BPG is committed to discovery and dissemination of knowledge
Cited by in F6Publishing
For: Milardi D, Gazit E, Radford SE, Xu Y, Gallardo RU, Caflisch A, Westermark GT, Westermark P, Rosa C, Ramamoorthy A. Proteostasis of Islet Amyloid Polypeptide: A Molecular Perspective of Risk Factors and Protective Strategies for Type II Diabetes. Chem Rev 2021;121:1845-93. [PMID: 33427465 DOI: 10.1021/acs.chemrev.0c00981] [Cited by in Crossref: 61] [Cited by in F6Publishing: 66] [Article Influence: 61.0] [Reference Citation Analysis]
Number Citing Articles
1 Reichelderfer VT, Chaparro Sosa AF, Kaar JL, Schwartz DK. Tuning the surface charge of phospholipid bilayers inhibits insulin fibrilization. Colloids and Surfaces B: Biointerfaces 2022;220:112904. [DOI: 10.1016/j.colsurfb.2022.112904] [Reference Citation Analysis]
2 Sbardella D, Tundo GR, Mecchia A, Palumbo C, Atzori MG, Levati L, Boccaccini A, Caccuri AM, Cascio P, Lacal PM, Graziani G, Varano M, Coletta M, Parravano M. A novel and atypical NF-KB pro-inflammatory program regulated by a CamKII-proteasome axis is involved in the early activation of Muller glia by high glucose. Cell Biosci 2022;12:108. [DOI: 10.1186/s13578-022-00839-x] [Reference Citation Analysis]
3 Maity D. Inhibition of Amyloid Protein Aggregation Using Selected Peptidomimetics. ChemMedChem 2022. [DOI: 10.1002/cmdc.202200499] [Reference Citation Analysis]
4 Bortoletto AS, Graham WV, Trout G, Bonito-Oliva A, Kazmi MA, Gong J, Weyburne E, Houser BL, Sakmar TP, Parchem RJ. Human Islet Amyloid Polypeptide (hIAPP) Protofibril-Specific Antibodies for Detection and Treatment of Type 2 Diabetes. Adv Sci (Weinh) 2022;:e2202342. [PMID: 36257905 DOI: 10.1002/advs.202202342] [Reference Citation Analysis]
5 Fortier M, Côté-cyr M, Nguyen V, Babych M, Nguyen PT, Gaudreault R, Bourgault S. Contribution of the 12–17 hydrophobic region of islet amyloid polypeptide in self-assembly and cytotoxicity. Front Mol Biosci 2022;9:1017336. [DOI: 10.3389/fmolb.2022.1017336] [Reference Citation Analysis]
6 Guillemain G, Lacapere J, Khemtemourian L. Targeting hIAPP fibrillation: A new paradigm to prevent β-cell death? Biochimica et Biophysica Acta (BBA) - Biomembranes 2022;1864:184002. [DOI: 10.1016/j.bbamem.2022.184002] [Reference Citation Analysis]
7 Kim H, Lee H, Kim Y, Jang B. Higher risk of cancer and neurodegenerative disease in elderly Koreans with type 2 diabetes.. [DOI: 10.21203/rs.3.rs-2049349/v1] [Reference Citation Analysis]
8 Wang G, Zhu X, Song X, Zhang Q, Qian Z. Melatonin Inhibits hIAPP Oligomerization by Preventing β-Sheet and Hydrogen Bond Formation of the Amyloidogenic Region Revealed by Replica-Exchange Molecular Dynamics Simulation. IJMS 2022;23:10264. [DOI: 10.3390/ijms231810264] [Reference Citation Analysis]
9 Xu Y, Maya-Martinez R, Radford SE. Controlling amyloid formation of intrinsically disordered proteins and peptides: slowing down or speeding up? Essays Biochem 2022:EBC20220046. [PMID: 35975807 DOI: 10.1042/EBC20220046] [Reference Citation Analysis]
10 Cuccioloni M, Cecarini V, Bonfili L, Pettinari R, Tombesi A, Pagliaricci N, Petetta L, Angeletti M, Eleuteri AM. Enhancing the Amyloid-β Anti-Aggregation Properties of Curcumin via Arene-Ruthenium(II) Derivatization. Int J Mol Sci 2022;23:8710. [PMID: 35955845 DOI: 10.3390/ijms23158710] [Reference Citation Analysis]
