His primary areas of investigation include Alpha-synuclein, Biochemistry, Protein folding, Protein structure and Crystallography. His research integrates issues of Lewy body, Fibril, Wild type, Phosphorylation and Amyloid in his study of Alpha-synuclein. The various areas that David Eliezer examines in his Biochemistry study include Molecular biology and Cell biology.
His Protein folding research includes elements of Biophysics, Gel electrophoresis, Protein quaternary structure and Escherichia coli. The concepts of his Protein structure study are interwoven with issues in Peptide sequence and Plasma protein binding. His study in Crystallography is interdisciplinary in nature, drawing from both Nuclear magnetic resonance spectroscopy and Protein secondary structure.
Alpha-synuclein, Biophysics, Biochemistry, Crystallography and Cell biology are his primary areas of study. He has included themes like Lewy body, Protein aggregation, Mutant, Phosphorylation and Mitochondrion in his Alpha-synuclein study. His Biophysics research is multidisciplinary, relying on both Membrane, Microtubule, Synuclein and Circular dichroism.
David Eliezer combines subjects such as Protein secondary structure and Protein folding with his study of Crystallography. His studies deal with areas such as Folding, Native state and Nuclear magnetic resonance spectroscopy as well as Protein folding. His work deals with themes such as Exocytosis, In vitro, Synaptic vesicle and Cell membrane, which intersect with Cell biology.
David Eliezer mainly focuses on Biophysics, Cell biology, Alpha-synuclein, Membrane and Synaptic vesicle. His Biophysics study integrates concerns from other disciplines, such as Nuclear magnetic resonance spectroscopy and Intracellular. His research on Cell biology also deals with topics like
His Alpha-synuclein research is multidisciplinary, incorporating elements of Lability, α synuclein, Lipid vesicle and Vesicle exocytosis. His Synaptic vesicle research includes themes of Exocytosis, Helix, Relaxation and Synuclein. His Complexin study combines topics in areas such as Protein tertiary structure and Protein folding.
David Eliezer spends much of his time researching Cell biology, Biophysics, Synaptic vesicle, Alpha-synuclein and α synuclein. His biological study spans a wide range of topics, including Cell, Cell culture and Tauopathy. His Biophysics study incorporates themes from Transporter, Extracellular, Protein domain, Nuclear magnetic resonance spectroscopy and Intracellular.
His Synaptic vesicle study also includes fields such as
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Conformational properties of alpha-synuclein in its free and lipid-associated states.
David Eliezer;Esin Kutluay;Robert Bussell;Gillian Browne.
Journal of Molecular Biology (2001)
α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer.
Bruno Fauvet;Martial Kamdem Mbefo;Mohamed-Bilal Fares;Carole Desobry.
Journal of Biological Chemistry (2012)
Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding.
David Eliezer;Jian Yao;H. Jane Dyson;Peter E. Wright.
Nature Structural & Molecular Biology (1998)
A Structural and Functional Role for 11-mer Repeats in α-Synuclein and Other Exchangeable Lipid Binding Proteins
Robert Bussell;David Eliezer.
Journal of Molecular Biology (2003)
Biophysical characterization of intrinsically disordered proteins.
Current Opinion in Structural Biology (2009)
Phosphorylation at Ser-129 but Not the Phosphomimics S129E/D Inhibits the Fibrillation of α-Synuclein
Katerina E. Paleologou;Adrian W. Schmid;Carla C. Rospigliosi;Hai Young Kim.
Journal of Biological Chemistry (2008)
Biophysics of Parkinson's disease: structure and aggregation of alpha-synuclein.
Vladimir N Uversky;David Eliezer.
Current Protein & Peptide Science (2009)
Residual Structure and Dynamics in Parkinson's Disease-associated Mutants of α-Synuclein
Robert Bussell;David Eliezer.
Journal of Biological Chemistry (2001)
Membrane-Bound α-Synuclein Forms an Extended Helix: Long-Distance Pulsed ESR Measurements Using Vesicles, Bicelles, and Rodlike Micelles
Elka R. Georgieva;Trudy F. Ramlall;Peter P. Borbat;Jack H. Freed.
Journal of the American Chemical Society (2008)
Is apomyoglobin a molten globule? Structural characterization by NMR.
David Eliezer;Peter E. Wright.
Journal of Molecular Biology (1996)
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