The Experts below are selected from a list of 201564 Experts worldwide ranked by ideXlab platform
Kurt Warncke - One of the best experts on this subject based on the ideXlab platform.
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engineering Metal Ion coordinatIon to regulate amyloid fibril assembly and toxicity
Proceedings of the National Academy of Sciences of the United States of America, 2007Co-Authors: Jijun Dong, Jeffrey M Canfield, Seth W Childers, Anil K Mehta, Jacob E Shokes, Kurt Warncke, Robert A Scott, Bo Tian, David G LynnAbstract:Protein and peptide assembly into amyloid has been implicated in functIons that range from beneficial epigenetic controls to pathological etiologies. However, the exact structures of the assemblies that regulate biological activity remain poorly defined. We have previously used Zn2+ to modulate the assembly kinetics and morphology of congeners of the amyloid β peptide (Aβ) associated with Alzheimer's disease. We now reveal a correlatIon among Aβ-Cu2+ coordinatIon, peptide self-assembly, and neuronal viability. By using the central segment of Aβ, HHQKLVFFA or Aβ(13–21), which contains residues H13 and H14 implicated in Aβ-Metal Ion binding, we show that Cu2+ forms complexes with Aβ(13–21) and its K16A mutant and that the complexes, which do not self-assemble into fibrils, have structures similar to those found for the human prIon protein, PrP. N-terminal acetylatIon and H14A substitutIon, Ac-Aβ(13–21)H14A, alters Metal coordinatIon, allowing Cu2+ to accelerate assembly into neurotoxic fibrils. These results establish that the N-terminal regIon of Aβ can access different Metal-Ion-coordinatIon environments and that different complexes can lead to profound changes in Aβ self-assembly kinetics, morphology, and toxicity. Related Metal-Ion coordinatIon may be critical to the etiology of other neurodegenerative diseases.
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engineering Metal Ion coordinatIon to regulate amyloid fibril assembly and toxicity
Proceedings of the National Academy of Sciences of the United States of America, 2007Co-Authors: Jijun Dong, Jeffrey M Canfield, Seth W Childers, Anil K Mehta, Jacob E Shokes, Robert A Scott, Bo Tian, James A Simmons, Zixu Mao, Kurt WarnckeAbstract:Abstract Protein and peptide assembly into amyloid has been implicated in functIons that range from beneficial epigenetic controls to pathological etiologies. However, the exact structures of the assemblies that regulate biological activity remain poorly defined. We have previously used Zn2+ to modulate the assembly kinetics and morphology of congeners of the amyloid β peptide (Aβ) associated with Alzheimer's disease. We now reveal a correlatIon among Aβ-Cu2+ coordinatIon, peptide self-assembly, and neuronal viability. By using the central segment of Aβ, HHQKLVFFA or Aβ(13–21), which contains residues H13 and H14 implicated in Aβ-Metal Ion binding, we show that Cu2+ forms complexes with Aβ(13–21) and its K16A mutant and that the complexes, which do not self-assemble into fibrils, have structures similar to those found for the human prIon protein, PrP. N-terminal acetylatIon and H14A substitutIon, Ac-Aβ(13–21)H14A, alters Metal coordinatIon, allowing Cu2+ to accelerate assembly into neurotoxic fibrils. These results establish that the N-terminal regIon of Aβ can access different Metal-Ion-coordinatIon environments and that different complexes can lead to profound changes in Aβ self-assembly kinetics, morphology, and toxicity. Related Metal-Ion coordinatIon may be critical to the etiology of other neurodegenerative diseases. copper-binding neurotoxicity self-assembly
Jijun Dong - One of the best experts on this subject based on the ideXlab platform.
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engineering Metal Ion coordinatIon to regulate amyloid fibril assembly and toxicity
Proceedings of the National Academy of Sciences of the United States of America, 2007Co-Authors: Jijun Dong, Jeffrey M Canfield, Seth W Childers, Anil K Mehta, Jacob E Shokes, Kurt Warncke, Robert A Scott, Bo Tian, David G LynnAbstract:Protein and peptide assembly into amyloid has been implicated in functIons that range from beneficial epigenetic controls to pathological etiologies. However, the exact structures of the assemblies that regulate biological activity remain poorly defined. We have previously used Zn2+ to modulate the assembly kinetics and morphology of congeners of the amyloid β peptide (Aβ) associated with Alzheimer's disease. We now reveal a correlatIon among Aβ-Cu2+ coordinatIon, peptide self-assembly, and neuronal viability. By using the central segment of Aβ, HHQKLVFFA or Aβ(13–21), which contains residues H13 and H14 implicated in Aβ-Metal Ion binding, we show that Cu2+ forms complexes with Aβ(13–21) and its K16A mutant and that the complexes, which do not self-assemble into fibrils, have structures similar to those found for the human prIon protein, PrP. N-terminal acetylatIon and H14A substitutIon, Ac-Aβ(13–21)H14A, alters Metal coordinatIon, allowing Cu2+ to accelerate assembly into neurotoxic fibrils. These results establish that the N-terminal regIon of Aβ can access different Metal-Ion-coordinatIon environments and that different complexes can lead to profound changes in Aβ self-assembly kinetics, morphology, and toxicity. Related Metal-Ion coordinatIon may be critical to the etiology of other neurodegenerative diseases.