11 Khan AN, Nabi F, Ajmal MR, Ali SM, Almutairi FM, Alalawy AI, Khan RH. Moxifloxacin Disrupts and Attenuates Aβ42 Fibril and Oligomer Formation: Plausibly Repositioning an Antibiotic as Therapeutic against Alzheimer's Disease. ACS Chem Neurosci 2022. [PMID: 35930676 DOI: 10.1021/acschemneuro.2c00371] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
12 Meleleo D, Gerbino A, Mastrodonato M. Evidence of the different effect of mercury and cadmium on the hIAPP aggregation process. Biophysical Chemistry 2022. [DOI: 10.1016/j.bpc.2022.106880] [Reference Citation Analysis]
13 Laneri F, García-Viñuales S, Lanza V, Licciardello N, Milardi D, Sortino S, Grasso G. Dipyridamole for tracking amyloidogenic proteins aggregation and enhancing polyubiquitination. Arch Biochem Biophys 2022;728:109354. [PMID: 35863477 DOI: 10.1016/j.abb.2022.109354] [Reference Citation Analysis]
14 Matveyenka M, Rizevsky S, Kurouski D. Amyloid aggregates exert cell toxicity causing irreversible damages in the endoplasmic reticulum. Biochim Biophys Acta Mol Basis Dis 2022;1868:166485. [PMID: 35840040 DOI: 10.1016/j.bbadis.2022.166485] [Cited by in Crossref: 3] [Cited by in F6Publishing: 2] [Article Influence: 3.0] [Reference Citation Analysis]
15 Espinosa YR, Barrera Valderrama DI, Carlevaro CM, Llanos EJ. Molecular basis of the anchoring and stabilization of human islet amyloid polypeptide in lipid hydroperoxidized bilayers. Biochim Biophys Acta Gen Subj 2022;1866:130200. [PMID: 35820640 DOI: 10.1016/j.bbagen.2022.130200] [Cited by in Crossref: 1] [Cited by in F6Publishing: 2] [Article Influence: 1.0] [Reference Citation Analysis]
16 Zheng Q, Lee B, Kebede MT, Ivancic VA, Kemeh MM, Brito HL, Spratt DE, Lazo ND. Exchange Broadening Underlies the Enhancement of IDE-Dependent Degradation of Insulin by Anionic Membranes. ACS Omega. [DOI: 10.1021/acsomega.2c02747] [Reference Citation Analysis]
17 Elenbaas BOW, Khemtemourian L, Killian JA, Sinnige T. Membrane-Catalyzed Aggregation of Islet Amyloid Polypeptide Is Dominated by Secondary Nucleation. Biochemistry 2022. [PMID: 35749314 DOI: 10.1021/acs.biochem.2c00184] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
18 Benhamou Goldfajn N, Tang H, Ding F. Substoichiometric Inhibition of Insulin against IAPP Aggregation Is Attenuated by the Incompletely Processed N-Terminus of proIAPP. ACS Chem Neurosci 2022. [PMID: 35704461 DOI: 10.1021/acschemneuro.2c00231] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
19 Sanderson JM. The Association of Lipids with Amyloid Fibrils. Journal of Biological Chemistry 2022. [DOI: 10.1016/j.jbc.2022.102108] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
20 García-Viñuales S, Ilie IM, Santoro AM, Romanucci V, Zarrelli A, Di Fabio G, Caflisch A, Milardi D. Silybins inhibit human IAPP amyloid growth and toxicity through stereospecific interactions. Biochim Biophys Acta Proteins Proteom 2022;1870:140772. [PMID: 35307557 DOI: 10.1016/j.bbapap.2022.140772] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 3.0] [Reference Citation Analysis]
21 Tempra C, Scollo F, Pannuzzo M, Lolicato F, La Rosa C. A unifying framework for amyloid-mediated membrane damage: The lipid-chaperone hypothesis. Biochim Biophys Acta Proteins Proteom 2022;1870:140767. [PMID: 35144022 DOI: 10.1016/j.bbapap.2022.140767] [Cited by in Crossref: 7] [Cited by in F6Publishing: 7] [Article Influence: 7.0] [Reference Citation Analysis]
