Search Results - "Raleigh, Daniel P"

General amyloid inhibitors? A critical examination of the inhibition of IAPP amyloid formation by inositol stereoisomers by Wang, Hui, Raleigh, Daniel P

“…Islet amyloid polypeptide (IAPP or amylin) forms amyloid deposits in the islets of Langerhans; a process that is believed to contribute to the progression of…”
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Analysis of the Inhibition and Remodeling of Islet Amyloid Polypeptide Amyloid Fibers by Flavanols by Cao, Ping, Raleigh, Daniel P

“…Islet amyloid polypeptide (IAPP, amylin) is responsible for amyloid formation in type 2 diabetes and in transplanted islets. The flavanol…”
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Linking Gas-Phase and Solution-Phase Protein Unfolding via Mobile Proton Simulations by Eldrid, Charles, Cragnolini, Tristan, Ben-Younis, Aisha, Zou, Junjie, Raleigh, Daniel P., Thalassinos, Konstantinos

“…Native mass spectrometry coupled to ion mobility (IM-MS) combined with collisional activation (CA) of ions in the gas phase (in vacuo) is an important method…”
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On the plasticity of amyloid formation: The impact of destabilizing small to large substitutions on islet amyloid polypeptide amyloid formation by Manathunga, Lakshan, Akter, Rehana, Zhyvoloup, Alexander, Simmerling, Carlos, Raleigh, Daniel P.

“…Amyloids are partially ordered, proteinaceous, β‐sheet rich deposits that have been implicated in a wide range of diseases. An even larger set of proteins that…”
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Histone H2B ubiquitylation disrupts local and higher-order chromatin compaction by Muir, Tom W, Fierz, Beat, Chatterjee, Champak, McGinty, Robert K, Bar-Dagan, Maya, Raleigh, Daniel P

“…Ubiquitylated histone H2B (uH2B) is a known chromatin modification involved in transcription. Analysis of nucleosome arrays containing chemically synthesized…”
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Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology by Cao, Ping, Abedini, Andisheh, Raleigh, Daniel P

“…[Display omitted] ► Islet amyloid contributes to type-2 diabetes and to islet transplant failure. ► IAPP is natively unfolded, but is one of the most…”
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Ion Mobility Spectrometry–Mass Spectrometry Defines the Oligomeric Intermediates in Amylin Amyloid Formation and the Mode of Action of Inhibitors by Young, Lydia M, Cao, Ping, Raleigh, Daniel P, Ashcroft, Alison E, Radford, Sheena E

“…The molecular mechanisms by which different proteins assemble into highly ordered fibrillar deposits and cause disease remain topics of debate. Human amylin…”
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Screening and classifying small-molecule inhibitors of amyloid formation using ion mobility spectrometry–mass spectrometry by Young, Lydia M., Saunders, Janet C., Mahood, Rachel A., Revill, Charlotte H., Foster, Richard J., Tu, Ling-Hsien, Raleigh, Daniel P., Radford, Sheena E., Ashcroft, Alison E.

“…The search for therapeutic agents that bind specifically to precursor protein conformations and inhibit amyloid assembly is an important challenge. Identifying…”
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Islet amyloid polypeptide toxicity and membrane interactions by Cao, Ping, Abedini, Andisheh, Wang, Hui, Tu, Ling-Hsien, Zhang, Xiaoxue, Schmidt, Ann Marie, Raleigh, Daniel P.

“…Islet amyloid polypeptide (IAPP) is responsible for amyloid formation in type 2 diabetes and contributes to the failure of islet cell transplants, however the…”
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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 Toxicity by Meng, Fanling, Abedini, Andisheh, Plesner, Annette, Verchere, C. Bruce, Raleigh, Daniel P

“…Islet amyloid polypeptide (IAPP, amylin) is the major protein component of the islet amyloid deposits associated with type 2 diabetes. The polypeptide lacks a…”
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Ionic Strength Effects on Amyloid Formation by Amylin Are a Complicated Interplay among Debye Screening, Ion Selectivity, and Hofmeister Effects by Marek, Peter J, Patsalo, Vadim, Green, David F, Raleigh, Daniel P

“…Amyloid formation plays a role in a wide range of human diseases. The rate and extent of amyloid formation depend on solution conditions, including pH and…”
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Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet by Buchanan, Lauren E., Dunkelberger, Emily B., Tran, Huong Q., Cheng, Pin-Nan, Chiu, Chi-Cheng, Cao, Ping, Raleigh, Daniel P., de Pablo, Juan J., Nowick, James S., Zanni, Martin T.

“…Amyloid formation is implicated in more than 20 human diseases, yet the mechanism by which fibrils form is not well understood. We use 2D infrared spectroscopy…”
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Islet amyloid: From fundamental biophysics to mechanisms of cytotoxicity by Cao, Ping, Marek, Peter, Noor, Harris, Patsalo, Vadim, Tu, Ling-Hsien, Wang, Hui, Abedini, Andisheh, Raleigh, Daniel P.

“…Pancreatic islet amyloid is a characteristic feature of type 2 diabetes. The major protein component of islet amyloid is the polypeptide hormone known as islet…”
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A Free Energy Barrier Caused by the Refolding of an Oligomeric Intermediate Controls the Lag Time of Amyloid Formation by hIAPP by Serrano, Arnaldo L, Lomont, Justin P, Tu, Ling-Hsien, Raleigh, Daniel P, Zanni, Martin T

“…Transiently populated oligomers formed en route to amyloid fibrils may constitute the most toxic aggregates associated with many amyloid-associated diseases…”
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A role for helical intermediates in amyloid formation by natively unfolded polypeptides? by Abedini, Andisheh, Raleigh, Daniel P

“…Amyloid formation and aberrant protein aggregation have been implicated in more than 15 different human diseases and an even wider range of proteins form…”
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Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology by 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

“…The hormone islet amyloid polypeptide (IAPP, or amylin) plays a role in glucose homeostasis but aggregates to form islet amyloid in type-2 diabetes. Islet…”
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Two-Dimensional IR Spectroscopy and Isotope Labeling Defines the Pathway of Amyloid Formation with Residue-Specific Resolution by Shim, Sang-Hee, Gupta, Ruchi, Ling, Yun L., Strasfeld, David B., Raleigh, Daniel P., Zanni, Martin T., Hochstrasser, Robin M.

“…There is considerable interest in uncovering the pathway of amyloid formation because the toxic properties of amyloid likely stems from prefibril intermediates…”
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Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics by 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

“…Islet amyloidosis by IAPP contributes to pancreatic β-cell death in diabetes, but the nature of toxic IAPP species remains elusive. Using concurrent…”
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Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structure by Meng, Wenli, Lyle, Nicholas, Luan, Bowu, Raleigh, Daniel P., Pappu, Rohit V.

“…The sizes of unfolded proteins under highly denaturing conditions scale as N ⁰.⁵⁹ with chain length. This suggests that denaturing conditions mimic good…”
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Defining the Molecular Basis of Amyloid Inhibitors: Human Islet Amyloid Polypeptide–Insulin Interactions by Susa, Anna C, Wu, Chun, Bernstein, Summer L, Dupuis, Nicholas F, Wang, Hui, Raleigh, Daniel P, Shea, Joan-Emma, Bowers, Michael T

“…Human islet amyloid polypeptide (hIAPP or Amylin) is a 37 residue hormone that is cosecreted with insulin from the pancreatic islets. The aggregation of hIAPP…”
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