Probing ion channel activity of human islet amyloid polypeptide (amylin).
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Ruth Nussinov | Hyunbum Jang | Guanghong Wei | R. Nussinov | Guanghong Wei | Jie Zheng | Jun Zhao | Xiang Yu | Yin Luo | Yin Luo | Jie Zheng | Xiang Yu | Jun Zhao | Hyunbum Jang
[1] Laxmikant V. Kale,et al. NAMD2: Greater Scalability for Parallel Molecular Dynamics , 1999 .
[2] Norbert Opitz,et al. Interaction of hIAPP with Model Raft Membranes and Pancreatic β‐Cells: Cytotoxicity of hIAPP Oligomers , 2010, Chembiochem : a European journal of chemical biology.
[3] A. Ramamoorthy,et al. Conformational studies of human islet amyloid peptide using molecular dynamics and simulated annealing methods. , 1998, Biopolymers.
[4] Maarten F. M. Engel,et al. Recent Insights in Islet Amyloid Polypeptide-Induced Membrane Disruption and Its Role in β-Cell Death in Type 2 Diabetes Mellitus , 2008, Experimental diabetes research.
[5] J. Jhamandas,et al. β-Amyloid protein (Aβ) and human amylin regulation of apoptotic genes occurs through the amylin receptor , 2011, Apoptosis.
[6] R. Nussinov,et al. Misfolded amyloid ion channels present mobile beta-sheet subunits in contrast to conventional ion channels. , 2009, Biophysical journal.
[7] Ayyalusamy Ramamoorthy,et al. Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment. , 2011, Biochimica et biophysica acta.
[8] Richard Leapman,et al. Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR. , 2007, Biochemistry.
[9] D. Harries,et al. Structure and fluctuations of charged phosphatidylserine bilayers in the absence of salt. , 2004, Biophysical journal.
[10] J. Brender,et al. Amyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptide. , 2008, Journal of the American Chemical Society.
[11] Ayyalusamy Ramamoorthy,et al. Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective. , 2012, Accounts of chemical research.
[12] KumarShankar,et al. The weighted histogram analysis method for free-energy calculations on biomolecules. I , 1992 .
[13] P. Westermark,et al. Islet amyloid polypeptide inhibits glucagon release and exerts a dual action on insulin release from isolated islets , 2003, Regulatory Peptides.
[14] L. Sarkisov,et al. Interactions of phospholipid bilayers with several classes of amphiphilic alpha-helical peptides: insights from coarse-grained molecular dynamics simulations. , 2010, The journal of physical chemistry. B.
[15] P. Argos,et al. Knowledge‐based protein secondary structure assignment , 1995, Proteins.
[16] R. Swendsen,et al. THE weighted histogram analysis method for free‐energy calculations on biomolecules. I. The method , 1992 .
[17] Jie Zheng,et al. Molecular dynamics simulations of low-ordered alzheimer β-amyloid oligomers from dimer to hexamer on self-assembled monolayers. , 2011, Langmuir : the ACS journal of surfaces and colloids.
[18] D. Eisenberg,et al. Toxic fibrillar oligomers of amyloid-β have cross-β structure , 2012, Proceedings of the National Academy of Sciences.
[19] C. Mukhopadhyay,et al. Cause and effect of melittin-induced pore formation: a computational approach. , 2009, Langmuir : the ACS journal of surfaces and colloids.
[20] M. Kawahara,et al. Molecular mechanism of neurodegeneration induced by Alzheimer’s β-amyloid protein: channel formation and disruption of calcium homeostasis , 2000, Brain Research Bulletin.
[21] E. Goormaghtigh,et al. Transformation of amyloid β(1–40) oligomers into fibrils is characterized by a major change in secondary structure , 2011, Cellular and Molecular Life Sciences.
[22] G. Veglia,et al. Conformational preferences of the amylin nucleation site in SDS micelles: An NMR study , 2003, Biopolymers.
[23] Guizhao Liang,et al. Structural polymorphism of human islet amyloid polypeptide (hIAPP) oligomers highlights the importance of interfacial residue interactions. , 2011, Biomacromolecules.
[24] Ian Parker,et al. Calcium Dysregulation and Membrane Disruption as a Ubiquitous Neurotoxic Mechanism of Soluble Amyloid Oligomers*♦ , 2005, Journal of Biological Chemistry.
[25] W. Im,et al. Automated Builder and Database of Protein/Membrane Complexes for Molecular Dynamics Simulations , 2007, PloS one.
[26] H. Guy,et al. Beta‐barrel models of soluble amyloid beta oligomers and annular protofibrils , 2010, Proteins.
[27] B. Wallace,et al. The pore dimensions of gramicidin A. , 1993, Biophysical journal.
[28] K Schulten,et al. VMD: visual molecular dynamics. , 1996, Journal of molecular graphics.
[29] B. Kagan,et al. Pore Formation by the Cytotoxic Islet Amyloid Peptide Amylin (*) , 1996, The Journal of Biological Chemistry.
[30] Bert L. de Groot,et al. g_wham—A Free Weighted Histogram Analysis Implementation Including Robust Error and Autocorrelation Estimates , 2010 .