22 Li Z, Tian J, Cheng Z, Teng W, Zhang W, Bao Y, Wang Y, Song B, Chen Y, Li B. Hypoglycemic bioactivity of anthocyanins: A review on proposed targets and potential signaling pathways. Crit Rev Food Sci Nutr 2022;:1-18. [PMID: 35333674 DOI: 10.1080/10408398.2022.2055526] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
23 Tang H, Sun Y, Ding F. Hydrophobic/Hydrophilic Ratio of Amphiphilic Helix Mimetics Determines the Effects on Islet Amyloid Polypeptide Aggregation. J Chem Inf Model 2022. [PMID: 35311274 DOI: 10.1021/acs.jcim.1c01566] [Cited by in Crossref: 1] [Cited by in F6Publishing: 3] [Article Influence: 1.0] [Reference Citation Analysis]
24 Khemtemourian L, Fatafta H, Davion B, Lecomte S, Castano S, Strodel B. Structural Dissection of the First Events Following Membrane Binding of the Islet Amyloid Polypeptide. Front Mol Biosci 2022;9:849979. [DOI: 10.3389/fmolb.2022.849979] [Reference Citation Analysis]
25 Dharmaraj GL, Arigo FD, Young KA, Martins R, Mancera RL, Bharadwaj P. Novel Amylin Analogues Reduce Amyloid-β Cross-Seeding Aggregation and Neurotoxicity. J Alzheimers Dis 2022. [PMID: 35275530 DOI: 10.3233/JAD-215339] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
26 Zeng X, Liu H, He H. Prediction of Intrinsically Disordered Proteins Using Machine Learning Based on Low Complexity Methods. Algorithms 2022;15:86. [DOI: 10.3390/a15030086] [Reference Citation Analysis]
27 Xu Y, Maya-Martinez R, Guthertz N, Heath GR, Manfield IW, Breeze AL, Sobott F, Foster R, Radford SE. Tuning the rate of aggregation of hIAPP into amyloid using small-molecule modulators of assembly. Nat Commun 2022;13:1040. [PMID: 35210421 DOI: 10.1038/s41467-022-28660-7] [Cited by in Crossref: 7] [Cited by in F6Publishing: 7] [Article Influence: 7.0] [Reference Citation Analysis]
28 Abioye RO, Okagu OD, Udenigwe CC. Disaggregation of Islet Amyloid Polypeptide Fibrils as a Potential Anti-Fibrillation Mechanism of Tetrapeptide TNGQ. Int J Mol Sci 2022;23:1972. [PMID: 35216095 DOI: 10.3390/ijms23041972] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
29 Lima LMTR, Sisnande T. Nutrient-sensing amyloid metastasis. Biofactors 2022. [PMID: 35128738 DOI: 10.1002/biof.1825] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
30 Elenbaas BO, Khemtemourian L, Killian JA, Sinnige T. Membrane-catalyzed aggregation of islet amyloid polypeptide is dominated by secondary nucleation.. [DOI: 10.1101/2022.02.04.479144] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
31 Bhowmick DC, Kudaibergenova Z, Burnett L, Jeremic AM. Molecular Mechanisms of Amylin Turnover, Misfolding and Toxicity in the Pancreas. Molecules 2022;27:1021. [PMID: 35164285 DOI: 10.3390/molecules27031021] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
32 Dang Y, Lai Y, Chen F, Sun Q, Ding C, Zhang W, Xu Z. Activatable NIR-II Fluorescent Nanoprobe for Rapid Detection and Imaging of Methylglyoxal Facilitated by the Local Nonpolar Microenvironment. Anal Chem . [DOI: 10.1021/acs.analchem.1c04076] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
