World's Best Scientists 2026 revealed!
Hermann Schindelin

Hermann Schindelin

D-Index & Metrics

Biology and Biochemistry

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

Chemistry

D-Index
58
Citations
12309
World Ranking
10599
National Ranking
768

Hermann Schindelin publication distribution in Chemistry in 2026

The chart shows the distribution of publications by all Research.com ranked scientists in the field of Chemistry in 2026. The highlighted bar marks where Hermann Schindelin sits on this spectrum.

61–80 publications: 66 scientists 81–100 publications: 302 scientists 101–120 publications: 623 scientists 121–140 publications: 918 scientists 141–160 publications: 1,218 scientists 161–180 publications: 1,350 scientists 181–200 publications: 1,344 scientists 201–220 publications: 1,281 scientists 221–240 publications: 1,216 scientists 241–260 publications: 1,100 scientists 261–280 publications: 979 scientists 281–300 publications: 939 scientists 301–320 publications: 764 scientists 321–340 publications: 643 scientists 341–360 publications: 628 scientists 361–380 publications: 522 scientists 381–400 publications: 459 scientists 401–420 publications: 397 scientists 421–440 publications: 327 scientists 441–460 publications: 270 scientists 461–480 publications: 265 scientists 481–500 publications: 252 scientists 501–520 publications: 201 scientists 521–540 publications: 185 scientists 541–560 publications: 148 scientists 561–580 publications: 148 scientists 581–600 publications: 132 scientists 601–620 publications: 114 scientists 621–640 publications: 104 scientists 641–660 publications: 91 scientists 661–680 publications: 92 scientists 681–700 publications: 73 scientists 701–720 publications: 57 scientists 721–740 publications: 54 scientists 741–760 publications: 67 scientists 761–780 publications: 45 scientists 781–800 publications: 46 scientists 801–820 publications: 39 scientists 821–840 publications: 32 scientists 841–860 publications: 36 scientists 861–880 publications: 29 scientists 881–900 publications: 26 scientists 901–920 publications: 24 scientists 921–940 publications: 14 scientists 941–960 publications: 23 scientists 961–980 publications: 28 scientists 981–1,000 publications: 15 scientists 1,001–1,020 publications: 29 scientists 1,021–1,040 publications: 12 scientists 1,041–1,060 publications: 19 scientists 1,061–1,080 publications: 12 scientists 1,081–1,100 publications: 6 scientists 1,101–1,120 publications: 8 scientists 1,121–1,140 publications: 12 scientists 1,141–1,160 publications: 5 scientists 1,161–1,180 publications: 6 scientists 1,181–1,200 publications: 14 scientists 1,201–1,220 publications: 7 scientists 1,221–1,240 publications: 2 scientists 1,241–1,260 publications: 6 scientists 1,261–1,280 publications: 4 scientists 1,281–1,294 publications: 6 scientists 1,295+ publications: 100 scientists
61 publications 1,295+

This scientist: 233 publications — 44th percentile

44% of scientists in this discipline score the same or lower.

The last bar groups every scientist with 1,295 publications or more.

Hermann Schindelin D-index placement in Chemistry in 2026

The chart shows the D-index (discipline H-index) distribution of Chemistry scientists ranked by Research.com in 2026. The highlighted bar marks where Hermann Schindelin sits on this spectrum.

40–41 D-Index: 289 scientists 42–43 D-Index: 612 scientists 44–45 D-Index: 808 scientists 46–47 D-Index: 776 scientists 48–49 D-Index: 835 scientists 50–51 D-Index: 861 scientists 52–53 D-Index: 872 scientists 54–55 D-Index: 933 scientists 56–57 D-Index: 1,051 scientists 58–59 D-Index: 930 scientists 60–61 D-Index: 882 scientists 62–63 D-Index: 834 scientists 64–65 D-Index: 731 scientists 66–67 D-Index: 775 scientists 68–69 D-Index: 683 scientists 70–71 D-Index: 646 scientists 72–73 D-Index: 561 scientists 74–75 D-Index: 501 scientists 76–77 D-Index: 437 scientists 78–79 D-Index: 388 scientists 80–81 D-Index: 354 scientists 82–83 D-Index: 292 scientists 84–85 D-Index: 275 scientists 86–87 D-Index: 254 scientists 88–89 D-Index: 235 scientists 90–91 D-Index: 185 scientists 92–93 D-Index: 192 scientists 94–95 D-Index: 155 scientists 96–97 D-Index: 163 scientists 98–99 D-Index: 125 scientists 100–101 D-Index: 105 scientists 102–103 D-Index: 105 scientists 104–105 D-Index: 112 scientists 106–107 D-Index: 88 scientists 108–109 D-Index: 68 scientists 110–111 D-Index: 69 scientists 112–113 D-Index: 65 scientists 114–115 D-Index: 79 scientists 116–117 D-Index: 61 scientists 118–119 D-Index: 44 scientists 120–121 D-Index: 37 scientists 122–123 D-Index: 40 scientists 124–125 D-Index: 33 scientists 126–127 D-Index: 26 scientists 128–129 D-Index: 34 scientists 130–131 D-Index: 35 scientists 132–133 D-Index: 25 scientists 134–135 D-Index: 27 scientists 136–137 D-Index: 17 scientists 138–139 D-Index: 16 scientists 140–141 D-Index: 20 scientists 142–143 D-Index: 20 scientists 144–145 D-Index: 15 scientists 146–147 D-Index: 9 scientists 148–149 D-Index: 9 scientists 150–151 D-Index: 16 scientists 152–153 D-Index: 11 scientists 154–155 D-Index: 9 scientists 156–157 D-Index: 3 scientists 158 D-Index: 3 scientists 159+ D-Index: 98 scientists
40 D-Index 159+

This scientist: 58 D-Index — 42nd percentile

42% of scientists in this discipline score the same or lower.

The last bar groups every scientist with 159 D-Index or more.

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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