Andisheh Abedini, Ph.D. - Publications

Affiliations: 
2006 Stony Brook University, Stony Brook, NY, United States 

38 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2020 Ridgway Z, Lee KH, Zhyvoloup A, Wong A, Eldrid C, Hannaberry E, Thalassinos K, Abedini A, Raleigh DP. Analysis of Baboon IAPP Provides Insight into Amyloidogenicity and Cytotoxicity of Human IAPP. Biophysical Journal. PMID 32105649 DOI: 10.1016/J.Bpj.2019.12.027  0.743
2018 Akter R, Bower RL, Abedini A, Schmidt AM, Hay DL, Raleigh DP. Amyloidogenicity, Cytotoxicity and Receptor Activity of Bovine Amylin; Implications for Xenobiotic Transplantation and the Design of Non-toxic Amylin Variants. Acs Chemical Biology. PMID 30086232 DOI: 10.1021/Acschembio.8B00690  0.689
2018 Derk J, Bermudez Hernandez K, Rodriguez M, He M, Koh H, Abedini A, Li H, Fenyö D, Schmidt AM. Diaphanous 1 (DIAPH1) is Highly Expressed in the Aged Human Medial Temporal Cortex and Upregulated in Myeloid Cells During Alzheimer's Disease. Journal of Alzheimer's Disease : Jad. PMID 29966194 DOI: 10.3233/Jad-180088  0.337
2018 Ridgway Z, Zhang X, Wong AG, Abedini A, Schmidt AM, Raleigh DP. Analysis of the role of the conserved disulfide in amyloid formation by human IAPP in homogenous and heterogeneous environments. Biochemistry. PMID 29697253 DOI: 10.1021/Acs.Biochem.8B00017  0.7
2018 Abedini A, Derk J, Schmidt AM. The Receptor for Advanced Glycation Endproducts is a mediator of toxicity by IAPP and other proteotoxic aggregates: Establishing and Exploiting Common Ground for Novel Amyloidosis Therapies. Protein Science : a Publication of the Protein Society. PMID 29664151 DOI: 10.1002/Pro.3425  0.512
2018 Abedini A, Cao P, Plesner A, Zhang J, He M, Derk J, Patil SA, Rosario R, Lonier J, Song F, Koh H, Li H, Raleigh DP, Schmidt AM. RAGE binds preamyloid IAPP intermediates and mediates pancreatic β cell proteotoxicity. The Journal of Clinical Investigation. PMID 29337308 DOI: 10.1172/Jci85210  0.64
2017 Akter R, Abedini A, Ridgway Z, Zhang X, Kleinberg J, Schmidt AM, Raleigh DP. Evolutionary Adaptation and Amyloid Formation: Does the Reduced Amyloidogenicity and Cytotoxicity of Ursine Amylin Contribute to the Metabolic Adaption of Bears and Polar Bears? Israel Journal of Chemistry. 57: 750-761. PMID 29955200 DOI: 10.1002/Ijch.201600081  0.642
2016 Abedini A, Plesner A, Cao P, Ridgway Z, Zhang J, Tu LH, Middleton CT, Chao B, Sartori D, Meng F, Wang H, Wong AG, Zanni MT, Verchere CB, Raleigh DP, et al. Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics. Elife. 5. PMID 27213520 DOI: 10.7554/Elife.12977  0.709
2016 Akter R, Cao P, Noor H, Ridgway Z, Tu LH, Wang H, Wong AG, Zhang X, Abedini A, Schmidt AM, Raleigh DP. Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology. Journal of Diabetes Research. 2016: 2798269. PMID 26649319 DOI: 10.1155/2016/2798269  0.7
2016 Abedini A, Cao P, Raleigh DP. Detection of Helical Intermediates During Amyloid Formation by Intrinsically Disordered Polypeptides and Proteins. Methods in Molecular Biology (Clifton, N.J.). 1345: 55-66. PMID 26453205 DOI: 10.1007/978-1-4939-2978-8_4  0.706
2016 Abedini A, Plesner A, Cao P, Ridgway Z, Zhang J, Tu L, Middleton CT, Chao B, Sartori DJ, Meng F, Wang H, Wong AG, Zanni MT, Verchere CB, Raleigh DP, et al. Author response: Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics Elife. DOI: 10.7554/Elife.12977.045  0.643
2014 Wang H, Abedini A, Ruzsicska B, Raleigh DP. Rationally designed, nontoxic, nonamyloidogenic analogues of human islet amyloid polypeptide with improved solubility. Biochemistry. 53: 5876-84. PMID 25140605 DOI: 10.1021/Bi500592P  0.608
