Author

R. Dias Teixeira

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· 1 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Assay:structural biology· 2 Research Focus:cancer & tumor microenvironment· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1 Approach:statistical model· 1

Frequent Co-Authors

A. Grahl· 1 shared A. Klotz· 1 shared D. Spiess· 1 shared F. Holzschuh· 1 shared G. Mas· 1 shared I. Santi· 1 shared L. A. Abiko· 1 shared N. Zamboni· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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1 shared paperBiophysics

A. Grahl

Mutual co-authors in cluster

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3 papers

Recent·Most cited

MicrobiologybioRxivPreprintSep 28, 2023

Toxin-mediated depletion of nicotinamide dinucleotides drives persister formation in a human pathogen

I. Santi, R. Dias Teixeira, P. Manfredi…·U. Jenal

This study shows that the RES domain TA system in P. aeruginosa promotes persister formation by depleting NAD and NADP under nutrient stress, enhancing bacterial survival during antibiotic treatment.

DOI 10.1101/2023.09.28.559889

humanproteomics

𝕏 PostBluesky

BiophysicsbioRxivAug 30, 2021

Filling of a water-free void explains the allosteric regulation of the β1-adrenergic receptor by cholesterol

L. A. Abiko, R. Dias Teixeira, S. Engilberge…·S. Grzesiek

The paper identifies dry voids in the β1-adrenergic receptor that cholesterol fills, explaining its allosteric regulation and suggesting new drug development strategies.

DOI 10.1038/s41557-022-01009-9

humanstructural biology

𝕏 PostBluesky

BiochemistrybioRxivAug 28, 2020

Activation mechanism of a small prototypic Rec-GGDEF diguanylate cyclase

R. Dias Teixeira, F. Holzschuh, T. Schirmer

The paper investigates the activation mechanism of a Rec-GGDEF diguanylate cyclase by showing how phosphorylation induces structural changes leading to catalytic activation.

DOI 10.1038/s41467-021-22492-7

structural biologyexperimental assay

𝕏 PostBluesky