World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
63
Citations
20094
World Ranking
10023
National Ranking
95

Michael H. Glickman publication distribution in Biology and Biochemistry in 2026

The chart shows the distribution of publications by all Research.com ranked scientists in the field of Biology and Biochemistry in 2026. The highlighted bar marks where Michael H. Glickman sits on this spectrum.

47–56 publications: 8 scientists 57–66 publications: 35 scientists 67–76 publications: 106 scientists 77–86 publications: 231 scientists 87–96 publications: 414 scientists 97–106 publications: 546 scientists 107–116 publications: 704 scientists 117–126 publications: 849 scientists 127–136 publications: 980 scientists 137–146 publications: 942 scientists 147–156 publications: 969 scientists 157–166 publications: 950 scientists 167–176 publications: 951 scientists 177–186 publications: 915 scientists 187–196 publications: 787 scientists 197–206 publications: 841 scientists 207–216 publications: 735 scientists 217–226 publications: 709 scientists 227–236 publications: 651 scientists 237–246 publications: 605 scientists 247–256 publications: 510 scientists 257–266 publications: 524 scientists 267–276 publications: 434 scientists 277–286 publications: 418 scientists 287–296 publications: 350 scientists 297–306 publications: 363 scientists 307–316 publications: 315 scientists 317–326 publications: 296 scientists 327–336 publications: 261 scientists 337–346 publications: 240 scientists 347–356 publications: 219 scientists 357–366 publications: 197 scientists 367–376 publications: 154 scientists 377–386 publications: 161 scientists 387–396 publications: 155 scientists 397–406 publications: 145 scientists 407–416 publications: 124 scientists 417–426 publications: 112 scientists 427–436 publications: 132 scientists 437–446 publications: 116 scientists 447–456 publications: 99 scientists 457–466 publications: 81 scientists 467–476 publications: 91 scientists 477–486 publications: 80 scientists 487–496 publications: 80 scientists 497–506 publications: 60 scientists 507–516 publications: 36 scientists 517–526 publications: 46 scientists 527–536 publications: 54 scientists 537–546 publications: 44 scientists 547–556 publications: 43 scientists 557–566 publications: 43 scientists 567–576 publications: 42 scientists 577–586 publications: 25 scientists 587–596 publications: 34 scientists 597–606 publications: 23 scientists 607–616 publications: 33 scientists 617–626 publications: 31 scientists 627–636 publications: 27 scientists 637–646 publications: 25 scientists 647–656 publications: 28 scientists 657–666 publications: 34 scientists 667–676 publications: 18 scientists 677–686 publications: 16 scientists 687–696 publications: 10 scientists 697–706 publications: 12 scientists 707–716 publications: 21 scientists 717–726 publications: 12 scientists 727–736 publications: 12 scientists 737–746 publications: 10 scientists 747–756 publications: 7 scientists 757–766 publications: 13 scientists 767–776 publications: 15 scientists 777–786 publications: 13 scientists 787–796 publications: 9 scientists 797–806 publications: 9 scientists 807–816 publications: 7 scientists 817–826 publications: 4 scientists 827–836 publications: 9 scientists 837–846 publications: 7 scientists 847–856 publications: 3 scientists 857–866 publications: 5 scientists 867–876 publications: 5 scientists 877–886 publications: 11 scientists 887–896 publications: 3 scientists 897–906 publications: 4 scientists 907–916 publications: 7 scientists 917–926 publications: 5 scientists 927–936 publications: 6 scientists 937–946 publications: 6 scientists 947–956 publications: 3 scientists 957–966 publications: 7 scientists 967–976 publications: 2 scientists 977–986 publications: 2 scientists 987–996 publications: 1 scientists 997–1,006 publications: 5 scientists 1,007–1,016 publications: 2 scientists 1,017–1,026 publications: 2 scientists 1,027 publications: 1 scientists 1,028+ publications: 100 scientists
47 publications 1,028+

This scientist: 121 publications — 12th percentile

12% of scientists in this discipline score the same or lower.

The last bar groups every scientist with 1,028 publications or more.

