Author

W. Blankenfeldt

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· 8 Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 9 Organism:bacteria (other)· 7 Research Focus:protein folding & dynamics· 4 Assay:protein structure· 4 Research Focus:protein structure prediction· 4 Organism:C. elegans· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

T. Kluenemann· 6 shared A. Flieger· 2 shared A. Schallmey· 2 shared A. Steffen· 2 shared C. Lang· 2 shared J. A. Rodriguez Buitrago· 2 shared M. Diwo· 2 shared T. Stradal· 2 shared

Activity by Year

2019-2023 · peak 7/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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6 shared papersBiochemistry

T. Kluenemann

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10 papers

Recent·Most cited

Formation of the pyruvoyl-dependent proline reductase Prd from Clostridioides difficile requires the maturation enzyme PrdH

C. Behlendorf, M. G. Diwo, M. Neumann-Schaal, M. Fuchs, F. Faber, W. Blankenfeldt

This paper identifies PrdH as the maturation enzyme required for the formation of the pyruvoyl group in the proline reductase Prd of C. difficile, essential for proline utilization and toxin production.

bioRxiv · Dec 15, 2023 · PreprintBiochemistry

Structure-function relationships underpin disulfide loop cleavage-dependent activation of Legionella pneumophila lysophosholipase A PlaA

M. Hiller, M. Diwo, S. Wamp, T. Gutsmann, C. Lang, W. Blankenfeldt, A. Flieger

This study reveals the structural basis for the regulated activation and substrate preference of PlaA, a lysophospholipase in Legionella pneumophila, showing how disulfide loop cleavage enhances catalytic activity and substrate specificity.

bioRxiv · Mar 24, 2023 · PreprintBiochemistry

NAD(H)-mediated tetramerization controls the activity of Legionella pneumophila phospholipase PlaB

M. Diwo, W. Michel, P. Aurass, K. Kuhle-Keindorf, J. Pippel, J. Krausze, C. Lang, W. Blankenfeldt, A. Flieger

This study identifies an NAD(H)-mediated tetramerization mechanism that regulates the activity and localization of the Legionella pneumophila phospholipase PlaB.

bioRxiv · Sep 1, 2020Microbiology

Crystal structure of full-length cytotoxic necrotizing factor CNFY reveals molecular building blocks for intoxication

P. Chaoprasid, P. Lukat, S. Mühlen, T. V. Heidler, E. M. Gazdag, S. Dong, W. Bi, C. Rueter, M. Kirchenwitz, A. Steffen, L. Jansch, T. Stradal, P. Dersch, W. Blankenfeldt

The paper determines the crystal structure of CNFY, revealing domains involved in toxin translocation and identifying its potential as a drug delivery tool.

bioRxiv · Apr 7, 2020Biochemistry

Expression, purification and crystal structure determination of a ferredoxin reductase from the actinobacterium Thermobifida fusca

J. A. Rodriguez Buitrago, T. Kluenemann, W. Blankenfeldt, A. Schallmey

The paper describes the expression, purification, and crystal structure determination of FdR9 from Thermobifida fusca, revealing its structural features and cofactor binding preferences.

bioRxiv · Mar 12, 2020Biochemistry

CYP154C5 regioselectivity in steroid hydroxylation explored by substrate and protein engineering

P. Bracco, H. J. Wijma, B. Nicolai, J. A. Rodriguez Buitrago, T. Kluenemann, A. Vila, P. Schrepfer, W. Blankenfeldt, D. B. Janssen, A. Schallmey

The paper explores how altering CYP154C5's regioselectivity in steroid hydroxylation can be achieved through protein and substrate engineering, revealing structural and dynamic changes in the active site.

bioRxiv · Mar 4, 2020Biochemistry

The crystal structure of heme d1 biosynthesis-associated small c-type cytochrome NirC reveals mixed oligomeric states in crystallo

T. Kluenemann, S. Henke, W. Blankenfeldt

The paper determines the crystal structure of NirC, revealing monomers and 3D-domain-swapped dimers in the same asymmetric unit.

bioRxiv · Feb 21, 2020Biochemistry

Structure of heme d1-free cd1 nitrite reductase NirS

T. Kluenemann, W. Blankenfeldt

The paper determines the crystal structure of heme d1-free cd1 nitrite reductase NirS from Pseudomonas aeruginosa, revealing an open conformation and potential link to flagella formation.

bioRxiv · Feb 12, 2020 · PreprintBiochemistry

Crystal structure of NirF: Insights into its role in heme d1 biosynthesis

T. Kluenemann, M. Nimtz, L. Jaensch, G. Layer, W. Blankenfeldt

The paper determines the crystal structure of NirF and its complex with dihydroheme d1, revealing its potential enzymatic role in heme d1 biosynthesis beyond mere binding.

bioRxiv · Jan 13, 2020Biochemistry

RhoG and Cdc42 can contribute to Rac-dependent lamellipodia formation through WAVE Regulatory Complex-binding

M. Schaks, H. Doering, F. Kage, A. Steffen, T. Kluenemann, W. Blankenfeldt, T. Stradal, K. Rottner

This study shows RhoG and Cdc42 can drive lamellipodia formation independently of Rac by directly interacting with the WAVE Regulatory Complex.

bioRxiv · Apr 9, 2019Cell Biology