World's Best Scientists 2026 revealed!
Hermann Schindelin

Hermann Schindelin

D-Index & Metrics

Chemistry

D-Index
58
Citations
12309
World Ranking
10601
National Ranking
767

Biology and Biochemistry

D-Index
60
Citations
12759
World Ranking
11965
National Ranking
850

Overview

What is he best known for?

The fields of study he is best known for:

  • Enzyme
  • Gene
  • Amino acid

His primary areas of investigation include Biochemistry, Molybdenum cofactor, Cyclic pyranopterin monophosphate, Stereochemistry and Active site. His Biochemistry study frequently links to other fields, such as Biophysics. Hermann Schindelin has included themes like Crystallography, Molybdenum and Molybdopterin in his Molybdenum cofactor study.

His Cyclic pyranopterin monophosphate research includes themes of Guanosine, Radical SAM and Ligand Binding Protein. His Stereochemistry research is multidisciplinary, incorporating perspectives in Folding, Thioredoxin and Cofactor. The various areas that Hermann Schindelin examines in his Active site study include Cooperativity, Protein disulfide-isomerase, Protein Disulfide-Isomerase Family, Protein folding and Isomerase.

His most cited work include:

  • Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction. (400 citations)
  • Molybdenum-Cofactor–Containing Enzymes: Structure and Mechanism (386 citations)
  • Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase. (349 citations)

What are the main themes of his work throughout his whole career to date?

Hermann Schindelin mostly deals with Biochemistry, Stereochemistry, Gephyrin, Cell biology and Crystallography. His Biochemistry study frequently intersects with other fields, such as Biophysics. His Stereochemistry study integrates concerns from other disciplines, such as Reductase, Protein disulfide-isomerase, Active site, Isomerase and Binding site.

His Gephyrin study also includes

  • Collybistin which is related to area like Plasma protein binding,
  • Inhibitory postsynaptic potential which is related to area like Neurotransmission. In general Crystallography study, his work on Crystal structure often relates to the realm of Monomer, thereby connecting several areas of interest. His Molybdenum cofactor study combines topics in areas such as Protein structure, Peptide sequence, Sequence alignment and Molybdenum.

He most often published in these fields:

  • Biochemistry (58.82%)
  • Stereochemistry (21.18%)
  • Gephyrin (18.82%)

What were the highlights of his more recent work (between 2017-2021)?

  • Cell biology (17.65%)
  • Crystal structure (10.59%)
  • Neurotransmission (5.88%)

In recent papers he was focusing on the following fields of study:

Hermann Schindelin mainly focuses on Cell biology, Crystal structure, Neurotransmission, Pyridoxal kinase and Ubiquitin. Hermann Schindelin focuses mostly in the field of Crystal structure, narrowing it down to topics relating to Stereochemistry and, in certain cases, Peptide and Ternary complex. The study incorporates disciplines such as Gephyrin, Scaffold protein and Inhibitory postsynaptic potential in addition to Neurotransmission.

His Ubiquitin research is multidisciplinary, incorporating elements of Extracellular, Intracellular and Proteasome. He undertakes multidisciplinary studies into Artesunate and Biochemistry in his work. His studies deal with areas such as Interactor and In vivo as well as Biochemistry.

Between 2017 and 2021, his most popular works were:

  • Developmental seizures and mortality result from reducing GABA A receptor α2-subunit interaction with collybistin (27 citations)
  • Structure–Function Relationships of Glycine and GABAA Receptors and Their Interplay With the Scaffolding Protein Gephyrin (20 citations)
  • Elucidating the molecular basis for inhibitory neurotransmission regulation by artemisinins. (11 citations)

In his most recent research, the most cited papers focused on:

  • Enzyme
  • Gene
  • Amino acid

Cell biology, Receptor, Neurotransmission, Ion channel and Glycine receptor are his primary areas of study. His Cell biology research incorporates themes from Aminobutyric acid, GABAB receptor, Structural protein and K channels. His Neurotransmission research incorporates elements of Inhibitory postsynaptic potential and GABAA receptor.