[31] P. Butler,et al. Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis. , 2008, Endocrine reviews.
[32] Guanghong Wei,et al. Interactions of Aβ25-35 β-barrel-like oligomers with anionic lipid bilayer and resulting membrane leakage: an all-atom molecular dynamics study. , 2011, The journal of physical chemistry. B.
[33] M. Horowitz,et al. Amylin , 2006 .
[34] Alexander D. MacKerell,et al. All-atom empirical potential for molecular modeling and dynamics studies of proteins. , 1998, The journal of physical chemistry. B.
[35] R. Nussinov,et al. New structures help the modeling of toxic amyloidbeta ion channels. , 2008, Trends in biochemical sciences.
[36] B. Kagan,et al. Pore formation by beta-2-microglobulin: A mechanism for the pathogenesis of dialysis associated amyloidosis , 2001, Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis.
[37] R. Nussinov,et al. Models of toxic beta-sheet channels of protegrin-1 suggest a common subunit organization motif shared with toxic alzheimer beta-amyloid ion channels. , 2008, Biophysical journal.
[38] Jie Zheng,et al. Cholesterol promotes the interaction of Alzheimer β-amyloid monomer with lipid bilayer. , 2012, Journal of molecular biology.
[39] A. Geliebter,et al. Amylin, food intake, and obesity. , 2002, Obesity research.
[40] Patrick M. Sexton,et al. International Union of Pharmacology. XXXII. The Mammalian Calcitonin Gene-Related Peptides, Adrenomedullin, Amylin, and Calcitonin Receptors , 2002, Pharmacological Reviews.
[41] Sara M. Butterfield,et al. Amyloidogenic Protein—Membrane Interactions: Mechanistic Insight from Model Systems , 2010 .
[42] M Morfis,et al. Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product. , 1999, Molecular pharmacology.
[43] F. Reimann,et al. Calcium elevation in mouse pancreatic beta cells evoked by extracellular human islet amyloid polypeptide involves activation of the mechanosensitive ion channel TRPV4 , 2008, Diabetologia.
[44] Ruth Nussinov,et al. Models of beta-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process. , 2007, Biophysical journal.
[45] H. Scheidt,et al. Solid-state NMR spectroscopic investigation of Aβ protofibrils: implication of a β-sheet remodeling upon maturation into terminal amyloid fibrils. , 2011, Angewandte Chemie.
[46] A. Miranker,et al. Conserved and cooperative assembly of membrane-bound alpha-helical states of islet amyloid polypeptide. , 2006, Biochemistry.
[47] P. Lansbury,et al. Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? , 2006, Quarterly Reviews of Biophysics.
[48] K. Matsuzaki,et al. Ganglioside‐induced amyloid formation by human islet amyloid polypeptide in lipid rafts , 2009, FEBS letters.
[49] E. Rojas,et al. Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein [A beta P-(1-40)] in bilayer membranes. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[50] Ruth Nussinov,et al. Truncated β-amyloid peptide channels provide an alternative mechanism for Alzheimer’s Disease and Down syndrome , 2010, Proceedings of the National Academy of Sciences.
[51] Guizhao Liang,et al. Heterogeneous triangular structures of human islet amyloid polypeptide (amylin) with internal hydrophobic cavity and external wrapping morphology reveal the polymorphic nature of amyloid fibrils. , 2011, Biomacromolecules.
[52] R. Nussinov,et al. K3 fragment of amyloidogenic beta(2)-microglobulin forms ion channels: implication for dialysis related amyloidosis. , 2009, Journal of the American Chemical Society.
[53] C. Betsholtz,et al. Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[54] Hai Lin,et al. Amyloid ion channels: a common structural link for protein-misfolding disease. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[55] A. Miranker,et al. Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity , 2011, Proceedings of the National Academy of Sciences.
[56] R. Seidel,et al. Amyloidogenic propensities and conformational properties of ProIAPP and IAPP in the presence of lipid bilayer membranes. , 2009, Journal of molecular biology.
[57] A. Alexandrescu,et al. Dynamic α-Helix Structure of Micelle-bound Human Amylin* , 2009, Journal of Biological Chemistry.
[58] Y. Ishii,et al. Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid , 2007, Nature Structural &Molecular Biology.
[59] R. Nussinov,et al. Structural Convergence Among Diverse, Toxic β-Sheet Ion Channels , 2010, The journal of physical chemistry. B.
[60] R. Lal,et al. Amyloid β protein forms ion channels: implications for Alzheimer's disease pathophysiology , 2001, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[61] A. Miranker,et al. The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: insights from type II diabetes. , 2009, Annual review of biophysics.
[62] J. Brender,et al. Induction of negative curvature as a mechanism of cell toxicity by amyloidogenic peptides: the case of islet amyloid polypeptide. , 2009, Journal of the American Chemical Society.
[63] J. Brender,et al. Membrane fragmentation by an amyloidogenic fragment of human Islet Amyloid Polypeptide detected by solid-state NMR spectroscopy of membrane nanotubes. , 2007, Biochimica et biophysica acta.