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Rudolf Ladenstein

Rudolf Ladenstein

D-Index & Metrics

Biology and Biochemistry

D-Index
60
Citations
12136
World Ranking
12017
National Ranking
177

Overview

Rudolf Ladenstein is affiliated with the Karolinska Institute in Sweden. Their research spans several interconnected fields, focusing primarily on biochemistry, genetics, and molecular biology, with additional contributions to chemistry.

The scientist's recent publication record includes work published in journals such as Biotechnology Reports, iScience, and SSRN Electronic Journal. Notable papers include:

  • Second career of a biosynthetic enzyme: Lumazine synthase as a virus-like nanoparticle in vaccine development, 2020, Biotechnology Reports
  • Structures of heat shock factor trimers bound to DNA, 2021, iScience
  • Structures of Heat Shock Factor Trimers Bound to DNA Reveal the Panoramic Architecture of the HSF-Regulated Transcriptional Machinery, 2021, SSRN Electronic Journal

The research interests and thematic focus can be summarized across several topics:

  • Heat shock proteins research
  • Thermodynamics and calorimetric analyses
  • Bacteriophages and microbial interactions
  • Monoclonal and Polyclonal Antibodies Research
  • HIV Research and Treatment
  • Protein Structure and Dynamics
  • Viral Infectious Diseases and Gene Expression in Insects

The scientist has collaborated frequently with a range of coauthors, including Avinash S. Punekar, Jingjin Ding, Wei Liu, Ekaterina Morgunova, and Na Feng.

Rudolf Ladenstein's work also intersects with particular subfields such as molecular biology, physical and theoretical chemistry, ecology, radiology, nuclear medicine and imaging, and virology.

Best Publications

  • The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution.

    Otto Epp;Rudolf Ladenstein;Albrecht Wendel

  • Critical Residues for Structure and Catalysis in Short-chain Dehydrogenases/Reductases

    Charlotta Filling;Kurt D. Berndt;Kurt D. Berndt;Jordi Benach;Stefan Knapp

  • Refined crystal structure of ascorbate oxidase at 1.9 A resolution.

    Albrecht Messerschmidt;Rudolf Ladenstein;Robert Huber;Martino Bolognesi

  • X-ray crystal structure of the blue oxidase ascorbate oxidase from zucchini. Analysis of the polypeptide fold and a model of the copper sites and ligands.

    Albrecht Messerschmidt;Antonello Rossi;Rudolf Ladenstein;Robert Huber

  • The three-dimensional structure of class pi glutathione S-transferase in complex with glutathione sulfonate at 2.3 A resolution.

    P. Reinemer;H.W. Dirr;R. Ladenstein;J. Schäffer

  • Ion pairs and the thermotolerance of proteins from hyperthermophiles: a ‘traffic rule’ for hot roads

    Andrey Karshikoff;Rudolf Ladenstein

  • Three-dimensional structure of class π glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 Å resolution☆

    P Reinemer;H.W Dirr;R Ladenstein;R Huber

  • X-ray structure analysis and crystallographic refinement of lumazine synthase from the hyperthermophile Aquifex aeolicus at 1.6 A resolution: determinants of thermostability revealed from structural comparisons.

    Xiaofeng Zhang;Winfried Meining;Winfried Meining;Markus Fischer;Adelbert Bacher

  • Electrostatic properties of two porin channels from Escherichia coli.

    A. Karshikoff;V. Spassov;S.W. Cowan;R. Ladenstein

  • Rigidity versus flexibility: the dilemma of understanding protein thermal stability

    Andrey Karshikoff;Lennart Nilsson;Rudolf Ladenstein

  • Proteins from hyperthermophiles: stability and enzymatic catalysis close to the boiling point of water.

    Rudolf Ladenstein;Garabed Antranikian

  • Solution Structure and DNA-binding Properties of a Thermostable Protein From the Archaeon Sulfolobus Solfataricus

    Herbert Baumann;Stefan Knapp;Thomas Lundbäck;Rudolf Ladenstein

  • The crystal structure of seleno-glutathione peroxidase from human plasma at 2.9 Å resolution

    Bin Ren;Wenhu Huang;Björn Åkesson;Rudolf Ladenstein

  • The optimization of protein‐solvent interactions: Thermostability and the role of hydrophobic and electrostatic interactions

    Velin Z. Spassov;Andrej D. Karshikoff;Rudolf Ladenstein

  • Heavy riboflavin synthase from Bacillus subtilis: Crystal structure analysis of the icosahedral β60 capsid at 3·3 Å resolution

    Rudolf Ladenstein;Monika Schneider;Robert Huber;Hans-Dieter Bartunik

  • Studies on the lumazine synthase/riboflavin synthase complex of Bacillus subtilis: crystal structure analysis of reconstituted, icosahedral beta-subunit capsids with bound substrate analogue inhibitor at 2.4 A resolution.

    Karl Ritsert;Robert Huber;Dusan Turk;Rudolf Ladenstein

  • Active site directed mutagenesis of 3 beta/17 beta-hydroxysteroid dehydrogenase establishes differential effects on short-chain dehydrogenase/reductase reactions

    Udo C. T. Oppermann;Charlotta Filling;Kurt D. Berndt;Bengt Persson

  • Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0 Å resolution

    S. Knapp;W.M. de Vos;D. Rice;R. Ladenstein

  • Structure analysis and molecular model of the selenoenzyme glutathione peroxidase at 2.8 A resolution.

    Rudolf Ladenstein;Otto Epp;Klaus Bartels;Alwyn Jones

  • Proteins from thermophilic and mesophilic organisms essentially do not differ in packing.

    Andrey Karshikoff;Rudolf Ladenstein

Frequent Co-Authors

Stefan Knapp
Stefan Knapp Goethe University Frankfurt
Adelbert Bacher
Adelbert Bacher Technical University of Munich
Markus Fischer
Markus Fischer Universität Hamburg
Robert Huber
Robert Huber University of Duisburg-Essen
Mark Cushman
Mark Cushman Purdue University West Lafayette
Robert Huber
Robert Huber Agricultural & Applied Economics Association
Markus Fischer
Markus Fischer University of Bern
Udo Oppermann
Udo Oppermann University of Oxford
David W. Rice
David W. Rice University of Sheffield
Hans Jörnvall
Hans Jörnvall Karolinska Institute

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