Author

N. Kachariya

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· 2 Plant Biology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell type annotation· 3 Assay:proteomics· 3 Organism:Arabidopsis· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:gene regulatory network inference· 1 Organism:human· 1 Assay:metagenomics· 1

Frequent Co-Authors

M. Sattler· 4 shared B. Lenzen· 2 shared C. Schmitz-Linneweber· 2 shared J. Legen· 2 shared A. Itzen· 1 shared A. Wulf· 1 shared B. Braeuning· 1 shared E. Klotzsch· 1 shared

Activity by Year

2019-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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4 shared papersPlant Biology

M. Sattler

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Author profile →

4 papers

Recent·Most cited

The Chloroplast RNA Binding Protein CP29A supports rbcL expression during cold acclimation

B. Lenzen, F. Roesch, H. Ruwe, N. Kachariya, J. Legen, M. Sattler, I. D. Small, C. Schmitz-Linneweber

bioRxiv · Nov 24, 2023 · PreprintPlant Biology

The prion-like domain of the chloroplast RNA binding protein CP29A is required for cold-induced phase separation next to nucleoids and supports RNA splicing and translation during cold acclimation

J. Legen, B. Lenzen, N. Kachariya, S. Feltgen, Y. Gao, S. Mergenthal, W. Weber, E. Klotzsch, R. Zoschke, M. Sattler, C. Schmitz-Linneweber

This study shows that the prion-like domain of CP29A enables temperature-dependent phase separation in Arabidopsis, supporting RNA splicing and translation during cold acclimation.

bioRxiv · Sep 29, 2023 · PreprintPlant Biology

Npl3 functions in mRNP assembly by recruitment of mRNP components to the transcription site and their transfer onto the mRNA

P. Keil, A. Wulf, N. Kachariya, S. Reuscher, K. Huehn, I. Silbern, J. Altmueller, R. Stehle, K. Zarnack, M. Sattler, H. Urlaub, K. Straesser

The paper identifies Npl3's role in mRNP assembly by recruiting components to the transcription site and transferring them onto mRNA.

bioRxiv · Jul 22, 2022Biochemistry

PINK1-dependent phosphorylation of Serine111 within the SF3 motif of Rab GTPases impairs effector interactions and LRRK2 mediated phosphorylation at Threonine72

S. Vieweg, K. Mulholland, B. Braeuning, N. Kachariya, Y.-C. Lai, R. Toth, M. Sattler, M. Groll, A. Itzen, M. Muqit

This study shows that PINK1 phosphorylates Rab GTPases at Ser111, which inhibits LRRK2-mediated phosphorylation at Thr72, suggesting PINK1 activators could treat LRRK2-related Parkinson's.

bioRxiv · Sep 12, 2019Biochemistry