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Heike Goehler
Researcher at Max Delbrück Center for Molecular Medicine
Publications - 6
Citations - 3080
Heike Goehler is an academic researcher from Max Delbrück Center for Molecular Medicine. The author has contributed to research in topics: Huntingtin & Protein structure. The author has an hindex of 6, co-authored 6 publications receiving 2910 citations.
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Journal ArticleDOI
A human protein-protein interaction network : a resource for annotating the proteome
Ulrich Stelzl,Uwe Worm,Maciej Lalowski,Christian Haenig,Felix H. Brembeck,Heike Goehler,Martin Stroedicke,Martina Zenkner,Anke Schoenherr,Susanne Koeppen,Jan Timm,Sascha Mintzlaff,Claudia Abraham,Nicole Bock,Silvia Kietzmann,Astrid Goedde,Engin Toksöz,Anja Droege,Sylvia Krobitsch,Bernhard Korn,Walter Birchmeier,Hans Lehrach,Erich E. Wanker +22 more
TL;DR: A large, highly connected network of interacting pairs of human proteins was identified, characterizing ANP32A and CRMP1 as modulators of Wnt signaling and two novel Axin-1 interactions were validated experimentally.
Journal ArticleDOI
A Protein Interaction Network Links GIT1, an Enhancer of Huntingtin Aggregation, to Huntington’s Disease
Heike Goehler,Maciej Lalowski,Ulrich Stelzl,Stephanie Waelter,Martin Stroedicke,Uwe Worm,Anja Droege,Katrin S. Lindenberg,Maria Knoblich,Christian Haenig,Martin Herbst,Jaana Suopanki,Eberhard Scherzinger,Claudia Abraham,Bianca Bauer,Renate Hasenbank,Anja Fritzsche,Andreas H. Ludewig,Konrad Buessow,Sarah H. Coleman,Claire-Anne Gutekunst,Bernhard Landwehrmeyer,Hans Lehrach,Erich E. Wanker,Erich E. Wanker +24 more
TL;DR: A strategy combining library and matrix yeast two-hybrid screens to generate a highly connected PPI network for Huntington's disease (HD) revealed 165 new potential interactions and facilitated the discovery of GIT1, a G protein-coupled receptor kinase-interacting protein, which enhances huntingtin aggregation by recruitment of the protein into membranous vesicles.
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The huntingtin interacting protein HIP1 is a clathrin and alpha-adaptin-binding protein involved in receptor-mediated endocytosis.
Stephanie Waelter,Eberhard Scherzinger,Renate Hasenbank,Eckhard Nordhoff,Rudi Lurz,Heike Goehler,Christine Gauss,Kirupa Sathasivam,Gillian P. Bates,Hans Lehrach,Erich E. Wanker +10 more
TL;DR: Large perinuclear vesicle-like structures containing HIP1, huntingtin, clathrin and endocytosed transferrin were observed, indicating that HIP1 is an endocytic protein, the structural integrity of which is crucial for maintenance of normal vesicles size in vivo.
Journal ArticleDOI
Huntingtin interacts with the receptor sorting family protein GASP2.
TL;DR: The verification of the interaction between htt and GASP2 (G protein-coupled receptor associated sorting protein 2), a protein involved in membrane receptor degradation, is described, suggesting that htt might influence receptor trafficking via the interaction with GASp2.
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Pathogenic polyglutamine tracts are potent inducers of spontaneous Sup35 and Rnq1 amyloidogenesis.
TL;DR: Investigating whether aggregation-promoting polyglutamine (polyQ) tracts can stimulate the de novo formation of ordered Sup35 protein aggregates in the absence of Q/N-rich yeast prions found that Sup35 fusions with pathogenic polyQ tracts efficiently form seeding-competentprotein aggregates.