Author

T. Moran Luengo

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 Cell Biology· 1

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 3 Approach:experimental assay· 2 Assay:proteomics· 2 Research Focus:cell type annotation· 1 Organism:E. coli· 1 Organism:human· 1 Approach:mechanistic / dynamical model· 1 Assay:protein structure· 1

Frequent Co-Authors

M. P. Mayer· 2 shared S. G. D. Rudiger· 2 shared A. T. Hoekstra· 1 shared C. Bauer· 1 shared C. R. Berkers· 1 shared D. Picard· 1 shared D. Wider· 1 shared K. Bhattacharya· 1 shared

Activity by Year

2017-2019 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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2 shared papersBiochemistry

M. P. Mayer

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Author profile →

3 papers

Recent·Most cited

The Hsp70/Hsp90 Co-Chaperone Hop/Stip1 Shifts the Proteostatic Balance from Folding Towards Degradation

K. Bhattacharya, L. Weidenauer, T. Moran Luengo, P. C. Echeverria, L. Bernasconi, D. Wider, M. Villemin, C. Bauer, S. G. D. Rüdiger, M. Quadroni, D. Picard

This study shows that Hop/Stip1 regulates proteostasis by shifting the balance between protein folding and degradation in eukaryotes.

bioRxiv · Feb 27, 2019Cell Biology

Refolding activity of bacterial Hsp90 in vivo reveals ancient chaperoning function

T. Moran Luengo, T. Ahlnas, A. T. Hoekstra, C. R. Berkers, M. P. Mayer, S. G. D. Rudiger

This study shows that bacterial Hsp90 enhances protein refolding after heat stress but is not required for de novo folding, revealing its ancient role in the chaperone cascade.

bioRxiv · Nov 5, 2018 · PreprintBiochemistry

Breaking the Deadlock of Molecular Chaperones

T. Moran Luengo, R. Kityk, M. P. Mayer, S. G. D. Rudiger

This paper proposes a mechanism where Hsp70 and Hsp90 chaperones facilitate protein folding by creating a hydrophobicity gradient, allowing productive folding to occur.

bioRxiv · Aug 16, 2017Biochemistry