Author

C. P. Richter

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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Biophysics· 2 Cell Biology· 1 Microbiology· 1

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Research Focus:cell signaling & trafficking· 4 Approach:microscopy & imaging analysis· 3 Assay:fluorescence / live-cell microscopy· 2 Organism:human· 2 Assay:bulk RNA-seq· 1 Research Focus:cell type annotation· 1 Research Focus:clustering· 1 Approach:deep learning· 1

Frequent Co-Authors

J. Piehler· 2 shared R. Kurre· 2 shared A. Kehl· 1 shared A. Plueckthun· 1 shared C. John· 1 shared C. You· 1 shared F. Hager· 1 shared H. Winkelmann· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersBiophysics

J. Piehler

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Author profile →

4 papers

Recent·Most cited

Correlative single-molecule and structured illumination microscopy of fast dynamics at the plasma membrane

H. Winkelmann, C. P. Richter, J. Eising, J. Piehler, R. Kurre

The paper combines TIRF and structured illumination microscopy to enable quantitative single-molecule analysis and track receptor dynamics in the plasma membrane.

bioRxiv · Oct 7, 2023 · PreprintBiophysics

Biofunctional nanodot arrays in living cells uncover synergistic co-condensation of Wnt signalodroplets

M. Philippi, C. P. Richter, M. Kappen, I. Watrinet, Y. Miao, M. Runge, L. Jorde, S. Korneev, M. Holtmannspoetter, R. Kurre, J. Holthuis, K. C. Garcia, A. Plueckthun, M. Steinhart, J. Piehler, C. You

The paper develops biofunctional nanodot arrays to study Wnt signalodroplets in live cells, revealing synergistic co-condensation through liquid-liquid phase separation.

bioRxiv · Jun 11, 2022Biophysics

A trafficome-wide RNAi screen reveals deployment of early and late secretory host proteins and the entire late endo-/lysosomal vesicle fusion machinery by intracellular Salmonella

A. Kehl, V. Göser, T. Reuter, V. Liss, M. Franke, C. John, C. P. Richter, J. Deiwick, M. Hensel

This study identifies host factors involved in Salmonella-induced endosomal remodeling through an RNAi screen, revealing key roles for SNARE complexes, GTPases, and clathrin-coated structures.

bioRxiv · Nov 19, 2019Microbiology

F1FO ATP synthase responds to glycolysis inhibition by localization into the inner boundary membrane

K. Zalyevskiy, F. Hager, C. P. Richter, K. Psathaki, T. Appelhans, K.B. Busch

This study shows that mitochondrial F1F0 ATP synthase relocates from cristae to the inner boundary membrane when glycolysis is inhibited, indicating dynamic spatial organization.

bioRxiv · Jul 23, 2018 · PreprintCell Biology