Author

H. Juergens

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· 1 Microbiology· 1 Pathology· 1 Physiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:yeast· 2 Assay:bulk RNA-seq· 1 Research Focus:cell type annotation· 1 Research Focus:differential expression· 1 Organism:human· 1 Research Focus:metabolism & bioenergetics· 1 Assay:metabolomics· 1

Frequent Co-Authors

R. Mans· 2 shared A. Godoy-Hernandez· 1 shared A. Kaljouw· 1 shared A. Marchetto· 1 shared A. Mielgo-Gomez· 1 shared A. Ranft· 1 shared A. Sastre· 1 shared A. Yeliseev· 1 shared

Activity by Year

2018-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 10 mutual co-author links

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2 shared papersPhysiology

R. Mans

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

ALiCE: A versatile, high yielding and scalable eukaryotic cell-free protein synthesis (CFPS) system

M. Das Gupta, Y. Flaskamp, R. Roentgen, H. Juergens, J. Armero Gimenez, F. Albrecht, J. Hemmerich, Z. Ahmad Arfi, J. Neuser, H. Spiegel, A. Yeliseev, L. Song, J. Qiu, C. Williams, R. Finnern

This paper introduces ALiCE, a scalable eukaryotic cell-free protein synthesis system capable of producing complex proteins at high yields and demonstrating functional activity and post-translational modifications.

bioRxiv · Nov 10, 2022 · PreprintBiochemistry

Re-oxidation of cytosolic NADH is a major contributor to the high oxygen requirements of the thermotolerant yeast Ogataea parapolymorpha in oxygen-limited cultures

W. J. Dekker, H. Juergens, R. A. Ortiz-Merino, C. Mooiman, R. van den Berg, A. Kaljouw, R. Mans, J. T. Pronk

This study identifies the high oxygen requirements of Ogataea parapolymorpha in oxygen-limited cultures as due to its inability to reoxidize NADH via glycerol formation, relying instead on aerobic respiration.

bioRxiv · Apr 30, 2021Physiology

Physiological relevance, localization and substrate specificity of the alternative (type II) mitochondrial NADH dehydrogenases of Ogataea parapolymorpha

H. Juergens, A. Mielgo-Gomez, A. Godoy-Hernandez, J. ter Horst, J. M. Nijenhuis, D. G. G. McMillan, R. Mans

This study investigates the physiological role, localization, and substrate specificity of alternative NADH dehydrogenases in Ogataea parapolymorpha, revealing metabolic redundancy and insights into respiratory chain function.

bioRxiv · Apr 28, 2021 · PreprintMicrobiology

SOX2 expression identifies Ewing sarcoma patients with high risk for tumor relapse and poor survival

G. Sannino, A. Marchetto, A. Ranft, S. Jabar, C. Zacherl, R. Alba-Rubio, S. Stein, F. S. Wehweck, M. M. Kiran, T. L. B. Hoelting, J. Musa, L. Romero-Perez, F. Cidre-Aranaz, M. M. L. Knott, J. Li, , T. G. P. Grunewald

bioRxiv · Dec 17, 2018Pathology