Michael H. Glickman D-index placement in Biology and Biochemistry in 2026

The chart shows the D-index (discipline H-index) distribution of Biology and Biochemistry scientists ranked by Research.com in 2026. The highlighted bar marks where Michael H. Glickman sits on this spectrum.

40–41 D-Index: 80 scientists 42–43 D-Index: 183 scientists 44–45 D-Index: 317 scientists 46–47 D-Index: 504 scientists 48–49 D-Index: 718 scientists 50–51 D-Index: 900 scientists 52–53 D-Index: 1,026 scientists 54–55 D-Index: 1,150 scientists 56–57 D-Index: 1,236 scientists 58–59 D-Index: 1,253 scientists 60–61 D-Index: 1,163 scientists 62–63 D-Index: 1,131 scientists 64–65 D-Index: 1,032 scientists 66–67 D-Index: 897 scientists 68–69 D-Index: 814 scientists 70–71 D-Index: 715 scientists 72–73 D-Index: 709 scientists 74–75 D-Index: 596 scientists 76–77 D-Index: 512 scientists 78–79 D-Index: 473 scientists 80–81 D-Index: 412 scientists 82–83 D-Index: 373 scientists 84–85 D-Index: 358 scientists 86–87 D-Index: 285 scientists 88–89 D-Index: 273 scientists 90–91 D-Index: 227 scientists 92–93 D-Index: 208 scientists 94–95 D-Index: 193 scientists 96–97 D-Index: 153 scientists 98–99 D-Index: 157 scientists 100–101 D-Index: 148 scientists 102–103 D-Index: 120 scientists 104–105 D-Index: 113 scientists 106–107 D-Index: 100 scientists 108–109 D-Index: 86 scientists 110–111 D-Index: 67 scientists 112–113 D-Index: 72 scientists 114–115 D-Index: 73 scientists 116–117 D-Index: 64 scientists 118–119 D-Index: 53 scientists 120–121 D-Index: 60 scientists 122–123 D-Index: 54 scientists 124–125 D-Index: 43 scientists 126–127 D-Index: 38 scientists 128–129 D-Index: 49 scientists 130–131 D-Index: 26 scientists 132–133 D-Index: 18 scientists 134–135 D-Index: 23 scientists 136–137 D-Index: 32 scientists 138–139 D-Index: 32 scientists 140–141 D-Index: 27 scientists 142–143 D-Index: 19 scientists 144–145 D-Index: 22 scientists 146–147 D-Index: 12 scientists 148–149 D-Index: 16 scientists 150–151 D-Index: 14 scientists 152–153 D-Index: 10 scientists 154–155 D-Index: 13 scientists 156–157 D-Index: 10 scientists 158–159 D-Index: 7 scientists 160–161 D-Index: 9 scientists 162–163 D-Index: 13 scientists 164–165 D-Index: 4 scientists 166 D-Index: 4 scientists 167+ D-Index: 98 scientists
40 D-Index 167+

This scientist: 63 D-Index — 49th percentile

49% of scientists in this discipline score the same or lower.

The last bar groups every scientist with 167 D-Index or more.

Overview

What is he best known for?

The fields of study he is best known for:

  • Enzyme
  • Amino acid
  • Biochemistry

The scientist’s investigation covers issues in Proteasome, Biochemistry, Cell biology, Ubiquitin ligase and Proteolysis. Michael H. Glickman studied Proteasome and Proteasome assembly that intersect with Protein structure. His Biochemistry study incorporates themes from Deubiquitinating enzyme and Ubiquitin-conjugating enzyme.

His Ubiquitin-conjugating enzyme research includes themes of Protein folding, Chaperone and Citrate synthase. In the subject of general Cell biology, his work in Mitochondrion is often linked to COP9 signalosome, thereby combining diverse domains of study. He has included themes like PSMB5, Ubiquitin proteasome and Nucleic acid in his Protein degradation study.

