G
Georg Lipps
Researcher at University of Applied Sciences and Arts Northwestern Switzerland FHNW
Publications - 50
Citations - 5617
Georg Lipps is an academic researcher from University of Applied Sciences and Arts Northwestern Switzerland FHNW. The author has contributed to research in topics: Primase & Sulfolobus. The author has an hindex of 24, co-authored 49 publications receiving 4352 citations. Previous affiliations of Georg Lipps include Life Sciences Institute & Center for Integrated Protein Science Munich.
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Journal ArticleDOI
Biological properties of extracellular vesicles and their physiological functions
María Yáñez-Mó,Pia Siljander,Zoraida Andreu,Apolonija Bedina Zavec,Francesc E. Borràs,Edit I. Buzás,Krisztina Buzas,Krisztina Buzas,Enriqueta Casal,Francesco Cappello,Joana Carvalho,Joana Carvalho,Eva Colas,Anabela Cordeiro da Silva,Anabela Cordeiro da Silva,Stefano Fais,Juan M. Falcón-Pérez,Irene M. Ghobrial,Bernd Giebel,Mario Gimona,Mario Gimona,Michael W. Graner,Ihsan Gursel,Mayda Gursel,Niels H. H. Heegaard,Niels H. H. Heegaard,An Hendrix,Peter Kierulf,Katsutoshi Kokubun,Maja Kosanović,Veronika Kralj-Iglič,Eva-Maria Krämer-Albers,Saara Laitinen,Cecilia Lässer,Thomas Lener,Thomas Lener,Erzsébet Ligeti,Aija Linē,Georg Lipps,Alicia Llorente,Jan Lötvall,Mateja Manček-Keber,Antonio Marcilla,María Mittelbrunn,Irina Nazarenko,Esther N. M. Nolte-‘t Hoen,Tuula A. Nyman,Lorraine O'Driscoll,Mireia Olivan,Carla Oliveira,Carla Oliveira,Éva Pállinger,Hernando A. del Portillo,Hernando A. del Portillo,Jaume Reventós,Jaume Reventós,Marina Rigau,Eva Rohde,Eva Rohde,Marei Sammar,Francisco Sánchez-Madrid,Nuno Santarém,Nuno Santarém,Katharina Schallmoser,Katharina Schallmoser,Marie Stampe Ostenfeld,Willem Stoorvogel,Roman Štukelj,Susanne G. van der Grein,M. Helena Vasconcelos,M. Helena Vasconcelos,Marca H. M. Wauben,Olivier De Wever +72 more
TL;DR: A comprehensive overview of the current understanding of the physiological roles of EVs is provided, drawing on the unique EV expertise of academia-based scientists, clinicians and industry based in 27 European countries, the United States and Australia.
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Evidence-Based Clinical Use of Nanoscale Extracellular Vesicles in Nanomedicine
Stefano Fais,Lorraine O'Driscoll,Francesc E. Borràs,Edit I. Buzás,Giovanni Camussi,Francesco Cappello,Joana Carvalho,Anabela Cordeiro da Silva,Hernando A. del Portillo,Samir El Andaloussi,Samir El Andaloussi,Tanja Ficko Trček,Roberto Furlan,An Hendrix,Ihsan Gursel,Veronika Kralj-Iglič,Bertrand Kaeffer,Maja Kosanović,Marilena E. Lekka,Georg Lipps,Mariantonia Logozzi,Antonio Marcilla,Marei Sammar,Alicia Llorente,Irina Nazarenko,Carla Oliveira,Gabriella Pocsfalvi,Lawrence Rajendran,Graça Raposo,Eva Rohde,Pia Siljander,Guillaume van Niel,M. Helena Vasconcelos,María Yáñez-Mó,Marjo Yliperttula,Natasa Zarovni,Apolonija Bedina Zavec,Bernd Giebel +37 more
TL;DR: The high potential of nanosized EVs for both diagnostic and therapeutic areas of nanomedicine, as demonstrated by the European Network on Microvesicles and Exosomes in Health and Disease (ME-HAD), is demonstrated.
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The XPC-HR23B complex displays high affinity and specificity for damaged DNA in a true-equilibrium fluorescence assay.
TL;DR: A quantitative study on the binding of XPC to damaged DNA using fluorescence anisotropy measurements and competition experiments with undamaged and damaged plasmid DNA indicate that the XPC-HR23B complex discriminates between damaged and undamaging sites with high specificity.
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A novel type of replicative enzyme harbouring ATPase, primase and DNA polymerase activity.
TL;DR: A new type of replication protein that constitutes the first member of the DNA polymerase family E. ORF904, encoded by the plasmid pRN1 from the thermoacidophile archaeon Sulfolobus islandicus, is a highly compact multifunctional enzyme with ATPase, primase andDNA polymerase activity.
Journal ArticleDOI
Structure of a bifunctional DNA primase-polymerase.
TL;DR: It is proposed that archaeal and eukaryotic primases and the prim-pol domain have a common evolutionary ancestor, a bifunctional replicase for small DNA genomes.