Author

D. Januliene

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· 3 Biophysics· 2 Physiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Assay:cryo-EM· 4 Research Focus:protein structure prediction· 3 Organism:yeast· 3 Research Focus:host-pathogen & immune response· 2 Research Focus:protein folding & dynamics· 2 Research Focus:cell signaling & trafficking· 1 Organism:human· 1

Frequent Co-Authors

A. Moeller· 5 shared B. M. Esch· 3 shared K. Parey· 3 shared S. Walter· 3 shared C. Körner· 2 shared F. Fröhlich· 2 shared J.-H. Schäfer· 2 shared A. M. P. Gjessing· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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5 shared papersBiochemistry

A. Moeller

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Author profile →

6 papers

Recent·Most cited

The structure of the Orm2-containing serine palmitoyltransferase complex reveals distinct inhibitory potentials of yeast Orm proteins.

C. Körner, J.-H. Schäfer, B. M. Esch, K. Parey, S. Walter, D. Teis, D. Januliene, O. Schmidt, A. Moeller, F. Fröhlich

The paper determines the cryo-EM structure of the SPT-Orm2 complex and shows Orm2 has higher inhibitory potential than Orm1, despite similar structures.

bioRxiv · Jan 30, 2024Biochemistry

Structure of the yeast ceramide synthase

J.-H. Schäfer, L. Clausmeyer, C. Körner, B. M. Esch, V. N. Wolf, S. Walter, D. Januliene, A. Moeller, F. Fröhlich

This study determines the structure of the yeast ceramide synthase complex using cryo-EM, revealing its active state and inhibition mechanism by fumonisin B1.

bioRxiv · Oct 24, 2023Biochemistry

Structure of the ceramide-bound SPOTS complex

J.-H. Schafer, C. Korner, B. M. Esch, S. Limar, K. Parey, S. Walter, D. Januliene, A. Moeller, F. Frohlich

The paper reports cryo-EM structures of the yeast SPT complex with Tsc3, Orm1, and Sac1, revealing ceramide-dependent inhibition and co-regulation of sphingolipid and sterol metabolism.

bioRxiv · Feb 3, 2023Biochemistry

Structure of the lysosomal membrane fusion machinery

D. Shvarev, J. Schoppe, C. Koenig, A. Perz, N. Fuellbrunn, S. Kiontke, L. Langemeyer, D. Januliene, K. Schnelle, D. Kuemmel, F. Froehlich, A. Moeller, C. Ungermann

This study determines the structure of HOPS, a lysosomal fusion machinery, revealing its rigid architecture and how it couples membrane tethering with SNARE assembly to facilitate fusion.

bioRxiv · May 5, 2022 · PreprintBiophysics

Tracing the substrate translocation mechanism in P-glycoprotein

T. Gewering, D. Waghray, K. Parey, H. Jung, N. N. B. Tran, J. Zapata, P. Zhao, H. Chen, D. Januliene, G. Hummer, I. L. Urbatsch, A. Moeller, Q. Zhang

This study reveals the substrate translocation mechanism in P-glycoprotein by determining cryoEM structures and using molecular dynamics simulations to identify conformational changes in TM1 that regulate transport.

bioRxiv · Apr 28, 2022 · PreprintBiophysics

Soluble SorCS1 binds the insulin receptor to enhance insulin sensitivity.

M. Kjolby, P. Breining, K. M. Pedersen, N. Wellner, K. M. J. Sorensen, A. M. P. Gjessing, D. Januliene, D. M. Vittrup, A. Manavalan, M. Rotman, G. Thotakura, G. Hermey, P. Madsen, C. B. Vaegter, S. Thirup, , A. Nykjaer

This study identifies sol-SorCS1 as a soluble form of SorCS1 that enhances insulin sensitivity by binding the insulin receptor, improving glucose uptake and signaling in myocytes.

bioRxiv · Nov 10, 2020 · PreprintPhysiology