Author

K. Boldt

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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Cell Biology· 3

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 3 Approach:experimental assay· 3 Assay:proteomics· 3 Organism:mouse· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Organism:human· 1

Frequent Co-Authors

C. K. Rezi· 2 shared G. D. Diwan· 2 shared K. Junger· 2 shared L. B. Pedersen· 2 shared M. Chamlali· 2 shared R. B. Russell· 2 shared S. T. Christensen· 2 shared Z. Anvarian· 2 shared

Activity by Year

2023-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 39 mutual co-author links

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2 shared papersCell Biology

C. K. Rezi

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

KIF13B controls ciliary protein content by promoting endocytic retrieval and suppressing release of large extracellular vesicles from cilia

C. K. Rezi, A. Frei, F. Campestre, K. Boldt, B. Mary, A. M. Fixdahl, A.-L. W. Petersen, A. Sicot, C. R. Berggreen, J. Laplace, S. L. Johansen, J. K. T. Sorensen, M. Chamlali, M. W. Berchtold, S. T. Christensen, , L. B. Pedersen

This study shows KIF13B regulates ciliary protein content by promoting endocytic retrieval and suppressing large EV release from cilia, with distinct effects during ciliation stages.

bioRxiv · Mar 21, 2024Cell Biology

DLG1 functions upstream of SDCCAG3 and IFT20 to control ciliary targeting of polycystin-2

C. K. Rezi, M. Aslanyan, G. D. Diwan, T. Cheng, M. Chamlali, K. Junger, Z. Anvarian, e. lorentzen, K. B. Pauly, Y. Bahadori, E. F. Fernandes, F. Qian, S. Tosi, S. T. Christensen, S. F. Pedersen, , L. B. Pedersen

This study shows DLG1 regulates ciliary protein trafficking in kidney cells, with loss of DLG1 causing ciliary elongation and cysts, and a specific DLG1 variant linked to kidney disease.

bioRxiv · Nov 10, 2023Cell Biology

Ciliopathy-associated missense mutations in IFT140 are hypomorphic and have edgetic effects on protein interaction networks

T. Leonhard, G. D. Diwan, F. Klose, I. F. Stehle, K. Junger, M. Seda, S. Bolz, F. Woerz, R. B. Russell, K. Boldt, D. Jenkins, M. Ueffing, T. Beyer

This study investigates how missense mutations in IFT140 affect protein interactions and complex stability, revealing hypomorphic and edgetic effects in ciliopathy-related diseases.

bioRxiv · Jan 18, 2023Cell Biology