33 Najarzadeh Z, Mohammad-beigi H, Pedersen JN, Christiansen G, Pedersen JS, Nielsen J, Otzen DE. Interaction of membrane vesicles with the Pseudomonas functional amyloid protein FapC facilitates amyloid formation. BBA Advances 2022;2:100055. [DOI: 10.1016/j.bbadva.2022.100055] [Reference Citation Analysis]
34 Abioye RO, Okagu OD, Udenigwe CC. Inhibition of Islet Amyloid Polypeptide Fibrillation by Structurally Diverse Phenolic Compounds and Fibril Disaggregation Potential of Rutin and Quercetin. J Agric Food Chem 2021. [PMID: 34964624 DOI: 10.1021/acs.jafc.1c06918] [Cited by in Crossref: 1] [Cited by in F6Publishing: 5] [Article Influence: 1.0] [Reference Citation Analysis]
35 Ben-Zichri S, Malishev R, Oren O, Bloch DN, Taube R, Papo N, Jelinek R. Bcl-2-Homology-Only Proapoptotic Peptides Modulate β-Amyloid Aggregation and Toxicity. ACS Chem Neurosci 2021;12:4554-63. [PMID: 34806861 DOI: 10.1021/acschemneuro.1c00611] [Reference Citation Analysis]
36 Khemtemourian L, Fatafta H, Davion B, Lecomte S, Castano S, Strodel B. Structural dissection of the first events following membrane binding of the islet amyloid polypeptide.. [DOI: 10.1101/2021.12.14.472560] [Reference Citation Analysis]
37 Zhytniakivska O, Kurutos A, Shchuka M, Vus K, Tarabara U, Trusova V, Gorbenko G. Fӧrster resonance energy transfer between Thioflavin T and unsymmetrical trimethine cyanine dyes on amyloid fibril scaffold. Chemical Physics Letters 2021;785:139127. [DOI: 10.1016/j.cplett.2021.139127] [Cited by in Crossref: 2] [Article Influence: 2.0] [Reference Citation Analysis]
38 Pomier KM, Ahmed R, Melacini G. Interactions of intrinsically disordered proteins with the unconventional chaperone human serum albumin: From mechanisms of amyloid inhibition to therapeutic opportunities. Biophysical Chemistry 2021. [DOI: 10.1016/j.bpc.2021.106743] [Cited by in Crossref: 3] [Cited by in F6Publishing: 4] [Article Influence: 3.0] [Reference Citation Analysis]
39 Tang Y, Zhang D, Gong X, Zheng J. A mechanistic survey of Alzheimer's disease. Biophys Chem 2021;281:106735. [PMID: 34894476 DOI: 10.1016/j.bpc.2021.106735] [Cited by in Crossref: 6] [Cited by in F6Publishing: 6] [Article Influence: 6.0] [Reference Citation Analysis]
40 Vogt AS, Roesti ES, Mohsen MO, Leonchiks A, Vogel M, Bachmann MF. Anti-IAPP Monoclonal Antibody Improves Clinical Symptoms in a Mouse Model of Type 2 Diabetes. Vaccines (Basel) 2021;9:1316. [PMID: 34835247 DOI: 10.3390/vaccines9111316] [Cited by in Crossref: 1] [Cited by in F6Publishing: 2] [Article Influence: 1.0] [Reference Citation Analysis]
41 Prabhu MPT, Sarkar N. Inhibitory effects of carbon quantum dots towards hen egg white lysozyme amyloidogenesis through formation of a stable protein complex. Biophys Chem 2022;280:106714. [PMID: 34749221 DOI: 10.1016/j.bpc.2021.106714] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
42 Joshi V, Sulthana F, Ramadas D. ORAL DELIVERY OF SILVER NANOPARTICLES – A REVIEW. Asian J Pharm Clin Res 2021. [DOI: 10.22159/ajpcr.2021.v14i11.42986] [Reference Citation Analysis]
43 Semenova M, Antipova A, Martirosova E, Zelikina D, Palmina N, Chebotarev S. Essential contributions of food hydrocolloids and phospholipid liposomes to the formation of carriers for controlled delivery of biologically active substances via the gastrointestinal tract. Food Hydrocolloids 2021;120:106890. [DOI: 10.1016/j.foodhyd.2021.106890] [Cited by in Crossref: 6] [Cited by in F6Publishing: 6] [Article Influence: 6.0] [Reference Citation Analysis]
