Author

R. S. Nirujogi

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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Biochemistry· 5 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Assay:proteomics· 6 Research Focus:cell signaling & trafficking· 4 Organism:human· 4 Research Focus:drug response / drug discovery· 2 Research Focus:cell type annotation· 1 Research Focus:clustering· 1 Research Focus:differential expression· 1

Frequent Co-Authors

D. R. Alessi· 5 shared A. Karapetsas· 3 shared M. Wightman· 3 shared R. Gourlay· 3 shared A. R. Prescott· 2 shared A. U. Malik· 2 shared F. Tonelli· 2 shared M. Dorward· 2 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 39 mutual co-author links

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5 shared papersBiochemistry

D. R. Alessi

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Author profile →

6 papers

Recent·Most cited

Golgi-IP, a novel tool for multimodal analysis of Golgi molecular content

R. Fasimoye, W. Dong, R. S. Nirujogi, E. S. Rawat, M. Iguchi, K. Nyame, T. K. Phung, E. Bagnoli, A. R. Prescott, D. R. Alessi, M. Abu-remaileh

This paper introduces Golgi-IP, a method to isolate and analyze the human Golgi's proteome, metabolome, and lipidome, revealing novel components and metabolic features.

bioRxiv · Nov 22, 2022Cell Biology

PKC isoforms activate LRRK1 kinase by phosphorylating conserved residues (Ser1064, Ser1074 and Thr1075) within the CORB GTPase domain

A. U. Malik, A. Karapetsas, R. S. Nirujogi, D. Chatterjee, T. K. Phung, M. Wightman, R. Gourlay, N. Morrice, S. Mathea, S. Knapp, D. R. Alessi

This study identifies that PKC isoforms activate LRRK1 by phosphorylating specific residues in the CORB GTPase domain, enhancing kinase activity.

bioRxiv · Jun 9, 2022Biochemistry

Characterization of protease activity of Nsp3 from SARS-CoV-2 and its in vitro inhibition by nanobodies

L. Armstrong, S. M. Lange, V. de Cesare, S. P. Matthews, R. S. Nirujogi, I. Cole, A. Hope, F. Cunningham, R. Toth, R. Mukherjee, D. Bojkova, F. Gruber, D. Gray, P. G. Wyatt, J. Cinatl, , Y. Kulathu

This study characterizes Nsp3 protease activity from SARS-CoV-2 and identifies nanobodies that inhibit PLpro with nanomolar affinity.

bioRxiv · Dec 9, 2020Biochemistry

Deciphering the LRRK code: LRRK1 and LRRK2 phosphorylate distinct Rab proteins and are regulated by diverse mechanisms

A. U. Malik, A. Karapetsas, R. S. Nirujogi, S. Mathea, P. Pal, P. Lis, M. Taylor, E. Purlyte, R. Gourlay, M. Dorward, S. Weidlich, R. Toth, N. K. Polinski, S. Knapp, F. Tonelli, D. R. Alessi

This study identifies distinct Rab proteins phosphorylated by LRRK1 and LRRK2, showing they are regulated by different mechanisms and respond differently to inhibitors.

bioRxiv · Nov 25, 2020Biochemistry

Phosphoproteomics reveals that the hVPS34 regulated SGK3 kinase specifically phosphorylates endosomal proteins including Syntaxin-7, Syntaxin-12, RFIP4 and WDR44

N. Malik, R. S. Nirujogi, J. Peltier, T. Macartney, M. Wightman, A. R. Prescott, R. Gourlay, M. Trost, D. R. Alessi, A. Karapetsas

This study identifies novel SGK3 substrates, including endosomal proteins, through phosphoproteomic screens and shows SGK3 specifically phosphorylates these proteins at sites distinct from Akt.

bioRxiv · Aug 20, 2019Biochemistry

PPM1H phosphatase counteracts LRRK2 signaling by selectively dephosphorylating Rab proteins

K. Berndsen, P. Lis, W. Yeshaw, P. S. Wawro, R. S. Nirujogi, M. Wightman, T. Macartney, M. Dorward, A. Knebel, F. Tonelli, S. R. Pfeffer, D. R. Alessi

This study identifies PPM1H as a phosphatase that counteracts LRRK2 signaling by dephosphorylating Rab proteins, suggesting it as a potential therapeutic target for Parkinson's disease.

bioRxiv · Jul 22, 2019Biochemistry