Mechanisms of islet amyloidosis toxicity in type 2 diabetes von Abedini, Andisheh, Schmidt, Ann Marie

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Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology von Cao, Ping, Abedini, Andisheh, Raleigh, Daniel P

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Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics von Abedini, Andisheh, Plesner, Annette, Cao, Ping, Ridgway, Zachary, Zhang, Jinghua, Tu, Ling-Hsien, Middleton, Chris T, Chao, Brian, Sartori, Daniel J, Meng, Fanling, Wang, Hui, Wong, Amy G, Zanni, Martin T, Verchere, C Bruce, Raleigh, Daniel P, Schmidt, Ann Marie

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Islet amyloid polypeptide toxicity and membrane interactions von Cao, Ping, Abedini, Andisheh, Wang, Hui, Tu, Ling-Hsien, Zhang, Xiaoxue, Schmidt, Ann Marie, Raleigh, Daniel P.

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The Flavanol (−)-Epigallocatechin 3-Gallate Inhibits Amyloid Formation by Islet Amyloid Polypeptide, Disaggregates Amyloid Fibrils, and Protects Cultured Cells against IAPP-Induced... von Meng, Fanling, Abedini, Andisheh, Plesner, Annette, Verchere, C. Bruce, Raleigh, Daniel P

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Islet amyloid: From fundamental biophysics to mechanisms of cytotoxicity von Cao, Ping, Marek, Peter, Noor, Harris, Patsalo, Vadim, Tu, Ling-Hsien, Wang, Hui, Abedini, Andisheh, Raleigh, Daniel P.

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A role for helical intermediates in amyloid formation by natively unfolded polypeptides? von Abedini, Andisheh, Raleigh, Daniel P

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Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology von Schmidt, Ann Marie, Raleigh, Daniel P., Abedini, Andisheh, Wong, Amy G., Wang, Hui, Tu, Ling-Hsien, Ridgway, Zachary, Noor, Harris, Cao, Ping, Akter, Rehana, Zhang, Xiaoxue

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RAGE Suppresses ABCG1-Mediated Macrophage Cholesterol Efflux in Diabetes von Daffu, Gurdip, Shen, Xiaoping, Senatus, Laura, Thiagarajan, Devi, Abedini, Andisheh, Hurtado Del Pozo, Carmen, Rosario, Rosa, Song, Fei, Friedman, Richard A, Ramasamy, Ravichandran, Schmidt, Ann Marie

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The Role of His-18 in Amyloid Formation by Human Islet Amyloid Polypeptide von Abedini, Andisheh, Raleigh, Daniel P

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Rational design of potent domain antibody inhibitors of amyloid fibril assembly von Ladiwala, Ali Reza A, Bhattacharya, Moumita, Perchiacca, Joseph M, Cao, Ping, Raleigh, Daniel P, Abedini, Andisheh, Schmidt, Ann Marie, Varkey, Jobin, Langen, Ralf, Tessier, Peter M

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Incorporation of Pseudoproline Derivatives Allows the Facile Synthesis of Human IAPP, a Highly Amyloidogenic and Aggregation-Prone Polypeptide von Abedini, Andisheh, Raleigh, Daniel P

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Recovery and purification of highly aggregation-prone disulfide-containing peptides: Application to islet amyloid polypeptide von Abedini, Andisheh, Singh, Gagandeep, Raleigh, Daniel P.

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Amyloid Formation by Pro-Islet Amyloid Polypeptide Processing Intermediates:  Examination of the Role of Protein Heparan Sulfate Interactions and Implications for Islet Amyloid For... von Meng, Fanling, Abedini, Andisheh, Song, Benben, Raleigh, Daniel P.

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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 Amylo... von Meng, Fanling, Abedini, Andisheh, Plesner, Annette, Middleton, Chris T., Potter, Kathryn J., Zanni, Martin T., Verchere, C. Bruce, Raleigh, Daniel P.

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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... von Abedini, Andisheh, Derk, Julia, Schmidt, Ann Marie

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Editorial von Abedini, Andisheh, Khemtemourian, Lucie, Ivanova, Magdalena, Milardi, Danilo, La Rosa, Carmelo

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Editorial von Abedini, Andisheh, Khemtemourian, Lucie, Ivanova, Magdalena, Milardi, Danilo, La Rosa, Carmelo

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A Single-Point Mutation Converts the Highly Amyloidogenic Human Islet Amyloid Polypeptide into a Potent Fibrillization Inhibitor von Abedini, Andisheh, Meng, Fanling, Raleigh, Daniel P

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A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides von Abedini, Andisheh, Raleigh, Daniel P.

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