Author
J. Lauer
Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.
Biology Disciplines
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2019-2022 · peak 2/yrCo-Author Collaboration Network
10 top collaborators · 13 mutual co-author links6 papers
Recent·Most cited
GTPase-dependent cyclic flexibility transitions drive the two-component EEA1-Rab5 molecular motor
A. Singh, J. A. Soler, J. Lauer, S. W. Grill, M. Jahnel, M. Zerial, S. Thutupalli
This study shows that Rab5 and EEA1 form a two-component molecular motor using GTP hydrolysis to drive cyclic flexibility transitions that perform mechanical work.
bioRxiv · Jul 18, 2022 · PreprintBiophysics
Structure of the human FERRY Rab5 effector complex
D. Quentin, J. Schuhmacher, B. U. Klink, J. Lauer, T. Shaikh, P. J. Huis in 't Veld, L. M. Welp, H. Urlaub, M. Zerial, S. Raunser
The paper determines the cryo-EM structure of the human FERRY Rab5 effector complex and shows Fy-2 acts as a binding hub for subunits and mRNA/Rab5.
bioRxiv · Jun 21, 2021 · PreprintBiochemistry
Multi-animal pose estimation and tracking with DeepLabCut
J. Lauer, M. Zhou, S. Ye, W. Menegas, T. Nath, M. M. Rahman, V. Di Santo, D. Soberanes, G. Feng, V. N. Murthy, G. Lauder, C. Dulac, M. W. Mathis, A. Mathis
The paper enhances DeepLabCut for multi-animal pose estimation and tracking by adding identity prediction and robust assembly features, validated on four benchmark datasets.
bioRxiv · Apr 30, 2021Animal Behavior & Cognition
A non-linear system patterns Rab5 GTPase on the membrane
A. Cezanne, J. Lauer, A. Solomatina, I. F. Sbalzarini, M. Zerial
The paper demonstrates that Rab5 GTPase forms membrane patterns through a handover mechanism involving Rabex5/Rabaptin5 and requires an endosomal lipid composition.
bioRxiv · Dec 17, 2019Biochemistry
Allosteric structural alterations and auto-regulation of Rab5 GEF activity in Rabex5
J. Lauer, A. Cezanne, G. Guaitoli, F. Raimondi, M. Gentzel, V. Alva, M. Habeck, M. Ueffing, A. N. Lupas, C. J. Gloeckner, M. Zerial
This study reevaluates the autoinhibition mechanism of Rabex5 by analyzing structural changes and nucleotide exchange activity, revealing new regulatory roles for Ubiquitin binding domains.
bioRxiv · Feb 27, 2019 · PreprintBiophysics