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engineering Metal Ion coordinatIon to regulate amyloid fibril assembly and toxicity
Proceedings of the National Academy of Sciences of the United States of America, 2007Co-Authors: Jijun Dong, Jeffrey M Canfield, Seth W Childers, Anil K Mehta, Jacob E Shokes, Robert A Scott, Bo Tian, James A Simmons, Zixu Mao, Kurt WarnckeAbstract:Abstract Protein and peptide assembly into amyloid has been implicated in functIons that range from beneficial epigenetic controls to pathological etiologies. However, the exact structures of the assemblies that regulate biological activity remain poorly defined. We have previously used Zn2+ to modulate the assembly kinetics and morphology of congeners of the amyloid β peptide (Aβ) associated with Alzheimer's disease. We now reveal a correlatIon among Aβ-Cu2+ coordinatIon, peptide self-assembly, and neuronal viability. By using the central segment of Aβ, HHQKLVFFA or Aβ(13–21), which contains residues H13 and H14 implicated in Aβ-Metal Ion binding, we show that Cu2+ forms complexes with Aβ(13–21) and its K16A mutant and that the complexes, which do not self-assemble into fibrils, have structures similar to those found for the human prIon protein, PrP. N-terminal acetylatIon and H14A substitutIon, Ac-Aβ(13–21)H14A, alters Metal coordinatIon, allowing Cu2+ to accelerate assembly into neurotoxic fibrils. These results establish that the N-terminal regIon of Aβ can access different Metal-Ion-coordinatIon environments and that different complexes can lead to profound changes in Aβ self-assembly kinetics, morphology, and toxicity. Related Metal-Ion coordinatIon may be critical to the etiology of other neurodegenerative diseases. copper-binding neurotoxicity self-assembly
N H L Wang - One of the best experts on this subject based on the ideXlab platform.
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immobilized Metal Ion affinity chromatography imac chemistry and bioseparatIon applicatIons
Separation and Purification Methods, 1991Co-Authors: Jon W Wong, Robert Lee Albright, N H L WangAbstract:Abstract This review discusses the principles of immobilized Metal Ion affinity chromatography (IMAC) and its applicatIons to protein separatIons. IMAC functIons by binding the accessible electron-donating pendant groups of a protein - such as histidine, cysteine, and tryptophan - to a Metal Ion which is held by a chelating group covalently attached on a statIonary support. A common chelating group is iminodiacetate. The Ions commonly used are of borderline or soft Metals, such as Cu2+, Ni2+, Co2+, and Zn2+. Protein retentIon in IMAC depends on the number and type of pendant groups which can interact with the Metal. The interactIon is affected by a variety of independent variables such as pH, temperature, solvent type, salt type, salt concentratIon, nature of immobilized Metal and chelate, ligand density, and protein size. Proteins are usually eluted by a decreasing pH gradient or by an increasing gradient of a competitive agent, such as imidazole, in a buffer. There are still several unresolved issues in...
Chongli Zhong - One of the best experts on this subject based on the ideXlab platform.
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a versatile mof based trap for heavy Metal Ion capture and dispersIon
Nature Communications, 2018Co-Authors: Yaguang Peng, Hongliang Huang, Yuxi Zhang, Chufan Kang, Shuangming Chen, Li Song, Dahuan Liu, Chongli ZhongAbstract:Current technologies for removing heavy Metal Ions are typically Metal Ion specific. Herein we report the development of a broad-spectrum heavy Metal Ion trap by incorporatIon of ethylenediaminetetraacetic acid into a robust Metal-organic framework. The capture experiments for a total of 22 heavy Metal Ions, covering hard, soft, and borderline Lewis Metal Ions, show that the trap is very effective, with removal efficiencies of >99% for single-component adsorptIon, multi-component adsorptIon, or in breakthrough processes. The material can also serve as a host for Metal Ion loading with arbitrary selectIons of Metal Ion amounts/types with a controllable uptake ratio to prepare well-dispersed single or multiple Metal catalysts. This is supported by the excellent performance of the prepared Pd2+-loaded composite toward the Suzuki coupling reactIon. This work proposes a versatile heavy Metal Ion trap that may find applicatIons in the fields of separatIon and catalysis.
David G Lynn - One of the best experts on this subject based on the ideXlab platform.
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engineering Metal Ion coordinatIon to regulate amyloid fibril assembly and toxicity
Proceedings of the National Academy of Sciences of the United States of America, 2007Co-Authors: Jijun Dong, Jeffrey M Canfield, Seth W Childers, Anil K Mehta, Jacob E Shokes, Kurt Warncke, Robert A Scott, Bo Tian, David G LynnAbstract:Protein and peptide assembly into amyloid has been implicated in functIons that range from beneficial epigenetic controls to pathological etiologies. However, the exact structures of the assemblies that regulate biological activity remain poorly defined. We have previously used Zn2+ to modulate the assembly kinetics and morphology of congeners of the amyloid β peptide (Aβ) associated with Alzheimer's disease. We now reveal a correlatIon among Aβ-Cu2+ coordinatIon, peptide self-assembly, and neuronal viability. By using the central segment of Aβ, HHQKLVFFA or Aβ(13–21), which contains residues H13 and H14 implicated in Aβ-Metal Ion binding, we show that Cu2+ forms complexes with Aβ(13–21) and its K16A mutant and that the complexes, which do not self-assemble into fibrils, have structures similar to those found for the human prIon protein, PrP. N-terminal acetylatIon and H14A substitutIon, Ac-Aβ(13–21)H14A, alters Metal coordinatIon, allowing Cu2+ to accelerate assembly into neurotoxic fibrils. These results establish that the N-terminal regIon of Aβ can access different Metal-Ion-coordinatIon environments and that different complexes can lead to profound changes in Aβ self-assembly kinetics, morphology, and toxicity. Related Metal-Ion coordinatIon may be critical to the etiology of other neurodegenerative diseases.