2013 Cao P, Abedini A, Wang H, Tu LH, Zhang X, Schmidt AM, Raleigh DP. Islet amyloid polypeptide toxicity and membrane interactions. Proceedings of the National Academy of Sciences of the United States of America. 110: 19279-84. PMID 24218607 DOI: 10.1073/Pnas.1305517110  0.595
2013 Cao P, Marek P, Noor H, Patsalo V, Tu LH, Wang H, Abedini A, Raleigh DP. Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity. Febs Letters. 587: 1106-18. PMID 23380070 DOI: 10.1016/J.Febslet.2013.01.046  0.819
2013 Abedini A, Schmidt AM. Mechanisms of islet amyloidosis toxicity in type 2 diabetes. Febs Letters. 587: 1119-27. PMID 23337872 DOI: 10.1016/J.Febslet.2013.01.017  0.503
2013 Cao P, Abedini A, Raleigh DP. Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology. Current Opinion in Structural Biology. 23: 82-9. PMID 23266002 DOI: 10.1016/J.Sbi.2012.11.003  0.674
2013 Cao P, Abedini A, Plesner A, Marie Schmidt A, Raleigh D. Toxic Intermediates in Islet Amyloid Formation: Analysis of IAPP Mutants Reveals a Correlation between Lag Time and Toxicity Biophysical Journal. 104: 359a. DOI: 10.1016/J.Bpj.2012.11.1995  0.726
2012 Ladiwala AR, Bhattacharya M, Perchiacca JM, Cao P, Raleigh DP, Abedini A, Schmidt AM, Varkey J, Langen R, Tessier PM. Rational design of potent domain antibody inhibitors of amyloid fibril assembly. Proceedings of the National Academy of Sciences of the United States of America. 109: 19965-70. PMID 23161913 DOI: 10.1073/Pnas.1208797109  0.654
2012 Cao P, Tu LH, Abedini A, Levsh O, Akter R, Patsalo V, Schmidt AM, Raleigh DP. Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20. Journal of Molecular Biology. 421: 282-95. PMID 22206987 DOI: 10.1016/J.Jmb.2011.12.032  0.728
2010 Meng F, Raleigh DP, Abedini A. Combination of kinetically selected inhibitors in trans leads to highly effective inhibition of amyloid formation. Journal of the American Chemical Society. 132: 14340-2. PMID 20873820 DOI: 10.1021/Ja1046186  0.792
2010 Meng F, Abedini A, Plesner A, Verchere CB, Raleigh DP. The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity. Biochemistry. 49: 8127-33. PMID 20707388 DOI: 10.1021/Bi100939A  0.807
2010 Meng F, Abedini A, Plesner A, Middleton CT, Potter KJ, Zanni MT, Verchere CB, Raleigh DP. The sulfated triphenyl methane derivative acid fuchsin is a potent inhibitor of amyloid formation by human islet amyloid polypeptide and protects against the toxic effects of amyloid formation. Journal of Molecular Biology. 400: 555-66. PMID 20452363 DOI: 10.1016/J.Jmb.2010.05.001  0.803
2010 Potter KJ, Abedini A, Marek P, Klimek AM, Butterworth S, Driscoll M, Baker R, Nilsson MR, Warnock GL, Oberholzer J, Bertera S, Trucco M, Korbutt GS, Fraser PE, Raleigh DP, et al. Islet amyloid deposition limits the viability of human islet grafts but not porcine islet grafts. Proceedings of the National Academy of Sciences of the United States of America. 107: 4305-10. PMID 20160085 DOI: 10.1073/Pnas.0909024107  0.787
2010 Cao P, Meng F, Abedini A, Raleigh DP. The ability of rodent islet amyloid polypeptide to inhibit amyloid formation by human islet amyloid polypeptide has important implications for the mechanism of amyloid formation and the design of inhibitors. Biochemistry. 49: 872-81. PMID 20028124 DOI: 10.1021/Bi901751B  0.785
2010 Abedini A, Gupta R, Marek P, Meng F, Raleigh DP, Taskent H, Tracz S. Role of Posttranslational Modifications in Amyloid Formation Protein Misfolding Diseases: Current and Emerging Principles and Therapies. 131-144. DOI: 10.1002/9780470572702.ch7  0.777