44 Tanaka T, Betkekar VV, Ohmori K, Suzuki K, Shigemori H. Evaluation of Amyloid Polypeptide Aggregation Inhibition and Disaggregation Activity of A-Type Procyanidins. Pharmaceuticals (Basel) 2021;14:1118. [PMID: 34832900 DOI: 10.3390/ph14111118] [Cited by in Crossref: 2] [Cited by in F6Publishing: 3] [Article Influence: 2.0] [Reference Citation Analysis]
45 Lorentzon E, Horvath I, Kumar R, Rodrigues JI, Tamás MJ, Wittung-Stafshede P. Effects of the Toxic Metals Arsenite and Cadmium on α-Synuclein Aggregation In Vitro and in Cells. Int J Mol Sci 2021;22:11455. [PMID: 34768886 DOI: 10.3390/ijms222111455] [Cited by in Crossref: 2] [Cited by in F6Publishing: 4] [Article Influence: 2.0] [Reference Citation Analysis]
46 Yoo YM, Joo SS. Human Islet Amyloid Polypeptide Overexpression in INS-1E Cells Influences Amylin Oligomerization under ER Stress and Oxidative Stress. Int J Mol Sci 2021;22:11341. [PMID: 34768769 DOI: 10.3390/ijms222111341] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
47 Wang Y, Westermark GT. The Amyloid Forming Peptides Islet Amyloid Polypeptide and Amyloid β Interact at the Molecular Level. Int J Mol Sci 2021;22:11153. [PMID: 34681811 DOI: 10.3390/ijms222011153] [Cited by in Crossref: 3] [Cited by in F6Publishing: 5] [Article Influence: 3.0] [Reference Citation Analysis]
48 Lima LMTR, Icart LP. Amyloidogenicity of peptides targeting diabetes and obesity. Colloids Surf B Biointerfaces 2021;209:112157. [PMID: 34715595 DOI: 10.1016/j.colsurfb.2021.112157] [Cited by in Crossref: 1] [Cited by in F6Publishing: 2] [Article Influence: 1.0] [Reference Citation Analysis]
49 Lesma J, Bizet F, Berardet C, Tonali N, Pellegrino S, Taverna M, Khemtemourian L, Soulier JL, van Heijenoort C, Halgand F, Ha-Duong T, Kaffy J, Ongeri S. β-Hairpin Peptide Mimics Decrease Human Islet Amyloid Polypeptide (hIAPP) Aggregation. Front Cell Dev Biol 2021;9:729001. [PMID: 34604227 DOI: 10.3389/fcell.2021.729001] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
50 Kunitomi R, Pradipta AR, Kawabe H, Lobsiger N, Tanaka K, Zako T. Inhibition of amyloid formation of amyloid β (1-42), amylin and insulin by 1,5-diazacyclooctanes, a spermine-acrolein conjugate. Bioorg Med Chem 2021;46:116391. [PMID: 34488020 DOI: 10.1016/j.bmc.2021.116391] [Reference Citation Analysis]
51 Zheng Q, Kebede MT, Lee B, Krasinski CA, Islam S, Wurfl LA, Kemeh MM, Ivancic VA, Jakobsche CE, Spratt DE, Lazo ND. Differential Effects of Polyphenols on Insulin Proteolysis by the Insulin-Degrading Enzyme. Antioxidants (Basel) 2021;10:1342. [PMID: 34572974 DOI: 10.3390/antiox10091342] [Cited by in Crossref: 3] [Cited by in F6Publishing: 4] [Article Influence: 3.0] [Reference Citation Analysis]
52 Willbold D, Strodel B, Schröder GF, Hoyer W, Heise H. Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids. Chem Rev 2021;121:8285-307. [PMID: 34137605 DOI: 10.1021/acs.chemrev.1c00196] [Cited by in Crossref: 31] [Cited by in F6Publishing: 35] [Article Influence: 31.0] [Reference Citation Analysis]
