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Christoph F. Kurat
Researcher at Ludwig Maximilian University of Munich
Publications - 21
Citations - 1986
Christoph F. Kurat is an academic researcher from Ludwig Maximilian University of Munich. The author has contributed to research in topics: Chromatin & Chromatin remodeling. The author has an hindex of 11, co-authored 17 publications receiving 1602 citations. Previous affiliations of Christoph F. Kurat include University of Toronto & Francis Crick Institute.
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Journal ArticleDOI
A global genetic interaction network maps a wiring diagram of cellular function
Michael Costanzo,Benjamin VanderSluis,Elizabeth N. Koch,Anastasia Baryshnikova,Carles Pons,Guihong Tan,Wen Wang,Matej Usaj,Julia Hanchard,Susan D. Lee,Vicent Pelechano,Erin B. Styles,Maximilian Billmann,Jolanda van Leeuwen,Nydia Van Dyk,Zhen Yuan Lin,Elena Kuzmin,Justin Nelson,Jeff S. Piotrowski,Tharan Srikumar,Sondra Bahr,Yiqun Chen,Raamesh Deshpande,Christoph F. Kurat,Sheena C. Li,Zhijian Li,Mojca Mattiazzi Usaj,Hiroki Okada,Natasha Pascoe,Bryan Joseph San Luis,Sara Sharifpoor,Emira Shuteriqi,Scott W. Simpkins,Jamie Snider,Harsha Garadi Suresh,Yizhao Tan,Hongwei Zhu,Noël Malod-Dognin,Vuk Janjić,Natasa Przulj,Natasa Przulj,Olga G. Troyanskaya,Igor Stagljar,Tian Xia,Tian Xia,Yoshikazu Ohya,Anne-Claude Gingras,Brian Raught,Michael Boutros,Lars M. Steinmetz,Lars M. Steinmetz,Claire Moore,Adam P. Rosebrock,Amy A. Caudy,Chad L. Myers,Brenda J. Andrews,Charles Boone +56 more
TL;DR: A global genetic interaction network highlights the functional organization of a cell and provides a resource for predicting gene and pathway function and how coherent sets of negative or positive genetic interactions connect protein complex and pathways to map a functional wiring diagram of the cell.
Journal ArticleDOI
Chromatin Controls DNA Replication Origin Selection, Lagging-Strand Synthesis, and Replication Fork Rates
TL;DR: The minimum requirements for chromatin replication in vitro are defined and how multiple chromatin factors might modulate replication fork rates in vivo are shown.
Journal ArticleDOI
Global Gene Deletion Analysis Exploring Yeast Filamentous Growth
Owen Ryan,Rebecca S. Shapiro,Christoph F. Kurat,David Mayhew,Anastasia Baryshnikova,Brian L. Chin,Zhen-Yuan Lin,Michael J. Cox,Frederick S. Vizeacoumar,Doris Cheung,Sondra Bahr,Kyle Tsui,Faiza Tebbji,Faiza Tebbji,Adnane Sellam,Adnane Sellam,Fabian Istel,Tobias Schwarzmüller,Todd B. Reynolds,Karl Kuchler,David K. Gifford,David K. Gifford,Malcolm Whiteway,Malcolm Whiteway,Guri Giaever,Corey Nislow,Michael Costanzo,Anne-Claude Gingras,Anne-Claude Gingras,Robi D. Mitra,Brenda J. Andrews,Gerald R. Fink,Gerald R. Fink,Leah E. Cowen,Charles Boone +34 more
TL;DR: This work constructed a genome-wide set of targeted deletion alleles and introduced them into a filamentous S. cerevisiae strain and identified genes involved in morphologically distinct forms of filamentation: haploid invasive growth, biofilm formation, and diploid pseudohyphal growth.
Journal ArticleDOI
The mammalian-membrane two-hybrid assay (MaMTH) for probing membrane-protein interactions in human cells
Julia Petschnigg,Bella Groisman,Max Kotlyar,Mikko Taipale,Yong Zheng,Christoph F. Kurat,Christoph F. Kurat,Azin Sayad,J Rafael Sierra,Mojca Mattiazzi Usaj,Jamie Snider,Alex Nachman,Irina Krykbaeva,Ming-Sound Tsao,Ming-Sound Tsao,Jason Moffat,Tony Pawson,Susan Lindquist,Susan Lindquist,Igor Jurisica,Igor Jurisica,Igor Stagljar +21 more
TL;DR: MaMTH can detect changes in PPIs conferred by mutations such as those in oncogenic ErbB receptor variants or by treatment with drugs such as the tyrosine kinase inhibitor erlotinib and is a powerful tool for investigating the dynamic interactomes of human integral membrane proteins.
Journal ArticleDOI
Dissecting BAR Domain Function in the Yeast Amphiphysins Rvs161 and Rvs167 during Endocytosis
Ji-Young Youn,Helena Friesen,Takuma Kishimoto,William Mike Henne,Christoph F. Kurat,Wei Ye,Derek F. Ceccarelli,Frank Sicheri,Sepp D. Kohlwein,Harvey T. McMahon,Brenda J. Andrews +10 more
TL;DR: Using a structure–function analysis, it is found that Rvs proteins are initially recruited to sites of endocytosis through their curvature-sensing and membrane-binding ability in a manner dependent on complex sphingolipids.