Author

L. Lorenzo-Orts

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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Research Focus:cell type annotation· 4 Approach:experimental assay· 4 Organism:plant (other)· 3 Assay:proteomics· 3 Research Focus:chromatin & epigenetic regulation· 2 Research Focus:protein folding & dynamics· 2 Organism:bacteria (other)· 1 Assay:cryo-EM· 1

Frequent Co-Authors

M. Hothorn· 3 shared J. Zhu· 2 shared U. Hohmann· 2 shared A. Henschen· 1 shared A. Meinhart· 1 shared A. Pauli· 1 shared A. Utz-Pugin· 1 shared C. Pribitzer· 1 shared

Activity by Year

2019-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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3 shared papersPlant Biology

M. Hothorn

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Author profile →

4 papers

Recent·Most cited

A molecular network of conserved factors keeps ribosomes dormant in the egg

K. F. Leesch, L. Lorenzo-Orts, C. Pribitzer, I. Grishkovskaya, M. Matzinger, E. Roitinger, K. Belacic, S. Kandolf, T.-Y. Lin, K. Mechtler, A. Meinhart, D. Haselbach, A. Pauli

The paper identifies conserved factors that maintain ribosome dormancy in zebrafish and Xenopus eggs and embryos, transitioning to an active state during early development.

bioRxiv · Nov 3, 2021Biochemistry

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

A genetically validated approach to detect inorganic polyphosphates in plants.

J. Zhu, S. Loubery, L. Broger, L. Lorenzo-Orts, A. Utz-Pugin, Y.-T. Chang, M. Hothorn

The paper develops a method to detect inorganic polyphosphates in plants using a dye and binding domain, finding that higher plants lack large polyP stores.

bioRxiv · May 8, 2019Plant Biology

Molecular characterization of CHAD domains as inorganic polyphosphate binding modules

L. Lorenzo-Orts, U. Hohmann, J. Zhu, M. Hothorn

This study identifies CHAD domains as specific inorganic polyphosphate binding modules across bacteria, archaea, and eukaryotes, revealing their structural and functional roles in polyP metabolism and localization.

bioRxiv · Mar 4, 2019Biochemistry