Author

N. M. Patel

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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Pharmacology & Toxicology· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 2 Organism:rat· 2 Organism:mouse· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Approach:statistical model· 1

Frequent Co-Authors

C. Thiemermann· 2 shared E. Aimaretti· 2 shared G. Ferreira Alves· 2 shared M. Collino· 2 shared S. M. Coldewey· 2 shared D. Collotta· 1 shared F. R. Oliveira· 1 shared H. Pillmann Ramos· 1 shared

Activity by Year

2021-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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2 shared papersPharmacology & Toxicology

C. Thiemermann

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Inhibition of the JAK/STAT pathway with baricitinib reduces the multiple organ dysfunction caused by hemorrhagic shock in rats

N. M. Patel, D. Collotta, E. Aimaretti, G. Ferreira Alves, S. Kröller, S. M. Coldewey, M. Collino, C. Thiemermann

This study shows that baricitinib reduces multiple organ dysfunction in hemorrhagic shock rats by inhibiting JAK/STAT, NF-κB, and NLRP3 pathways.

bioRxiv · Jan 13, 2022Pharmacology & Toxicology

Inhibition of Bruton's tyrosine kinase activity attenuates trauma-induced multiple organ dysfunction in rats

N. M. Patel, F. R. Oliveira, H. Pillmann Ramos, E. Aimaretti, G. Ferreira Alves, S. M. Coldewey, M. Collino, R. Sordi, C. Thiemermann

This study shows that BTK inhibitors reduce trauma-induced multiple organ dysfunction in rats by inhibiting BTK, NF-κB, and NLRP3 activation.

bioRxiv · Sep 23, 2021Pharmacology & Toxicology

The middle lipin (M-Lip) domain is a new dimeric protein fold that binds membranes

W. Gu, S. Gao, H. Wang, K. D. Fleming, R. M. Hoffmann, J. W. Yang, N. M. Patel, Y. M. Choi, J. E. Burke, K. Reue, M. V. Airola

The paper identifies the M-Lip domain as a novel dimeric protein fold that binds membranes and is essential for lipin function.

bioRxiv · Mar 19, 2021Biochemistry