A. Abedini

发表

Amyloidogenicity, Cytotoxicity, and Receptor Activity of Bovine Amylin: Implications for Xenobiotic Transplantation and the Design of Nontoxic Amylin Variants.

D. Raleigh, A. Schmidt, Rebekah L. Bower, 2018, ACS chemical biology.

RAGE Suppresses ABCG1-Mediated Macrophage Cholesterol Efflux in Diabetes

R. Friedman, R. Ramasamy, A. Schmidt, 2015, Diabetes.

Inflammation and obesity: STAMPing out insulin resistance?

S. Shoelson, A. Abedini, 2007, Immunology and cell biology.

Diaphanous 1 (DIAPH1) is Highly Expressed in the Aged Human Medial Temporal Cortex and Upregulated in Myeloid Cells During Alzheimer's Disease.

D. Fenyö, A. Schmidt, Hyunwook Koh, 2018, Journal of Alzheimer's disease : JAD.

Islet Amyloid Polypeptide

D. Raleigh, A. Abedini, 2010 .

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.

D. Raleigh, M. Zanni, C. Verchere, 2010, Journal of molecular biology.

Detection of Helical Intermediates During Amyloid Formation by Intrinsically Disordered Polypeptides and Proteins.

D. Raleigh, P. Cao, A. Abedini, 2016, Methods in molecular biology.

Analysis of the role of the conserved disulfide in amyloid formation by human IAPP in homogenous and heterogeneous environments

D. Raleigh, Zachary M. Ridgway, Schmidt, 2018 .

Characterization of the heparin binding site in the N-terminus of human pro-islet amyloid polypeptide: implications for amyloid formation.

D. Raleigh, Jae-Hyun Cho, Sylvia M Tracz, 2006, Biochemistry.

The role of His-18 in amyloid formation by human islet amyloid polypeptide.

D. Raleigh, A. Abedini, 2005, Biochemistry.

A role for helical intermediates in amyloid formation by natively unfolded polypeptides?

D. Raleigh, Daniel P Raleigh, Andisheh Abedini, 2009, Physical biology.

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.

D. Raleigh, B. Song, Fanling Meng, 2007, Biochemistry.

Islet amyloid polypeptide toxicity and membrane interactions

D. Raleigh, P. Cao, A. Schmidt, 2013, Proceedings of the National Academy of Sciences.

Mechanisms of islet amyloidosis toxicity in type 2 diabetes

A. Schmidt, A. Abedini, 2013, FEBS letters.

Destabilization of human IAPP amyloid fibrils by proline mutations outside of the putative amyloidogenic domain: is there a critical amyloidogenic domain in human IAPP?

D. Raleigh, A. Abedini, 2006, Journal of molecular biology.

Recovery and purification of highly aggregation-prone disulfide-containing peptides: application to islet amyloid polypeptide.

D. Raleigh, Gagandeep Singh, A. Abedini, 2006, Analytical biochemistry.

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

A. Schmidt, A. Abedini, J. Derk, 2018, Protein science : a publication of the Protein Society.

Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology

D. Raleigh, P. Cao, A. Schmidt, 2015, Journal of diabetes research.

Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology.

D. Raleigh, P. Cao, Daniel P Raleigh, 2013, Current opinion in structural biology.

A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides.

D. Raleigh, A. Abedini, 2009, Protein engineering, design & selection : PEDS.

A single-point mutation converts the highly amyloidogenic human islet amyloid polypeptide into a potent fibrillization inhibitor.

Fanling Meng, D. Raleigh, Daniel P Raleigh, 2007, Journal of the American Chemical Society.

Islet amyloid: From fundamental biophysics to mechanisms of cytotoxicity

Peter Marek, D. Raleigh, P. Marek, 2012, FEBS letters.

RAGE binds preamyloid IAPP intermediates and mediates pancreatic &bgr; cell proteotoxicity

D. Raleigh, P. Cao, A. Schmidt, 2018, The Journal of clinical investigation.

Analysis of Baboon IAPP Provides Insight into Amyloidogenicity and Cytotoxicity of Human IAPP.

D. Raleigh, K. Thalassinos, Zachary M. Ridgway, 2020, Biophysical journal.

Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology.

Stanislaus S. Wong, D. Raleigh, P. Marek, 2007, Biochemistry.

Islet amyloid deposition limits the viability of human islet grafts but not porcine islet grafts

D. Raleigh, P. Fraser, M. R. Nilsson, 2010, Proceedings of the National Academy of Sciences.

Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics

D. Raleigh, P. Cao, M. Zanni, 2016, eLife.

Incorporation of pseudoproline derivatives allows the facile synthesis of human IAPP, a highly amyloidogenic and aggregation-prone polypeptide.

D. Raleigh, A. Abedini, 2005, Organic letters.

Rationally Designed, Nontoxic, Nonamyloidogenic Analogues of Human Islet Amyloid Polypeptide with Improved Solubility

D. Raleigh, B. Ruzsicska, A. Abedini, 2014, Biochemistry.

Rational design of potent domain antibody inhibitors of amyloid fibril assembly

D. Raleigh, P. Cao, A. Schmidt, 2012, Proceedings of the National Academy of Sciences.

The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity.

Fanling Meng, D. Raleigh, C. Verchere, 2010, Biochemistry.

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.

Fanling Meng, D. Raleigh, P. Cao, 2010, Biochemistry.

Role of aromatic interactions in amyloid formation by peptides derived from human Amylin.

D. Raleigh, Miles Driscoll, Daniel P Raleigh, 2004, Biochemistry.

Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20.

Ann Marie Schmidt, Olesya Levsh, D. Raleigh, 2012, Journal of molecular biology.

Role of Posttranslational Modifications in Amyloid Formation

D. Raleigh, P. Marek, Sylvia M Tracz, 2010 .

Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology

D. Raleigh, P. Cao, A. Schmidt, 2015, Journal of diabetes research.

Evolutionary Adaptation and Amyloid Formation: Does the Reduced Amyloidogenicity and Cytotoxicity of Ursine Amylin Contribute to the Metabolic Adaption of Bears and Polar Bears?

D. Raleigh, A. Schmidt, Zachary M. Ridgway, 2017, Israel journal of chemistry.

Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20.

D. Raleigh, P. Cao, Vadim Patsalo, 2012, Journal of molecular biology.

Analysis of the Role of the Conserved Disulfide in Amyloid Formation by Human Islet Amyloid Polypeptide in Homogeneous and Heterogeneous Environments.

D. Raleigh, A. Schmidt, Zachary M. Ridgway, 2018, Biochemistry.

Amyloidogenicity, Cytotoxicity, and Receptor Activity of Bovine Amylin: Implications for Xenobiotic Transplantation and the Design of Nontoxic Amylin Variants.

D. Raleigh, A. Schmidt, Rebekah L. Bower, 2018, ACS chemical biology.

Combination of kinetically selected inhibitors in trans leads to highly effective inhibition of amyloid formation.

Fanling Meng, D. Raleigh, Daniel P Raleigh, 2010, Journal of the American Chemical Society.