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Gunter Schneider

Gunter Schneider

D-Index & Metrics

Biology and Biochemistry

D-Index
73
Citations
17737
World Ranking
5982
National Ranking
88

Overview

Gunter Schneider is affiliated with the Karolinska Institute in Sweden. The scientist's research work spans multiple disciplines, focusing particularly on molecular biology and related subfields.

The main areas of study include:

  • Molecular Biology
  • General Health Professions
  • Materials Chemistry
  • Ecology
  • Genetics

Their research topics cover diverse scientific issues, such as:

  • Enzyme Structure and Function
  • Bacteriophages and Microbial Interactions
  • Bacterial Genetics and Biotechnology
  • Legal and Policy Issues
  • Biochemical and Molecular Research
  • Mycobacterium Research and Diagnosis
  • RNA Modifications and Cancer

Selected recent publications illustrate the breadth of their scientific contributions:

  • "A FabG inhibitor targeting an allosteric binding site inhibits several orthologs from Gram-negative ESKAPE pathogens", 2020, Bioorganic & Medicinal Chemistry
  • "Pseudouridine-Modifying Enzymes SapB and SapH Control Entry into the Pseudouridimycin Biosynthetic Pathway", 2023, ACS Chemical Biology
  • "The Importance of Cybersecurity in Digital Government Implementations", 2025, COGNITIONIS Scientific Journal
  • "Mechanism of Two-Component Mono-Oxygenases Involved in Anthracycline 1-Hydroxylation", 2024, ACS Catalysis
  • "Influence of the Eastern cottontail on tree reproduction in sugar maple-beech stands of southern Michigan", 2024, Michigan State University Libraries

Frequent publication venues for Schneider's work include:

  • COGNITIONIS Scientific Journal
  • The Journal of Immunology
  • Bioorganic & Medicinal Chemistry
  • ACS Chemical Biology
  • ACS Catalysis

Collaborations play a significant role in Schneider's research output, with frequent coauthors being:

  • R. Schnell
  • Keisuke Wagatsuma
  • Mika Uematsu
  • Kazuki Teranishi
  • Asako Tsubouchi

Best Publications

  • Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed.

    Ekaterina Morgunova;Ari Tuuttila;Ulrich Bergmann;Mikhail Isupov

  • Crystal structure of delta9 stearoyl-acyl carrier protein desaturase from castor seed and its relationship to other di-iron proteins.

    Y. Lindqvist;W. Huang;G. Schneider;J. Shanklin

  • Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution.

    Ylva Lindqvist;Gunter Schneider;Ulrich Ermler;Michael Sundström

  • Three-dimensional structure of a mammalian thioredoxin reductase: Implications for mechanism and evolution of a selenocysteine-dependent enzyme

    Tatyana Sandalova;Liangwei Zhong;Ylva Lindqvist;Arne Holmgren

  • The manifold of vitamin B6 dependent enzymes

    Gunter Schneider;Helena Käck;Ylva Lindqvist

  • How Thiamine Diphosphate Is Activated in Enzymes

    Dorothee Kern;Gunther Kern;Holger Neef;Kai Tittmann

  • Crystal structure of the active site of ribulose-bisphosphate carboxylase

    Inger Andersson;Stefan Knight;Gunter Schneider;Ylva Lindqvist

  • Structure of the complex between the antibiotic cerulenin and its target, beta-ketoacyl-acyl carrier protein synthase.

    Martin Moche;Gunter Schneider;Patricia Edwards;Katayoon Dehesh

  • High Resolution Crystal Structure of Pyruvate Decarboxylase from Zymomonas mobilis IMPLICATIONS FOR SUBSTRATE ACTIVATION IN PYRUVATE DECARBOXYLASES

    Doreen Dobritzsch;Doreen Dobritzsch;Stephan König;Gunter Schneider;Guoguang Lu

  • Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes.

    Weijun Huang;Jia Jia;Patricia Edwards;Katayoon Dehesh

  • Redesign of soluble fatty acid desaturases from plants for altered substrate specificity and double bond position

    Edgar B. Cahoon;Ylva Lindqvist;Gunter Schneider;John Shanklin

  • Three-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9 Å resolution

    Gunter Schneider;Ylva Lindqvist;Carl-Ivar Brändén;George Lorimer

  • Circular permutations of natural protein sequences: structural evidence.

    Ylva Lindqvist;Gunter Schneider

  • The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis

    Cristofer Enroth;Halina Neujahr;Gunter Schneider;Ylva Lindqvist

  • Three-dimensional structure of a mammalian purple acid phosphatase at 2.2 A resolution with a mu-(hydr)oxo bridged di-iron center.

    Ylva Lindqvist;Eva Johansson;Helena Kaija;Pirkko Vihko;Pirkko Vihko

  • Examination of Substrate Binding in Thiamin Diphosphate- dependent Transketolase by Protein Crystallography and Site-directed Mutagenesis *

    Ulrika Nilsson;Ulrika Nilsson;Ludmilla Meshalkina;Ylva Lindqvist;Gunter Schneider

  • NMR analysis of covalent intermediates in thiamin diphosphate enzymes.

    Kai Tittmann;Ralph Golbik;Kathrin Uhlemann;Ludmila Khailova

  • Siroheme- and [Fe4-S4]-dependent NirA from Mycobacterium tuberculosis is a sulfite reductase with a covalent Cys-Tyr bond in the active site.

    Robert Schnell;Tatyana Sandalova;Ulf Hellman;Ylva Lindqvist

  • Crystal structure of diaminopelargonic acid synthase: evolutionary relationships between pyridoxal-5'-phosphate-dependent enzymes

    Helena Käck;Jenny Sandmark;Katharine Gibson;Gunter Schneider

  • Yeast TKL1 gene encodes a transketolase that is required for efficient glycolysis and biosynthesis of aromatic amino acids.

    M Sundström;Y Lindqvist;G Schneider;U Hellman

Frequent Co-Authors

Ylva Lindqvist
Ylva Lindqvist Karolinska Institute
Georg A. Sprenger
Georg A. Sprenger University of Stuttgart
Klas Kärre
Klas Kärre Karolinska Institute
Robert A. Harris
Robert A. Harris Karolinska Institute
Hermann Sahm
Hermann Sahm Forschungszentrum Jülich
Jakob Michaëlsson
Jakob Michaëlsson Karolinska University Hospital
Israel Silman
Israel Silman Weizmann Institute of Science
Udo Heinemann
Udo Heinemann Max Delbrück Center for Molecular Medicine
Hans-Gustaf Ljunggren
Hans-Gustaf Ljunggren Karolinska Institute
Joel L. Sussman
Joel L. Sussman Weizmann Institute of Science

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