Author

J. Nicolet

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Plant Biology· 4

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 4 Research Focus:cell signaling & trafficking· 2 Research Focus:cell type annotation· 2 Research Focus:development & morphogenesis· 2 Organism:plant (other)· 2 Assay:proteomics· 2 Organism:Arabidopsis· 1 Research Focus:metabolism & bioenergetics· 1

Frequent Co-Authors

M. Hothorn· 3 shared U. Hohmann· 2 shared A. Emonet· 1 shared A. Henschen· 1 shared A. Moretti· 1 shared A. Shukla· 1 shared C. Fuchs· 1 shared D. Couto· 1 shared

Activity by Year

2018-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersPlant Biology

M. Hothorn

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Inositol pyrophosphate catabolism by three families of phosphatases controls plant growth and development

F. Laurent, S. M. Bartsch, A. Shukla, F. E. Rico Resendiz, D. Couto, C. Fuchs, J. Nicolet, S. Loubery, H. J. Jessen, D. Fiedler, M. Hothorn

This study identifies three phosphatase families involved in inositol pyrophosphate catabolism in plants, showing their roles in growth, development, and nutrient signaling.

bioRxiv · Apr 30, 2024 · PreprintPlant Biology

Comparisons of two receptor pathways in a single cell-type reveal features of signalling specificity.

Y. Ma, I. Fluckiger, J. Nicolet, J. Pang, J. Dickinson, D. De Bellis, A. Emonet, S. Fujita, N. Geldner

The paper compares two receptor pathways in Arabidopsis root endodermis cells, showing distinct outputs despite similar MPK phosphorylation patterns, suggesting specificity through combinatorial activation and cross-pathway inhibition.

bioRxiv · Jul 3, 2023 · PreprintPlant Biology

Constitutive activation of leucine-rich repeat receptor kinase signaling pathways by BAK1-interacting receptor-like kinase 3 chimera

U. Hohmann, P. Ramakrishna, K. Wang, L. Lorenzo-Orts, J. Nicolet, A. Henschen, M. Barberon, M. Bayer, M. Hothorn

The paper reports that chimeric receptor proteins formed by fusing BIR3 LRR domains with SERK-dependent LRR-RK kinase domains activate signaling pathways constitutively, leading to gain-of-function phenotypes.

bioRxiv · Feb 18, 2020Plant Biology

Mechanistic analysis of the SERK3 elongated allele defines a role for BIR ectodomains in brassinosteroid signaling

U. Hohmann, J. Nicolet, A. Moretti, L. A. Hothorn, M. Hothorn

The paper investigates the role of the SERK3 elongated allele in brassinosteroid signaling, finding that it disrupts BIR ectodomain interactions with co-receptors rather than enhancing BRI1 binding.

bioRxiv · Jan 31, 2018Plant Biology