Author

M. A. Fierro

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· 5 Cell Biology· 3

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 7 Organism:plant (other)· 5 Research Focus:cell type annotation· 4 Research Focus:host-pathogen & immune response· 4 Research Focus:cell signaling & trafficking· 2 Research Focus:development & morphogenesis· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2

Frequent Co-Authors

V. Muralidharan· 5 shared A. Florentin· 3 shared D. W. Cobb· 3 shared J. R. Beck· 3 shared T. Hussain· 2 shared A. Muheljic· 1 shared A. Villegas· 1 shared B. Asady· 1 shared

Activity by Year

2017-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 14 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

5 shared papersCell Biology

V. Muralidharan

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

Plasmodium RON11 triggers biogenesis of the merozoite rhoptry pair and is essential for erythrocyte invasion

D. Anaguano, O. Adewale Fasoro, G. S. Vick, J. A. Blauwkamp, S. Yanik, M. A. Fierro, S. Absalon, P. SRINIVASAN, V. Muralidharan

This study shows that RON11 is essential for the biogenesis of the second rhoptry in Plasmodium falciparum merozoites and is required for erythrocyte invasion.

bioRxiv · Jan 29, 2024Cell Biology

PEXEL is a proteolytic maturation site for both exported and non-exported Plasmodium proteins

M. A. Fierro, A. Muheljic, J. Sha, J. A. Wohlschlegel, J. R. Beck

The paper shows that non-exported Plasmodium proteins also contain PEXEL motifs that are processed by PMV, but specific residues in the mature N-terminus determine export.

bioRxiv · Jul 12, 2023 · PreprintMicrobiology

Knock-sideways by inducible ER retrieval enables anovel approach for studying Plasmodium secreted proteins

M. A. Fierro, T. Hussain, L. J. Campin, J. R. Beck

The paper introduces knockER, a method to conditionally sequester Plasmodium secreted proteins in the ER, enabling loss-of-function studies and sub-compartmental resolution of protein function.

bioRxiv · Oct 2, 2022 · PreprintMicrobiology

The PTEX pore component EXP2 is important for intrahepatic development during the Plasmodium liver stage

T. Hussain, J. Linera-Gonzalez, J. M. Beck, M. A. Fierro, G. R. Mair, R. C. Smith, J. R. Beck

This study uses a ribozyme-based approach to show EXP2 is essential for Plasmodium liver stage development, highlighting its role in the PTEX translocon at the hepatocyte-parasite interface.

bioRxiv · Oct 2, 2022Microbiology

An ER CREC family protein regulates the egress proteolytic cascade in malaria parasites

M. A. Fierro, B. Asady, C. F. Brooks, A. Villegas, S. N. J. Moreno, V. Muralidharan

This study identifies PfERC, an ER-resident CREC family protein, as essential for the proteolytic cascade regulating egress in malaria parasites.

bioRxiv · Jul 31, 2019 · PreprintCell Biology

The ER chaperone PfGRP170 is essential for asexual development and is linked to stress response in malaria parasites.

H. M. Kudyba, D. W. Cobb, M. A. Fierro, A. Florentin, D. Ljolje, B. Singh, N. W. Lucchi, V. Muralidharan

This study identifies PfGRP170 as an essential ER chaperone in Plasmodium falciparum, critical for asexual development and stress response.

bioRxiv · Apr 17, 2019Cell Biology

The exported chaperone PfHsp70x is dispensable for the Plasmodium falciparum intraerythrocytic lifecycle

D. W. Cobb, A. Florentin, M. A. Fierro, M. Krakowiak, J. M. Moore, V. Muralidharan

This study shows that PfHsp70x, the sole exported Hsp70 in P. falciparum, is not essential for parasite growth or protein export during the intraerythrocytic lifecycle.

bioRxiv · Aug 11, 2017Microbiology

PfClpC Is An Essential Clp Chaperone Required For Plastid Integrity And Clp Protease Stability In Plasmodium falciparum

A. Florentin, D. W. Cobb, J. D. Fishburn, M. J. Cipriano, P. S. Kim, M. A. Fierro, B. Striepen, V. Muralidharan

This paper identifies PfClpC as an essential apicoplast-targeted chaperone in Plasmodium falciparum, showing its role in maintaining apicoplast integrity and parasite viability.

bioRxiv · Jun 20, 2017Microbiology