Author

L. K. Read

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· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:bulk RNA-seq· 2 Research Focus:cell type annotation· 2 Organism:human· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:differential expression· 1 Research Focus:gene regulatory network inference· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

M. Ciganda· 2 shared A. Mishra· 1 shared A. P. Dubey· 1 shared A. Raczkowski· 1 shared D. I. McSkimming· 1 shared E. Hegedusova· 1 shared E. W. Debler· 1 shared H. Hashimoto· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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2 shared papersMicrobiology

M. Ciganda

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Translational control by Trypanosoma brucei DRBD18 contributes to the maintenance of the procyclic state

M. Ciganda, J. Sotelo-Silveira, J. T. Smith, S. Shen, J. Qu, P. Smircich, L. K. Read

This study shows that DRBD18 in Trypanosoma brucei regulates translational efficiency of specific transcripts, maintaining the procyclic form by repressing procyclic-specific proteins and enhancing bloodstream/metacyclic-specific proteins.

bioRxiv · Feb 8, 2023Microbiology

Selective nuclear export of mRNAs is promoted by DRBD18 in Trypanosoma brucei

A. Mishra, J. N. Kaur, D. I. McSkimming, E. Hegedusova, A. P. Dubey, M. Ciganda, Z. Paris, L. K. Read

This study identifies DRBD18 as a regulator of selective mRNA nuclear export in Trypanosoma brucei by promoting mRNP mobilization through the nuclear pore complex.

bioRxiv · Jun 14, 2021Microbiology

Structural Basis of Protein Arginine Methyltransferase Activation by a Catalytically Dead Homolog (Prozyme)

H. Hashimoto, L. Kafkova, A. Raczkowski, K. D. Jordan, L. K. Read, E. W. Debler

This paper reports the crystal structure of a Trypanosoma brucei PRMT1 enzyme-prozyme heterotetramer, revealing how the prozyme stabilizes the enzyme and enables catalysis through structural and functional interactions.

Journal of Molecular Biology · Jan 1, 2020Peer-reviewedBiochemistry