His studies in GABAA receptor integrate themes in fields like Collybistin, Plasma protein binding, Mutation and HEK 293 cells. His biological study spans a wide range of topics, including Small-angle X-ray scattering, Biophysics, Transient receptor potential channel and Protein secondary structure. Hermann Schindelin studies Gephyrin, a branch of Glycine receptor.

Best Publications

  • Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction.

    Hermann Schindelin;Caroline Kisker;Jamie L. Schlessman;James B. Howard

  • Molybdenum-Cofactor–Containing Enzymes: Structure and Mechanism

    Caroline Kisker;Hermann Schindelin;Douglas C. Rees

  • Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase.

    Caroline Kisker;Hermann Schindelin;Andrew Pacheco;William A Wehbi

  • Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination.

    Hermann Schindelin;Caroline Kisker;James Hilton;K. V. Rajagopalan

  • Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein.

    Hermann Schindelin;Mohamed A. Marahiel;Udo Heinemann

  • The Crystal Structure of Yeast Protein Disulfide Isomerase Suggests Cooperativity between Its Active Sites

    Geng Tian;Song Xiang;Robert Noiva;William J. Lennarz

  • Crystal structure of CspA, the major cold shock protein of Escherichia coli

    Hermann Schindelin;Weining Jiang;Masayori Inouye;Udo Heinemann

  • Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes.

    Imsang Lee;Hermann Schindelin;Hermann Schindelin

  • Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 A resolution.

    Frank Schneider;Jan Löwe;Robert Huber;Hermann Schindelin

  • A left-hand beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila.

    Caroline Kisker;Hermann Schindelin;Birgit E. Alber;James G. Ferry

  • Mechanism of Ubiquitin Activation Revealed by the Structure of a Bacterial MoeB-MoaD Complex

    Michael W. Lake;Margot M. Wuebbens;K. V. Rajagopalan;Hermann Schindelin

  • Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans

    Petra Hänzelmann;Hermann Schindelin

  • Control of p97 function by cofactor binding

    Alexander Buchberger;Hermann Schindelin;Petra Hänzelmann

  • Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation

    Michael J. Rudolph;Margot M. Wuebbens;K.V. Rajagopalan;Hermann Schindelin

  • The Interplay of Cofactor Interactions and Post-translational Modifications in the Regulation of the AAA+ ATPase p97

    Petra Hänzelmann;Hermann Schindelin

  • A structural comparison of molybdenum cofactor-containing enzymes

    Caroline Kisker;Hermann Schindelin;Dietmar Baas;Janos Rétey

  • The residence time of GABA(A)Rs at inhibitory synapses is determined by direct binding of the receptor α1 subunit to gephyrin

    Jayanta Mukherjee;Karla Kretschmannova;Geraldine Gouzer;Hans-Michael Maric

  • The 1.3 Å Crystal Structure of Rhodobacter sphaeroides Dimethyl Sulfoxide Reductase Reveals Two Distinct Molybdenum Coordination Environments

    H.K Li;K Temple;K.V Rajagopalan;H. Schindelin

  • Binding of 5'-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism.

    Petra Hänzelmann;Hermann Schindelin

  • Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis

    Petra Hänzelmann;Heather L. Hernández;Christian Menzel;Ricardo García-Serres

Frequent Co-Authors

Caroline Kisker
Caroline Kisker University of Würzburg
Douglas C. Rees
Douglas C. Rees California Institute of Technology
William J. Lennarz
William J. Lennarz Stony Brook University
K. V. Rajagopalan
K. V. Rajagopalan Duke University
Stephen J. Moss
Stephen J. Moss Tufts University
Udo Heinemann
Udo Heinemann Max Delbrück Center for Molecular Medicine
James G. Ferry
James G. Ferry Pennsylvania State University
Hiroaki Kiyokawa
Hiroaki Kiyokawa Northwestern University
James B. Howard
James B. Howard University of Minnesota
Anthony A. Holder
Anthony A. Holder The Francis Crick Institute

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