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Chemistry

D-Index
42
Citations
6984
World Ranking
17487
National Ranking
1268

Overview

Wulf Blankenfeldt is affiliated with Technische Universität Braunschweig in Germany. Their research spans several areas within biochemistry, genetics, and molecular biology, with notable contributions also in medicine.

Their main fields of study include biochemistry, genetics, and molecular biology, with a focus on subfields such as molecular biology, materials chemistry, pharmacology, immunology, and genetics.

Main topics explored by Blankenfeldt encompass bacterial biofilms and quorum sensing, enzyme structure and function, antibiotic resistance in bacteria, microbial natural products and biosynthesis, bacterial genetics and biotechnology, research on Legionella and Acanthamoeba, and photosynthetic processes and mechanisms.

They have authored numerous papers, among which are:

  • Citraconate inhibits ACOD1 (IRG1) catalysis, reduces interferon responses and oxidative stress, and modulates inflammation and cell metabolism (2022, Nature Metabolism)
  • Moonlighting chaperone activity of the enzyme PqsE contributes to RhlR-controlled virulence of Pseudomonas aeruginosa (2022, Nature Communications)
  • Structural basis of ergothioneine biosynthesis (2020, Current Opinion in Structural Biology)
  • A New PqsR Inverse Agonist Potentiates Tobramycin Efficacy to Eradicate Pseudomonas aeruginosa Biofilms (2021, Advanced Science)
  • Antimicrobial resistance dynamics and the one-health strategy: a review (2021, Environmental Chemistry Letters)

Frequent co-authors of Blankenfeldt include:

  • Peer Lukat
  • Stefan Schmelz
  • Anna K. H. Hirsch
  • Thomas Klünemann
  • Lothar Jänsch

Publication venues where Blankenfeldt regularly contributes include:

  • bioRxiv (Cold Spring Harbor Laboratory)
  • Advanced Science
  • The Cambridge Structural Database
  • Nature Communications
  • Scientific Reports

Best Publications

  • Phenazine Compounds in Fluorescent Pseudomonas Spp. Biosynthesis and Regulation

    Dmitri V. Mavrodi;Wulf Blankenfeldt;Linda S. Thomashow

  • The Legionella Effector Protein DrrA AMPylates the Membrane Traffic Regulator Rab1b

    Matthias P. Müller;Heide Peters;Julia Blümer;Wulf Blankenfeldt

  • The structural basis of the catalytic mechanism and regulation of glucose‐1‐phosphate thymidylyltransferase (RmlA)

    Wulf Blankenfeldt;Miryam Asuncion;Joseph S. Lam;James H. Naismith

  • Recent developments in the isolation, biological function, biosynthesis, and synthesis of phenazine natural products

    Nikolaus Guttenberger;Wulf Blankenfeldt;Rolf Breinbauer

  • RabGDI Displacement by DrrA from Legionella Is a Consequence of Its Guanine Nucleotide Exchange Activity

    Stefan Schoebel;Lena Katharina Oesterlin;Wulf Blankenfeldt;Roger Sidney Goody

  • Analysis of the eukaryotic prenylome by isoprenoid affinity tagging

    Uyen T. T. Nguyen;Zhong Guo;Christine Delon;Yaowen Wu

  • Insights Into Ssdna Recognition by the Ob Fold from a Structural and Thermodynamic Study of Sulfolobus Ssb Protein

    Iain D. Kerr;Ross I.M. Wadsworth;Liza Cubeddu;Wulf Blankenfeldt

  • Structures of the Dual Bromodomains of the P-TEFb-activating Protein Brd4 at Atomic Resolution

    Friederike Vollmuth;Wulf Blankenfeldt;Matthias Geyer

  • Of Two Make One: The Biosynthesis of Phenazines

    Matthias Mentel;Ekta G. Ahuja;Dmitri V. Mavrodi;Rolf Breinbauer

  • The structural biology of phenazine biosynthesis.

    Wulf Blankenfeldt;James F Parsons

  • Crystal structures of human cardiac β-myosin II S2-Δ provide insight into the functional role of the S2 subfragment

    Wulf Blankenfeldt;Nicolas H. Thomä;John S. Wray;Mathias Gautel

  • Noncompaction of the Ventricular Myocardium Is Associated with a De Novo Mutation in the β-Myosin Heavy Chain Gene

    Birgit S. Budde;Priska Binner;Stephan Waldmüller;Wolfgang Höhne

  • A structural basis for Lowe syndrome caused by mutations in the Rab-binding domain of OCRL1.

    Xiaomin Hou;Nina Hagemann;Stefan Schoebel;Wulf Blankenfeldt

  • Structure and function of the phenazine biosynthetic protein PhzF from Pseudomonas fluorescens

    Wulf Blankenfeldt;Alexandre P. Kuzin;Tatiana Skarina;Yuriy Korniyenko

  • Structure of the Sulfoxide Synthase EgtB from the Ergothioneine Biosynthetic Pathway.

    Kristina V. Goncharenko;Allegra Vit;Wulf Blankenfeldt;Florian P. Seebeck

  • High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA

    Stefan Schoebel;Wulf Blankenfeldt;Roger S Goody;Aymelt Itzen

  • Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate.

    Karin Kühnel;Wulf Blankenfeldt;James Terner;Ilme Schlichting

  • The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step.

    Miryam Asuncion;Wulf Blankenfeldt;John N. Barlow;David Gani

  • Biosynthesis of methyl-proline containing griselimycins, natural products with anti-tuberculosis activity.

    Peer Lukat;Yohei Katsuyama;Silke Wenzel;Tina Binz

  • Variation on a theme of SDR. dTDP-6-deoxy-L- lyxo-4-hexulose reductase (RmlD) shows a new Mg2+-dependent dimerization mode.

    Wulf Blankenfeldt;Iain D Kerr;Marie-France Giraud;Helen J McMiken

  • PhzA/B Catalyzes the Formation of the Tricycle in Phenazine Biosynthesis

    Ekta G. Ahuja;Petra Janning;Matthias Mentel;Almut Graebsch

Frequent Co-Authors

Herbert Waldmann
Herbert Waldmann Max Planck Society
Roger S. Goody
Roger S. Goody Max Planck Society
Linda S. Thomashow
Linda S. Thomashow Washington State University
Rolf Breinbauer
Rolf Breinbauer Graz University of Technology
James H. Naismith
James H. Naismith Rosalind Franklin Institute
Kirill Alexandrov
Kirill Alexandrov Queensland University of Technology
Rolf Müller
Rolf Müller Saarland University
Theresia E. B. Stradal
Theresia E. B. Stradal Helmholtz Centre for Infection Research
Chris Whitfield
Chris Whitfield University of Guelph
Klemens Rottner
Klemens Rottner Technische Universität Braunschweig

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