Publications

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Hiefinger* C., Mandl* S., Wieland* M., Kneuttinger A.
(2023)?In?Methods in Enzymology: Integrated Methods in Protein Biochemistry: PartC?edited by A. K. Shukla, 247-288?
Chapter Eight?-?Rational design, production and in vitro analysis of photoxenoproteins

Kneuttinger A.C., Sterner R.
(2021)?Biochemistry 60,?3422–3423
The Structure of Carbamoylphosphate Synthetase Unravels Central
Functional Features of a Key Metabolic Multienzyme Complex.

Wurm J.P., Sung S., Kneuttinger A.C., Hupfeld E., Sterner E., Wilmanns M., Sprangers R.
(2021) Nat. Commun.?12, 2748
Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex.

Simeth* N.A., Kinateder* T., Rajendran C., Nazet J., Merkl R., Sterner R., K?nig B., Kneuttinger A.C.
(2021) Chem. - Eur. J. 27, 2439–2451
Towards Photochromic Azobenzene-Based Inhibitors for Tryptophan Synthase.

Kneuttinger A.C., Rajendran C., Simeth N.A., Bruckmann A., K?nig B., Sterner R.?
(2020) Biochemistry 59, 2729–2742
Significance of the protein interface configuration for allostery in imidazole glycerol phosphate synthase.

Kneuttinger A.C., Zwisele S., Straub K., Bruckmann A., Busch F., Kinateder T., Gaim B., Wysocki VH., Merkl R., Sterner R.?
(2019) Int. J. Mol. Sci. 20, E5106
Light-regulation of tryptophan synthase by combining protein design and enzymology.

Kneuttinger A.C., Straub K., Bittner P., Simeth N.A., Bruckmann A., Busch F., Rajendran C., Hupfeld E., Wysocki V.H., Horinek D., K?nig B., Merkl R., Sterner R.?
(2019) Cell Chem. Biol. 26, 1501–1514
Light regulation of enzyme allostery through photo-responsive unnatural amino acids.

Highlighted in:?
Courtney, T.M., Deiters, A.?
(2019) Cell Chem. Biol. 26, 1481–1483

Kneuttinger A.C., Winter M., Simeth N.A., Heyn K., Merkl R., K?nig B., Sterner R.
(2018) Chembiochem 19, 1750–1757
Artificial light regulation of an allosteric bienzyme complex by a photosensitive ligand.

Simeth N.A., Kneuttinger A.C., Sterner R., K?nig B.?
(2017)
Chem. Sci. 8, 6474–6483
Photochromic coenzyme Q derivatives: switching redox potentials with light.

Heidinger L., Kneuttinger A.C., Kashiwazaki G., Weber S., Carell T., Schleicher E.?
(2016) FEBS Lett. 590, 4489–4494
Direct observation of a deoxyadenosyl radical in an active enzyme environment.

Kneuttinger A.C., Kashiwazaki G., Prill S., Heil K., Müller M., Carell T.?
(2014) Photochem. Photobiol. 90, 1–14
Formation and direct repair of UV-induced dimeric DNA pyrimidine lesions.

Kneuttinger A.C., Heil K., Kashiwazaki G., Carell T.?
(2013) Chem. Commun. 25, 722–724
The radical SAM enzyme spore photoproduct lyase employs a tyrosyl radical for DNA repair.

Brandmayr C., Wagner M., Brückl T., Globisch D., Pearson D., Kneuttinger A.C., Reiter V., Hienzsch A., Koch S., Thoma I., Thumbs P., Michalakis S., Müller M., Biel M., Carell T.?
(2012) Angew. Chem. Int. Ed. 51, 11162–11165
Isotope-based analysis of modified tRNA nucleosides correlates modification density with translational efficiency.

Reiter V., Matschkal D.M., Wagner M., Globisch D., Kneuttinger A.C., Müller M., Carell T.?
(2012) Nucleic Acids Res. 40, 6235–6240
The CDK5 repressor CDK5RAP1 is a methylthiotransferase acting on nuclear and mitochondrial RNA.

Globisch D., Pearson D., Hienzsch A., Brückl T., Wagner M., Thoma I., Thumbs P., Reiter V., Kneuttinger A.C., Müller M., Siber S.A., Carell T.?
(2011) Angew. Chem. Int. Ed. 50, 9739–9742
Systems-based analysis of modified tRNA bases.

Heil, K., Kneuttinger, A.C., Schneider, S., Lischke, U., Carell, T.?
(2011) Chem. - Eur. J. 17, 9651–9657
Crystal structures and repair studies reveal the identity and the base-pairing properties of the UV-induced spore photoproduct DNA lesion.