & Soto, C. A. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2015.04.005 · Cited by 338 · see citing works

Screening and classifying small-molecule inhibitors of amyloid formation using ion mobility spectrometry–mass spectrometry

Young, L. M., Saunders, J. C., Mahood, R. A., Revill, C., Foster, R. J., Tu, L., Raleigh, D. P., Radford, S. E., & Ashcroft, A. E. (2014) · Nature Chemistry · doi:10.1038/nchem.2129 · Cited by 281 · see citing works

Islet amyloid polypeptide: structure, function, and pathophysiology

Akter, R., Cao, P., Noor, H., Ridgway, Z., Tu, L.-H., Wang, H., Wong, A. G., Zhang, X., Abedini, A., Schmidt, A. M., et al. (2016) · Journal of Diabetes Research · doi:10.1155/2016/2798269 · Cited by 273 · see citing works

Resveratrol, A Neuroprotective Supplement for Alzheimer's Disease

Li, F., Gong, Q., Dong, H., & Shi, J. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212798919075 · Cited by 231 · see citing works

Chapter 20 Protein Precipitation Techniques

Burgess, R. R. (2009) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(09)63020-2 · Cited by 223 · see citing works

Mechanisms of islet amyloidosis toxicity in type 2 diabetes

Abedini, A., & Schmidt, A. M. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.017 · Cited by 201 · see citing works

Ion Mobility Spectrometry–Mass Spectrometry Defines the Oligomeric Intermediates in Amylin Amyloid Formation and the Mode of Action of Inhibitors

Young, L. M., Cao, P., Raleigh, D. P., Ashcroft, A. E., & Radford, S. E. (2013) · Journal of the American Chemical Society · doi:10.1021/ja406831n · Cited by 190 · see citing works

Glucagon-like peptide-1 analogues: An overview

Gupta, V. (2013) · Indian Journal of Endocrinology and Metabolism · doi:10.4103/2230-8210.111625 · Cited by 186 · see citing works

Insulin therapy for type 2 diabetes.

Swinnen, S. G., Hoekstra, J. B., & DeVries, J. H. (2009) · Diabetes Care · doi:10.2337/dc09-s318 · Cited by 181 · see citing works

Ionic Strength Effects on Amyloid Formation by Amylin Are a Complicated Interplay among Debye Screening, Ion Selectivity, and Hofmeister Effects

Marek, P., Patsalo, V., Green, D. F., & Raleigh, D. P. (2012) · Biochemistry · doi:10.1021/bi300574r · Cited by 168 · see citing works

Performance of a physically adsorbed high-molecular-mass polyethyleneimine layer as coating for the separation of basic proteins and peptides by capillary electrophoresis

Erim, F. B., Cifuentes, A., Poppe, H., et al. (1995) · Journal of Chromatography A · doi:10.1016/0021-9673(95)00394-3 · Cited by 158 · see citing works

Structural Characterisation of Islet Amyloid Polypeptide Fibrils

Makin, O. S., & Serpell, L. C. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.11.048 · Cited by 147 · see citing works

Inhibition of IAPP Aggregation and Toxicity by Natural Products and Derivatives

Pithadia, A. S., Brender, J., Fierke, C. A., & Ramamoorthy, A. (2015) · Journal of Diabetes Research · doi:10.1155/2016/2046327 · Cited by 142 · see citing works

Two decades of studying non-covalent biomolecular assemblies by means of electrospray ionization mass spectrometry

Hilton, G. R., & Benesch, J. L. P. (2012) · Journal of The Royal Society Interface · doi:10.1098/rsif.2011.0823 · Cited by 140 · see citing works

Fibril Structure of Human Islet Amyloid Polypeptide*♦

Bedrood, S., Li, Y.-Y., Isas, J., Hegde, B. G., Baxa, U., Haworth, I., & Langen, R. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.327817 · Cited by 136 · see citing works

The β-cell assassin: IAPP cytotoxicity

Raleigh, D. P., Zhang, X., Hastoy, B., & Clark, A. (2017) · Journal of Molecular Endocrinology · doi:10.1530/jme-17-0105 · Cited by 135 · see citing works

Efficacy, safety and regulatory status of SGLT2 inhibitors: focus on canagliflozin