2009 Abedini A, Raleigh DP. A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides. Protein Engineering, Design & Selection : Peds. 22: 453-9. PMID 19596696 DOI: 10.1093/Protein/Gzp036  0.709
2009 Abedini A, Raleigh DP. A role for helical intermediates in amyloid formation by natively unfolded polypeptides? Physical Biology. 6: 015005. PMID 19208933 DOI: 10.1088/1478-3975/6/1/015005  0.735
2008 Potter K, Abedini A, Butterworth S, Driscoll M, Marek P, Baker R, Korbutt GS, Fraser PE, Raleigh DP, Verchere CB. SPECIES-SPECIFIC SEQUENCE VARIATION OF PORCINE ISLET AMYLOID POLYPEPTIDE REDUCES ITS AMYLOIDOGENICITY AND MAY CONTRIBUTE TO IMPROVED FUNCTION AND SURVIVAL OF PIG ISLET XENOGRAFTS Clinical & Investigative Medicine. 31: 20. DOI: 10.25011/Cim.V31I4.4823  0.813
2008 Potter K, Abedini A, Baker R, Butterworth S, Driscoll M, Marek P, Korbutt G, Fraser P, Raleigh D, Verchere C. Lack of amyloidogenicity and altered prohormone processing of porcine islet amyloid polypeptide may promote function and survival of pig islet xenografts. Canadian Journal of Diabetes. 32: 365. DOI: 10.1016/S1499-2671(08)24259-0  0.783
2007 Meng F, Abedini A, Song B, Raleigh DP. Amyloid formation by pro-islet amyloid polypeptide processing intermediates: examination of the role of protein heparan sulfate interactions and implications for islet amyloid formation in type 2 diabetes. Biochemistry. 46: 12091-9. PMID 17924651 DOI: 10.1021/Bi7004834  0.808
2007 Abedini A, Meng F, Raleigh DP. A single-point mutation converts the highly amyloidogenic human islet amyloid polypeptide into a potent fibrillization inhibitor. Journal of the American Chemical Society. 129: 11300-1. PMID 17722920 DOI: 10.1021/Ja072157Y  0.801
2007 Marek P, Abedini A, Song B, Kanungo M, Johnson ME, Gupta R, Zaman W, Wong SS, Raleigh DP. Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology. Biochemistry. 46: 3255-61. PMID 17311418 DOI: 10.1021/Bi0621967  0.842
2006 Abedini A, Tracz SM, Cho JH, Raleigh DP. Characterization of the heparin binding site in the N-terminus of human pro-islet amyloid polypeptide: implications for amyloid formation. Biochemistry. 45: 9228-37. PMID 16866369 DOI: 10.1021/Bi0510936  0.813
2006 Abedini A, Singh G, Raleigh DP. Recovery and purification of highly aggregation-prone disulfide-containing peptides: application to islet amyloid polypeptide. Analytical Biochemistry. 351: 181-6. PMID 16406209 DOI: 10.1016/J.Ab.2005.11.029  0.671
2006 Abedini A, Raleigh DP. Destabilization of human IAPP amyloid fibrils by proline mutations outside of the putative amyloidogenic domain: is there a critical amyloidogenic domain in human IAPP? Journal of Molecular Biology. 355: 274-81. PMID 16303136 DOI: 10.1016/J.Jmb.2005.10.052  0.708
2005 Abedini A, Raleigh DP. The role of His-18 in amyloid formation by human islet amyloid polypeptide. Biochemistry. 44: 16284-91. PMID 16331989 DOI: 10.1021/Bi051432V  0.62
2005 Abedini A, Raleigh DP. Incorporation of pseudoproline derivatives allows the facile synthesis of human IAPP, a highly amyloidogenic and aggregation-prone polypeptide. Organic Letters. 7: 693-6. PMID 15704927 DOI: 10.1021/Ol047480+  0.575
2004 Tracz SM, Abedini A, Driscoll M, Raleigh DP. Role of aromatic interactions in amyloid formation by peptides derived from human Amylin. Biochemistry. 43: 15901-8. PMID 15595845 DOI: 10.1021/Bi048812L  0.823
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