Author

I. M. Cristea

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Microbiology· 3

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Organism:human· 2 Organism:bacteria (other)· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:electronic health records· 1 Research Focus:host-pathogen & immune response· 1 Assay:proteomics· 1

Frequent Co-Authors

T. M. Greco· 2 shared A. Binz· 1 shared A. Hickford Martinez· 1 shared A. Pichlmair· 1 shared A. Piras· 1 shared A. Pohlmann· 1 shared A. Ramos Nascimento· 1 shared A. W. Kulczyk· 1 shared

Activity by Year

2022-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersMicrobiology

T. M. Greco

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

YlaN is an iron(II) binding protein that functions to relieve Fur-mediated repression of gene expression in Staphylococcus aureus

J. M. Boyd, K. M. esquilin-lebron, C. J. Campbell, K. M. Ryan Kaler, J. Norambuena, M. E. Foley, T. G. Stephens, G. Rios, G. Mereddy, V. Zheng, H. Bovermann, J. Kim, A. W. Kulczyk, J. H. Yang, T. M. Greco, , T. L. Stemmler

This study identifies YlaN as an Fe(II) binding protein in S. aureus that relieves Fur-mediated repression of gene expression during Fe deprivation.

bioRxiv · Oct 3, 2023 · PreprintMicrobiology

The Protein Interaction Networks of Catalytically-Active and Catalytically-Inactive PqsE in Pseudomonas aeruginosa

I. Taylor, L. A. Murray-Nerger, I. M. Cristea, B. Bassler

This paper identifies protein interactions of catalytically-active and inactive PqsE variants in P. aeruginosa, showing that catalytic activity influences specific interactions and that RhlR may compete with other proteins for PqsE binding.

bioRxiv · May 31, 2022Microbiology

The interferon-inducible GTPase MxB promotes capsid disassembly and genome release of herpesviruses

B. Sodeik, M. C. Serrero, V. Girault, S. Weigang, T. M. Greco, A. Ramos Nascimento, F. Anderson, A. Piras, A. Hickford Martinez, J. Hertzog, A. Binz, A. Pohlmann, U. Prank, J. Rehwinkel, R. Bauerfeind, , G. Kochs

This study identifies MxB as an interferon-inducible GTPase that disassembles herpesvirus capsids, promoting genome release and enhancing innate immune responses.

bioRxiv · Jan 25, 2022Microbiology