Author

D. Kornitzer

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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Microbiology· 3 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:C. elegans· 3 Research Focus:cell signaling & trafficking· 3 Research Focus:cell type annotation· 2 Research Focus:host-pathogen & immune response· 2 Assay:proteomics· 2 Research Focus:chromatin & epigenetic regulation· 1 Organism:human· 1

Frequent Co-Authors

M. Pinsky· 3 shared Z. Weissman· 3 shared A. R. Reddi· 1 shared A. Sinha· 1 shared A. Thakur· 1 shared B. E. Lemma· 1 shared D. Fushman· 1 shared E. Pick· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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3 shared papersMicrobiology

M. Pinsky

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Regulation of heme utilization and homeostasis in Candida albicans

N. Andrawes, Z. Weissman, M. Pinsky, S. Moshe, J. Berman, D. Kornitzer

This study identifies Huf1 as a heme-responsive transcription factor in C. albicans that regulates both heme homeostasis and uptake from the environment.

bioRxiv · Jun 22, 2022Microbiology

Ferric reductase-related proteins mediate fungal heme acquisition

U. Roy, S. Yaish, Z. Weissman, M. Pinsky, S. Dey, G. Horev, D. Kornitzer

The paper identifies Frp1 and Frp2 as proteins required for heme utilization in Candida albicans and shows they form a functional complex with CFEM hemophores for extracellular heme uptake.

bioRxiv · May 25, 2022Microbiology

Using genetically encoded heme sensors to probe the mechanisms of heme uptake and homeostasis in Candida albicans

Z. Weissman, M. Pinsky, R. K. Donegan, A. R. Reddi, D. Kornitzer

This study uses genetically encoded heme sensors to show that C. albicans takes up heme from hemoglobin and hemin via different pathways and uses Hmx1 to prevent heme toxicity.

bioRxiv · Jul 26, 2020Microbiology

Rub1/NEDD8, a ubiquitin-like modifier, is also a ubiquitin modifier

S. Zerath Gurevich, A. Sinha, J. Longworth, R. K. Singh, B. E. Lemma, A. Thakur, O. Popp, D. Kornitzer, N. Reis, M. Scheffner, G. Dittmar, E. Pick, D. Fushman, M. H. Glickman

This paper shows that a single amino acid swap at position 72 can switch the substrate specificity of Rub1/NEDD8 and ubiquitin, revealing their distinct roles in cellular modification pathways.

bioRxiv · Jun 18, 2020 · PreprintBiochemistry