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Carolin Sailer
Researcher at University of Konstanz
Publications - 15
Citations - 332
Carolin Sailer is an academic researcher from University of Konstanz. The author has contributed to research in topics: Biology & Gene. The author has an hindex of 5, co-authored 10 publications receiving 166 citations.
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Journal ArticleDOI
First Community-Wide, Comparative Cross-Linking Mass Spectrometry Study.
Claudio Iacobucci,Christine Piotrowski,Ruedi Aebersold,Ruedi Aebersold,Bruno C. Amaral,Philip C. Andrews,Katja Bernfur,Christoph H. Borchers,Nicolas I. Brodie,James E. Bruce,Yong Cao,Stéphane Chaignepain,Juan D. Chavez,Stéphane Claverol,Jürgen Cox,Trisha N. Davis,Gianluca Degliesposti,Meng-Qiu Dong,Nufar Edinger,Cecilia Emanuelsson,Michael Götze,Francisco Gomes-Neto,Fabio C. Gozzo,Craig B. Gutierrez,Caroline Haupt,Albert J. R. Heck,Franz Herzog,Lan Huang,Michael R. Hoopmann,Nir Kalisman,Oleg Klykov,Zdeněk Kukačka,Fan Liu,Michael J. MacCoss,Karl Mechtler,Ravit Mesika,Robert L. Moritz,Nagarjuna Nagaraj,Victor Nesati,Ana G.C. Neves-Ferreira,Robert Ninnis,Petr Novák,Francis J. O’Reilly,Matthias Pelzing,Evgeniy V. Petrotchenko,Lolita Piersimoni,Manolo Plasencia,Tara L. Pukala,Kasper D. Rand,Juri Rappsilber,Juri Rappsilber,Dana Reichmann,Carolin Sailer,Chris P. Sarnowski,Chris P. Sarnowski,Richard A. Scheltema,Carla Schmidt,David C. Schriemer,Yi Shi,J. Mark Skehel,Moriya Slavin,Frank Sobott,Frank Sobott,Victor Solis-Mezarino,Heike Stephanowitz,Florian Stengel,Christian E. Stieger,Esben Trabjerg,Michael J. Trnka,Marta Vilaseca,Rosa Viner,Yufei Xiang,Şule Yılmaz,Alex Zelter,Daniel S. Ziemianowicz,Alexander Leitner,Andrea Sinz +76 more
TL;DR: This first, community-based harmonization study onXL-MS is based on the results of 32 groups participating worldwide and builds the framework for establishing best practice guidelines to conduct cross-linking experiments, perform data analysis, and define reporting formats with the ultimate goal of assisting scientists to generate accurate and reproducible XL-MS results.
Journal ArticleDOI
Structural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex
Carolin Sailer,Fabian Offensperger,Alexandra Julier,Kai-Michael Kammer,Ryan Walker-Gray,Matthew G. Gold,Martin Scheffner,Florian Stengel +7 more
TL;DR: The authors study the structural basis of this process by qualitative and quantitative cross-linking mass spectrometry, providing insights into E6AP-E6-p53 complex assembly and the conformational dynamics that enable p53 ubiquitination.
Journal ArticleDOI
Early Scanning of Nascent Polypeptides inside the Ribosomal Tunnel by NAC.
Martin Gamerdinger,Kan Kobayashi,Annalena Wallisch,Stefan G. Kreft,Carolin Sailer,Renate Schlömer,Nadine Sachs,Ahmad Jomaa,Florian Stengel,Nenad Ban,Elke Deuerling +10 more
TL;DR: It is demonstrated that the tunnel-probing activity of NAC is essential for organismal viability and critical to regulate endoplasmic reticulum (ER) protein transport by controlling ribosome-Sec61 translocon interactions.
Journal ArticleDOI
Mechanism of completion of peptidyltransferase centre assembly in eukaryotes.
Vasileios Kargas,Pablo Castro-Hartmann,Norberto Escudero-Urquijo,Kyle Dent,Christine Hilcenko,Carolin Sailer,Gertrude Zisser,Maria J Marques-Carvalho,Simone Pellegrino,Leszek Wawiórka,Stefan M.V. Freund,Jane L. Wagstaff,Antonina Andreeva,Alexandre Faille,Edwin Chen,Florian Stengel,Helmut Bergler,Alan J. Warren +17 more
TL;DR: The mechanism of peptidyltransferase centre (PTC) completion is presented that explains how integration of the last ribosomal proteins is coupled to release of the nuclear export adaptor Nmd3 and reveals how the central functional site of the ribosome is sculpted.
Journal ArticleDOI
The ubiquitin-like modifier FAT10 interferes with SUMO activation.
Annette Aichem,Carolin Sailer,Stella Ryu,Nicola Catone,Nicolas Stankovic-Valentin,Gunter Schmidtke,Frauke Melchior,Florian Stengel,Marcus Groettrup +8 more
TL;DR: Another function of FAT10 is identified, showing that it interferes with the activation of SUMO1/2/3 in vitro and down-regulates SUMO conjugation and the SUMO-dependent formation of promyelocytic leukemia protein (PML) bodies in cells.