Author

H. A. Lorenzi

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· 2 Immunology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 3 Research Focus:cell signaling & trafficking· 2 Organism:human· 2 Research Focus:cell type annotation· 1 Research Focus:drug response / drug discovery· 1 Assay:proteomics· 1

Frequent Co-Authors

A. Ferrel· 1 shared A. Naor· 1 shared A. Shamsaddini· 1 shared E. Tenborg· 1 shared E. Yeh· 1 shared F. A. Otaizo-Carrasquero· 1 shared F. Parween· 1 shared H. H. Zhang· 1 shared

Activity by Year

2017-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 13 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

1 shared paperMicrobiology

A. Ferrel

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Chemokine positioning determines mutually exclusive roles for their receptors in extravasation of pathogenic human T cells

F. Parween, S. P. Singh, H. H. Zhang, N. Kathuria, F. A. Otaizo-Carrasquero, A. Shamsaddini, P. J. Gardina, S. Ganesan, J. Kabat, H. A. Lorenzi, T. G. Myers, J. M. Farber

This study identifies that chemokine receptors on pathogenic human T cells have mutually exclusive roles in extravasation, with CCR6 mediating arrest and CCR2 enabling transendothelial migration through distinct ligand interactions.

bioRxiv · Jan 25, 2023 · PreprintImmunology

Translocation of dense granule effectors across the parasitophorous vacuole membrane in Toxoplasma-infected cells requires the activity of ROP17, a rhoptry protein kinase.

M. W. Panas, A. Ferrel, A. Naor, E. Tenborg, H. A. Lorenzi, J. C. Boothroyd

bioRxiv · Apr 18, 2019Microbiology

Small molecule inhibition of apicomplexan FtsH1 disrupts plastid biogenesis in human pathogens

K. Amberg-Johnson, S. B. Hari, S. M. Ganesan, H. A. Lorenzi, R. T. Sauer, J. C. Niles, E. Yeh

The paper identifies FtsH1 as a novel druggable target for antimalarial drugs by showing that its inhibition disrupts apicoplast biogenesis in Plasmodium falciparum and Toxoplasma gondii.

bioRxiv · Aug 19, 2017Microbiology