Author

C. Tueting

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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Biochemistry· 6 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Research Focus:protein structure prediction· 6 Assay:cryo-EM· 4 Assay:proteomics· 3 Organism:human· 2 Approach:microscopy & imaging analysis· 2 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1

Frequent Co-Authors

P. L. Kastritis· 7 shared A. Sinz· 5 shared F. L. Kyrilis· 4 shared C. H. Ihling· 3 shared D. A. Semchonok· 3 shared F. Hamdi· 3 shared A. Meister· 2 shared C. Iacobucci· 2 shared

Activity by Year

2018-2022 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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7 shared papersBiochemistry

P. L. Kastritis

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

Structural Assessment of the Full-Length Wild-Type Tumor Suppressor Protein p53 by Mass Spectrometry-Guided Computational Modeling

A. Di Ianni, C. Tueting, M. Kipping, C. H. Ihling, J. S. Koeppen, C. Iacobucci, C. Arlt, P. L. Kastritis, A. Sinz

This study uses mass spectrometry and computational modeling to assess the structure of full-length wild-type p53, revealing compaction of the C-terminal region and supporting a model of DNA binding.

bioRxiv · Nov 11, 2022 · PreprintBiochemistry

AI-guided cryo-EM probes a thermophilic cell-free system with succinyl-coA manufacturing capability

I. Skalidis, F. L. Kyrilis, C. Tueting, F. Hamdi, T. K. Traeger, J. Belapure, G. Hause, M. Fratini, F. J. O'Reilly, I. Heilmann, J. Rappsilber, P. L. Kastritis

The paper characterizes a thermophilic cell-free system producing succinyl-CoA using cryo-EM and biochemical methods, revealing its molecular structure and functional organization.

bioRxiv · Oct 8, 2022 · PreprintBiochemistry

Delineating organizational principles of the endogenous L-A virus by cryo-EM and computational analysis of native cell extracts

L. Schmidt, C. Tueting, F. L. Kyrilis, F. Hamdi, D. A. Semchonok, G. Hause, A. Meister, C. Ihling, P. N. Shah, M. T. Stubbs, A. Sinz, D. I. Stuart, P. L. Kastritis

The paper uses cryo-EM and computational analysis to study the structure and organization of the yeast L-A virus in native cell extracts, revealing capsid architecture and viral community dynamics.

bioRxiv · Jul 15, 2022Biochemistry

Cryo-EM structure of the Rhodobaca bogoriensis RC-LH1-PufX dimeric complex at 2.9 A

D. A. Semchonok, M. I. Siponen, C. Tueting, Q. Charras, F. L. Kyrilis, Y. Sadian, C. Jungas, P. L. Kastritis

The paper presents a cryo-EM structure of the RC-LH1-PufX dimeric complex in Rhodobaca bogoriensis, revealing its architecture and interactions.

bioRxiv · Feb 25, 2022 · PreprintBiophysics

First 3D-Structural Data of Full-length Rod-Outer-Segment Guanylyl Cyclase 1 in Bovine Retina by Cross-linking/Mass Spectrometry

A. Rehkamp, D. Taenzler, C. Tueting, P. L. Kastritis, C. H. Ihling, M. Kipping, K.-W. Koch, A. Sinz

The paper presents the first 3D-structural analysis of active, full-length ROS-GC1 in bovine retina using XL-MS and computational modeling, revealing a novel domain organization and dimeric architecture.

bioRxiv · Sep 25, 2020Biochemistry

Structural Analysis of 70S Ribosomes by Cross-Linking/Mass Spectrometry Reveals Conformational Plasticity

C. Tueting, C. Iacobucci, C. H. Ihling, P. L. Kastritis, A. Sinz

This study uses XL-MS to analyze E. coli ribosome structures, revealing conformational plasticity and remodeling 2,057 residues with high accuracy.

bioRxiv · May 4, 2020Biochemistry

2.7 A cryo-EM structure of vitrified M. musculus H-chain apoferritin from 200 keV \"screening microscope\"

F. Hamdi, C. Tueting, D. A. Semchonok, K. M. Visscher, F. L. Kyrilis, A. Meister, I. Skalidis, L. Schmidt, C. Parthier, M. T. Stubbs, P. L. Kastritis

The paper solves the 2.7 Å structure of mouse H-chain apoferritin using a 200 keV cryo-EM screening microscope without energy filters or aberration correctors.

bioRxiv · Aug 31, 2019Biophysics

Reconstitution of mammalian Cleavage Factor II involved in 3’ processing of mRNA precursors

P. Schaefer, C. Tueting, L. Schoenemann, U. Kuehn, T. Treiber, N. Treiber, C. Ihling, A. Graber, W. Keller, G. Meister, A. Sinz, E. Wahle

This study reconstitutes mammalian Cleavage Factor II as a heterodimer of hPcf11 and hClp1, showing its activity in RNA cleavage and RNA binding preferences.

bioRxiv · Aug 16, 2018Biochemistry