Abstract 2333 Molecular structure, cell localization, and evolutionary relationships of a novel family of putative lipases in Tetrahymena thermophila

Lipid droplets (LDs) are important and dynamic organelles in all cells. Proteomic studies have shown that LDs are decorated with up to hundreds of different proteins that modulate LD formation, function, and interaction with other organelles. Like other organisms, work in our lab has shown that the freshwater ciliate Tetrahymena thermophila increases LD formation during nutrient challenges such as starvation. To better understand the formation and function of Tetrahymena LDs during starvation, we performed a proteomic screen to identify LD-associated proteins.

Authors

Institutions

Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109428
Primary Topic
Protist diversity and phylogeny
Type
article
Field-Weighted Citation Impact
0.00

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Abstract 2333 Molecular structure, cell localization, and evolutionary relationships of a novel family of putative lipases in Tetrahymena thermophila

Sarah Tangen, Kim Kandl, Laura Listenberger, Jean Porterfield et al.
Journal of Biological Chemistry
Protist diversity and phylogeny
article

Abstract 2333 Molecular structure, cell localization, and evolutionary relationships of a novel family of putative lipases in Tetrahymena thermophila

Sarah Tangen, Kim Kandl, Laura Listenberger, Jean Porterfield, Austin B. Williams, Ella Wiggenhorn, Vera Sablak, Ian Knowles
article en

Abstract

Lipid droplets (LDs) are important and dynamic organelles in all cells. Proteomic studies have shown that LDs are decorated with up to hundreds of different proteins that modulate LD formation, function, and interaction with other organelles. Like other organisms, work in our lab has shown that the freshwater ciliate Tetrahymena thermophila increases LD formation during nutrient challenges such as starvation. To better understand the formation and function of Tetrahymena LDs during starvation, we performed a proteomic screen to identify LD-associated proteins.

Journal of Biological ChemistryVol. 301(5)
St. Olaf College (US)
Rutgers, The State University of New Jersey, National Institutes of Health
Zero hunger
Openalex Percentile: Top 88%
Protist diversity and phylogeny
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.