Erich E. Wanker focuses on Huntingtin, Huntingtin Protein, Cell biology, Biochemistry and Protein aggregation. His Huntingtin study is concerned with the larger field of Huntington's disease. His Huntingtin Protein research is multidisciplinary, relying on both Molecular biology, Polyglutamine tract and Signal transducing adaptor protein.
His research integrates issues of Huntingtin-interacting protein 1, Binding protein, Transgene and Heat shock protein in his study of Cell biology. His research in Fibrillogenesis tackles topics such as Amyloid which are related to areas like Amino acid. The Genetics study combines topics in areas such as Scoring system and Computational biology.
Erich E. Wanker spends much of his time researching Cell biology, Huntingtin, Biochemistry, Genetics and Huntingtin Protein. He has included themes like Ubiquitin, Pathogenesis, Apoptosis, Programmed cell death and Inclusion bodies in his Cell biology study. His Huntingtin research is multidisciplinary, incorporating perspectives in Molecular biology, Nuclear protein and Neurodegeneration.
His Biochemistry research incorporates elements of Toxicity and Amyloid. His studies deal with areas such as Plasma protein binding and Computational biology as well as Genetics. His biological study spans a wide range of topics, including Mutation, Polyglutamine tract and Signal transducing adaptor protein.
His primary scientific interests are in Cell biology, Huntington's disease, Huntingtin, Biophysics and Fibril. His Cell biology research integrates issues from Pathogenesis, Mutant, Gene, Cofactor and Genetically modified mouse. His specific area of interest is Huntington's disease, where he studies Huntingtin Protein.
He interconnects RNA-binding protein and RNA splicing, Spliceosome in the investigation of issues within Huntingtin. His Biophysics research is multidisciplinary, incorporating elements of Lewy body and Amyloid fibril, Amyloid. In his research, Peptide, Plasma protein binding, Bioluminescence and Neuronal ceroid lipofuscinosis is intimately related to Small molecule, which falls under the overarching field of Fibril.
His main research concerns Cell biology, Huntingtin, Huntington's disease, Fibril and Neuroscience. His study in Cell biology is interdisciplinary in nature, drawing from both HEK 293 cells, Chaperone complex, Mutant and Trinucleotide repeat expansion. His Huntingtin study frequently draws parallels with other fields, such as Small molecule.
The various areas that Erich E. Wanker examines in his Huntington's disease study include Phenotype and Inclusion bodies. His Neuroscience study integrates concerns from other disciplines, such as Huntingtin Protein, Protein aggregation, Polyglutamine tract and Proteomics. His Huntingtin Protein research is classified as research in Disease.
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FORMATION OF NEURONAL INTRANUCLEAR INCLUSIONS UNDERLIES THE NEUROLOGICAL DYSFUNCTION IN MICE TRANSGENIC FOR THE HD MUTATION
Stephen W Davies;Mark Turmaine;Barbara A Cozens;Marian DiFiglia.
Cell (1997)
A human protein-protein interaction network : a resource for annotating the proteome
Ulrich Stelzl;Uwe Worm;Maciej Lalowski;Christian Haenig.
Cell (2005)
Huntingtin-Encoded Polyglutamine Expansions Form Amyloid-like Protein Aggregates In Vitro and In Vivo
Eberhard Scherzinger;Rudi Lurz;Mark Turmaine;Laura Mangiarini.
Cell (1997)
EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers.
Dagmar E Ehrnhoefer;Jan Bieschke;Annett Boeddrich;Martin Herbst.
Nature Structural & Molecular Biology (2008)
The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription.
Joan S. Steffan;Aleksey Kazantsev;Olivera Spasic-Boskovic;Marilee Greenwald.
Proceedings of the National Academy of Sciences of the United States of America (2000)
Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: Implications for Huntington’s disease pathology
Eberhard Scherzinger;Annie Sittler;Katja Schweiger;Volker Heiser.
Proceedings of the National Academy of Sciences of the United States of America (1999)
An empirical framework for binary interactome mapping
Kavitha Venkatesan;Kavitha Venkatesan;Jean François Rual;Alexei Vazquez;Alexei Vazquez;Ulrich Stelzl.
Nature Methods (2009)
EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity
Jan Bieschke;Jenny Russ;Ralf P. Friedrich;Dagmar E. Ehrnhoefer.
Proceedings of the National Academy of Sciences of the United States of America (2010)
Accumulation of Mutant Huntingtin Fragments in Aggresome-like Inclusion Bodies as a Result of Insufficient Protein Degradation
Stephanie Waelter;Annett Boeddrich;Rudi Lurz;Eberhard Scherzinger.
Molecular Biology of the Cell (2001)
Hsp70 and Hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils
Paul J. Muchowski;Gregor Schaffar;Annie Sittler;Erich E. Wanker.
Proceedings of the National Academy of Sciences of the United States of America (2000)
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