Haas, B., Eckstein, N., Pfeifer, V., Mayer, P. E., & Hass, M. D. S. (2014) · Nutrition and Diabetes · doi:10.1038/nutd.2014.40 · Cited by 114 · see citing works

pH Dependence of Amylin Fibrillization

Jha, S., Snell, J. M., Sheftic, S. R., Patil, S. M., Daniels, S. B., Kolling, F. W., & Alexandrescu, A. T. (2013) · Biochemistry · doi:10.1021/bi401164k · Cited by 112 · see citing works

The Molecular Basis of Distinct Aggregation Pathways of Islet Amyloid Polypeptide*

Wei, L., Jiang, P., Xu, W., Li, H., Zhang, H., Yan, L., Chan-Park, M., Liu, X.-W., Tang, K., Mu, Y., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.166678 · Cited by 105 · see citing works

Amylin Uncovered: A Review on the Polypeptide Responsible for Type II Diabetes

Pillay, K., & Govender, P. (2013) · BioMed Research International · doi:10.1155/2013/826706 · Cited by 94 · see citing works

Apoptosis induced by islet amyloid polypeptide soluble oligomers is neutralized by diabetes-associated specific antibodies

Bram, Y., Frydman‐Marom, A., Yanai, I., Gilead, S., Shaltiel‐Karyo, R., Amdursky, N., & Gazit, E. (2014) · Scientific Reports · doi:10.1038/srep04267 · Cited by 89 · see citing works

Low pH acts as inhibitor of membrane damage induced by human islet amyloid polypeptide.

Khemtemourian, L., Doménech, E., Doux, J. P. F., Koorengevel, M., & Killian, J. (2011) · Journal of the American Chemical Society · doi:10.1021/ja205007j · Cited by 83 · see citing works

Defining the Molecular Basis of Amyloid Inhibitors: Human Islet Amyloid Polypeptide–Insulin Interactions

Susa, A. C., Wu, C. F., Bernstein, S. L., Dupuis, N., Wang, H., Raleigh, D. P., Shea, J., & Bowers, M. T. (2014) · Journal of the American Chemical Society · doi:10.1021/ja504031d · Cited by 76 · see citing works

Capillary electrophoresis studies on the aggregation process of β‐amyloid 1‐42 and 1‐40 peptides

Sabella, S., Quaglia, M., Lanni, C., Racchi, M., Govoni, S. M., Caccialanza, G., Calligaro, A., Bellotti, V., & Lorenzi, E. D. (2004) · Electrophoresis · doi:10.1002/elps.200406062 · Cited by 73 · see citing works

Thioflavin T fluorescence to analyse amyloid formation kinetics: Measurement frequency as a factor explaining irreproducibility

Sebastiao, M., Quittot, N., & Bourgault, S. (2017) · Analytical Biochemistry · doi:10.1016/j.ab.2017.06.007 · Cited by 72 · see citing works

ESI-IMS–MS: A method for rapid analysis of protein aggregation and its inhibition by small molecules

Young, L. M., Saunders, J. C., Mahood, R. A., Revill, C., Foster, R. J., Ashcroft, A. E., & Radford, S. E. (2015) · Methods · doi:10.1016/j.ymeth.2015.05.017 · Cited by 66 · see citing works

Mutational Analysis of the Ability of Resveratrol To Inhibit Amyloid Formation by Islet Amyloid Polypeptide: Critical Evaluation of the Importance of Aromatic–Inhibitor and Histidine–Inhibitor Interactions

Tu, L., Young, L. M., Wong, A. G., Ashcroft, A. E., Radford, S. E., & Raleigh, D. P. (2014) · Biochemistry · doi:10.1021/bi501016r · Cited by 61 · see citing works

How Type II Diabetes-Related Islet Amyloid Polypeptide Damages Lipid Bilayers

Lee, C., Sun, Y., & Huang, H. W. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.01.039 · Cited by 61 · see citing works

Capillary electrophoresis of intact basic proteins using noncovalently triple‐layer coated capillaries

Haselberg, R., de Jong, G. J., & Somsen, G. W. (2009) · Journal of Separation Science · doi:10.1002/jssc.200900164 · Cited by 56 · see citing works

A foldamer approach to targeting membrane bound helical states of islet amyloid polypeptide

Kumar, S., & Miranker, A. D. (2013) · Chemical Communications · doi:10.1039/c3cc41452c · Cited by 52 · see citing works