53 Tan Q, Liu H, Duan M, Huo S. Interplay between human islet amyloid polypeptide aggregates and micro-heterogeneous membranes. Biochim Biophys Acta Biomembr 2021;1863:183691. [PMID: 34224702 DOI: 10.1016/j.bbamem.2021.183691] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
54 Xu J, Zheng T, Huang X, Wang Y, Yin G, Du W. Procyanidine resists the fibril formation of human islet amyloid polypeptide. Int J Biol Macromol 2021;183:1067-78. [PMID: 33965498 DOI: 10.1016/j.ijbiomac.2021.05.030] [Cited by in Crossref: 5] [Cited by in F6Publishing: 6] [Article Influence: 5.0] [Reference Citation Analysis]
55 El-Beyrouthy J, Freeman E. Characterizing the Structure and Interactions of Model Lipid Membranes Using Electrophysiology. Membranes (Basel) 2021;11:319. [PMID: 33925756 DOI: 10.3390/membranes11050319] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 3.0] [Reference Citation Analysis]
56 Christensen M, Berglund NA, Schiøtt B. The Effect of Cholesterol on Membrane-Bound Islet Amyloid Polypeptide. Front Mol Biosci 2021;8:657946. [PMID: 33968989 DOI: 10.3389/fmolb.2021.657946] [Cited by in Crossref: 5] [Cited by in F6Publishing: 6] [Article Influence: 5.0] [Reference Citation Analysis]
57 Sciacca MFM, Di Natale G, Milardi D, Pappalardo G. Tau/Aβ chimera peptides: A Thioflavin-T and MALDI-TOF study of Aβ amyloidosis in the presence of Cu(II) or Zn(II) ions and total lipid brain extract (TLBE) vesicles. Chem Phys Lipids 2021;237:105085. [PMID: 33895131 DOI: 10.1016/j.chemphyslip.2021.105085] [Cited by in Crossref: 1] [Cited by in F6Publishing: 2] [Article Influence: 1.0] [Reference Citation Analysis]
58 Khemtemourian L, Antoniciello F, Sahoo BR, Decossas M, Lecomte S, Ramamoorthy A. Investigation of the effects of two major secretory granules components, insulin and zinc, on human-IAPP amyloid aggregation and membrane damage. Chem Phys Lipids 2021;237:105083. [PMID: 33887213 DOI: 10.1016/j.chemphyslip.2021.105083] [Cited by in Crossref: 10] [Cited by in F6Publishing: 11] [Article Influence: 10.0] [Reference Citation Analysis]
59 Sciacca MFM, La Rosa C, Milardi D. Amyloid-Mediated Mechanisms of Membrane Disruption. Biophysica 2021;1:137-56. [DOI: 10.3390/biophysica1020011] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 3.0] [Reference Citation Analysis]
60 Porebska N, Pozniak M, Krzyscik MA, Knapik A, Czyrek A, Kucinska M, Jastrzebski K, Zakrzewska M, Otlewski J, Opalinski L. Dissecting biological activities of fibroblast growth factor receptors by the coiled-coil-mediated oligomerization of FGF1. Int J Biol Macromol 2021;180:470-83. [PMID: 33745974 DOI: 10.1016/j.ijbiomac.2021.03.094] [Cited by in Crossref: 4] [Cited by in F6Publishing: 4] [Article Influence: 4.0] [Reference Citation Analysis]
61 García-Viñuales S, Sciacca MFM, Lanza V, Santoro AM, Grasso G, Tundo GR, Sbardella D, Coletta M, Grasso G, La Rosa C, Milardi D. The interplay between lipid and Aβ amyloid homeostasis in Alzheimer's Disease: risk factors and therapeutic opportunities. Chem Phys Lipids 2021;236:105072. [PMID: 33675779 DOI: 10.1016/j.chemphyslip.2021.105072] [Cited by in Crossref: 6] [Cited by in F6Publishing: 6] [Article Influence: 6.0] [Reference Citation Analysis]
62 Ben-shushan S, Miller Y. Insulin fibrillation control by specific zinc binding sites. Inorg Chem Front 2021;8:5251-5259. [DOI: 10.1039/d1qi01054a] [Cited by in F6Publishing: 1] [Reference Citation Analysis]