Janelle C. Leggere
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Janelle C. Leggere has a total of 21 co-authors. Here are the top co-authors by number of shared publications:
- Claire D. McWhite
Department of Molecular and Cellular Biology, University of Arizona, Tucson, AZ 85721, USA
4 shared publications David Yang
University of California, Berkeley, Center for Computational Biology, Berkeley, CA 94720, USA
4 shared publications- Edward M. Marcotte
Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA
4 shared publications - Muyoung Lee
Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA
4 shared publications - Ophelia Papoulas
Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA
4 shared publications - Rachael M. Cox
Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA
4 shared publications
Latest Publications
- Open Access
- 5 June 2026
- Published by Elsevier in Cell Reports
- Vol. 45 (6) , 117422
A cross-vertebrate brain protein interaction map identifies conserved neural and non-neural complexes
- 5 June 2026
- Published by Elsevier in Cell Reports
- Vol. 45 (6) , 117422
Open AccessA cross-vertebrate brain protein interaction map identifies conserved neural and non-neural complexes
- Open Access
- 27 May 2026
- Published by Elsevier in Cell Genomics
- Vol. 6 (6) , 101254
A protein interactome for the last eukaryotic common ancestor illuminates the biochemical basis of modern genetic diseases
- 27 May 2026
- Published by Elsevier in Cell Genomics
- Vol. 6 (6) , 101254
Open AccessA protein interactome for the last eukaryotic common ancestor illuminates the biochemical basis of modern genetic diseases
- Open Access
VerteBrain reveals novel neural and non-neural protein assemblies conserved across vertebrate evolution
Protein-protein interactions underlie core brain functions, including neurotransmitter release, receptor activation, and intracellular signaling essential for learning, memory, and cognition. Here, we systematically map conserved brain protein interactions across five vertebrate species–rabbit, chicken, dolphin, pig, and mouse–using co-fractionation and immunoprecipitation mass spectrometry. From 2,197 biochemical fractions, we identify over 81,000 high-confidence interactions among 6,108 conserved proteins. This interaction map (VerteBrain) reveals both regulatory and structural complexes, including extensive synaptonemal protein associations likely involved in inter-neuronal coordination. Conservation across species underscores essential roles in neuronal and glial function, as well as in additional tissues for more widely expressed complexes. The VerteBrain dataset uncovers candidate disease mechanisms, including roles for ARHGEF1 in short stature syndromes, synaptic vesicle trafficking complexes in epilepsy, and RELCH in congenital deafness. VerteBrain provides a publicly accessible framework for investigating brain protein interactions and their relevance to human neurological disorders.
Open AccessVerteBrain reveals novel neural and non-neural protein assemblies conserved across vertebrate evolution
Protein-protein interactions underlie core brain functions, including neurotransmitter release, receptor activation, and intracellular signaling essential for learning, memory, and cognition. Here, we systematically map conserved brain protein interactions across five vertebrate species–rabbit, chicken, dolphin, pig, and mouse–using co-fractionation and immunoprecipitation mass spectrometry. From 2,197 biochemical fractions, we identify over 81,000 high-confidence interactions among 6,108 conserved proteins. This interaction map (VerteBrain) reveals both regulatory and structural complexes, including extensive synaptonemal protein associations likely involved in inter-neuronal coordination. Conservation across species underscores essential roles in neuronal and glial function, as well as in additional tissues for more widely expressed complexes. The VerteBrain dataset uncovers candidate disease mechanisms, including roles for ARHGEF1 in short stature syndromes, synaptic vesicle trafficking complexes in epilepsy, and RELCH in congenital deafness. VerteBrain provides a publicly accessible framework for investigating brain protein interactions and their relevance to human neurological disorders.
- Open Access
A protein interactome for the last eukaryotic common ancestor illuminates the biochemical basis of modern genetic diseases
SUMMARY: All eukaryotes share a single-celled ancestor from ∼1.5–1.8 billion years ago, the Last Eukaryotic Common Ancestor (LECA). Roughly half of gene families found in modern eukaryotes were already present in LECA, forming molecular systems that continue to influence genetic diseases and traits today. To investigate these systems, we compared genes across 156 organisms to define a core set of protein-coding gene families likely present in LECA, with a quarter remaining uncharacterized. Integrating >26,000 mass spectrometry proteomics analyses from 31 species, we inferred higher-order complexes among these ancient proteins. This reconstructed interactome reveals both established and novel assemblies, offering a biochemical snapshot of LECA’s organization. Finally, by exploring these ancient protein interactions, we found new human gene-disease associations for bone density and congenital birth defects, illustrating the value of ancestral protein networks for modern functional genetics.
Open AccessA protein interactome for the last eukaryotic common ancestor illuminates the biochemical basis of modern genetic diseases
SUMMARY: All eukaryotes share a single-celled ancestor from ∼1.5–1.8 billion years ago, the Last Eukaryotic Common Ancestor (LECA). Roughly half of gene families found in modern eukaryotes were already present in LECA, forming molecular systems that continue to influence genetic diseases and traits today. To investigate these systems, we compared genes across 156 organisms to define a core set of protein-coding gene families likely present in LECA, with a quarter remaining uncharacterized. Integrating >26,000 mass spectrometry proteomics analyses from 31 species, we inferred higher-order complexes among these ancient proteins. This reconstructed interactome reveals both established and novel assemblies, offering a biochemical snapshot of LECA’s organization. Finally, by exploring these ancient protein interactions, we found new human gene-disease associations for bone density and congenital birth defects, illustrating the value of ancestral protein networks for modern functional genetics.