Comparing the structural properties of human and rat islet amyloid polypeptide by MD computer simulations

Andrews, M. N., & Winter, R. (2011) · Biophysical Chemistry · doi:10.1016/j.bpc.2010.12.007 · Cited by 50 · see citing works

Direct measurement of islet amyloid polypeptide fibrillogenesis by mass spectrometry

Larson, J. L., Ko, E. C., & Miranker, A. D. (2000) · Protein Science · doi:10.1110/ps.9.2.427 · Cited by 49 · see citing works

Capillary electrophoresis of peptides and proteins at neutral pH in capillaries covalently coated with polyethyleneimine

Figeys, D., & Aebersold, R. (1997) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/s0378-4347(97)00022-4 · Cited by 42 · see citing works

Amphiphilic oligoamide α-helix peptidomimetics inhibit islet amyloid polypeptide aggregation

Kulikov, O. V., Kumar, S., Magzoub, M. M., et al. (2015) · Tetrahedron Letters · doi:10.1016/j.tetlet.2015.02.132 · Cited by 40 · see citing works

Folded Small Molecule Manipulation of Islet Amyloid Polypeptide

Kumar, S., Brown, M. A., Nath, A., & Miranker, A. D. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.05.007 · Cited by 34 · see citing works

An improved capillary electrophoresis method for in vitro monitoring of the challenging early steps of Aβ1–42 peptide oligomerization: Application to anti‐Alzheimer's drug discovery

Brinet, D., Kaffy, J., Oukacine, F., Glumm, S., Ongeri, S., & Taverna, M. (2014) · Electrophoresis · doi:10.1002/elps.201400271 · Cited by 30 · see citing works

Stepwise oligomerization of murine amylin and assembly of amyloid fibrils.

Palmieri, L., Melo-Ferreira, B., Braga, C., Fontes, G. N., Mattos, L., & Lima, L. M. T. R. (2013) · Biophysical Chemistry · doi:10.1016/j.bpc.2013.07.013 · Cited by 23 · see citing works

Influence of trehalose on human islet amyloid polypeptide fibrillation and aggregation

Chen, C., Yao, T. S., Zhang, Q., He, Y., Xu, L., Zheng, M., Zhou, G., Zhang, Y., Yang, H., & Zhou, P. (2016) · RSC Advances · doi:10.1039/c5ra27689f · Cited by 23 · see citing works

On the structure of the copper–amylin complex

Riba‐Garcia, I., Barran, P. E., Cooper, G. J. S., & Unwin, R. D. (2015) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2015.09.001 · Cited by 18 · see citing works

Field amplified sample stacking of amyloid beta (1-42) oligomers using capillary electrophoresis

Paracha, S., & Hestekin, C. N. (2016) · Biomicrofluidics · doi:10.1063/1.4954051 · Cited by 12 · see citing works

Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research

Gomes, F. P., & Yates, J. R. (2019) · Mass Spectrometry Reviews · doi:10.1002/mas.21599 · Cited by 112 · see citing works

ESR detection of non-equivalent scandium trimer

Suzuki, S., Kojima, Y., Nakao, Y., et al. (1994) · Chemical Physics Letters · doi:10.1016/0009-2614(94)01080-3 · Cited by 15 · see citing works

Synthesis of chemically-tethered amyloid-β segment trimer possessing amyloidogenic properties.

Shinoda, K., Sohma, Y., & Kanai, M. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2015.05.029 · Cited by 14 · see citing works

Oligomer of Indolizine Derivative and Its pH Sensitive Behavior

Nishiwaki, N., Furuta, K., Komatsu, M., et al. (1991) · Polymer Journal · doi:10.1295/polymj.23.789 · Cited by 3 · see citing works

Structure–activity relationships in well-defined conjugated oligomer photocatalysts for hydrogen production from water

Aitchison, C. M., Sachs, M., Little, M. A., Wilbraham, L., Brownbill, N. J., Kane, C. M., Blanc, F., Zwijnenburg, M. A., Durrant, J. R., Sprick, R. S., et al. (2020) · Chemical Science · doi:10.1039/d0sc02675a · Cited by 59 · see citing works

Microbial Degradation of Styrene Oligomer

Tsuchii, A., Suzuki, T., & Takahara, Y. (1977) · Agricultural and Biological Chemistry · doi:10.1080/00021369.1977.10862874 · Cited by 25 · see citing works