His most cited work include:

  • The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction (3307 citations)
  • A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. (803 citations)
  • A gated channel into the proteasome core particle. (659 citations)

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

His primary scientific interests are in Proteasome, Cell biology, Biochemistry, Proteolysis and Ubiquitin ligase. Michael H. Glickman combines subjects such as Saccharomyces cerevisiae, Protein degradation, Deubiquitinating enzyme, Biophysics and Protein structure with his study of Proteasome. The Mitochondrion research Michael H. Glickman does as part of his general Cell biology study is frequently linked to other disciplines of science, such as COP9 signalosome, therefore creating a link between diverse domains of science.

His research in Biochemistry intersects with topics in Proteasome regulatory particle, Ubiquitins and Ubiquitin-conjugating enzyme. His Proteolysis research focuses on Deubiquitination and how it connects with C-terminus and Lysine. His studies deal with areas such as Proteasome inhibitor and Phosphorylation as well as Ubiquitin ligase.

He most often published in these fields:

  • Proteasome (78.10%)
  • Cell biology (51.43%)
  • Biochemistry (49.52%)

What were the highlights of his more recent work (between 2014-2021)?

  • Proteasome (78.10%)
  • Cell biology (51.43%)
  • Proteolysis (24.76%)

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

His main research concerns Proteasome, Cell biology, Proteolysis, Biochemistry and Substrate. His study in Proteasome is interdisciplinary in nature, drawing from both Deubiquitination, Biophysics, Holoenzymes, Receptor and Small molecule. His Cell biology research is multidisciplinary, relying on both Autophagy and Proteasome assembly.

In his research on the topic of Proteolysis, Cell cycle progression, Cellular proteins, Proteasome activity and Intracellular is strongly related with Function. As a part of the same scientific study, Michael H. Glickman usually deals with the Biochemistry, concentrating on Ubiquitin ligase and frequently concerns with Proteasome inhibitor. Michael H. Glickman interconnects Isopeptide bond, Protein degradation and Cleavage in the investigation of issues within Substrate.

Between 2014 and 2021, his most popular works were:

  • UBQLN2 mediates autophagy-independent protein aggregate clearance by the proteasome (158 citations)
  • DNA-Damage-Inducible 1 Protein (Ddi1) Contains an Uncharacteristic Ubiquitin-like Domain that Binds Ubiquitin (45 citations)
  • The protein quality control machinery regulates its misassembled proteasome subunits. (38 citations)

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

  • Enzyme
  • Amino acid
  • Biochemistry

Michael H. Glickman mainly focuses on Proteasome, Biochemistry, Cell biology, Proteolysis and Ubiquitin-conjugating enzyme. He has researched Proteasome in several fields, including Receptor and Biophysics. His Biochemistry course of study focuses on Deubiquitination and Cleavage, Isopeptide bond and Substrate.

Many of his research projects under Cell biology are closely connected to Neurodegeneration with Neurodegeneration, tying the diverse disciplines of science together. His Proteolysis study integrates concerns from other disciplines, such as Proteasome assembly, Chaperone and Immunoprecipitation. Ubiquitin ligase covers Michael H. Glickman research in Ubiquitin-conjugating enzyme.

Best Publications

  • The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction

    Michael H. Glickman;Aaron Ciechanover

  • A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3.

    Michael H Glickman;David M Rubin;Olivier Coux;Inge Wefes

  • A gated channel into the proteasome core particle.

    Michael Groll;Monica Bajorek;Alwin Köhler;Luis Moroder

  • The Regulatory Particle of the Saccharomyces cerevisiae Proteasome

    Michael H. Glickman;David M. Rubin;Victor A. Fried;Daniel Finley

  • The base of the proteasome regulatory particle exhibits chaperone-like activity.

    Beate C. Braun;Michael Glickman;Regine Kraft;Burkhardt Dahlmann

  • The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover.

    S van Nocker;S Sadis;D M Rubin;M Glickman

  • Stress-induced phosphorylation and proteasomal degradation of mitofusin 2 facilitates mitochondrial fragmentation and apoptosis.

    Guillaume P. Leboucher;Yien Che Tsai;Mei Yang;Kristin C. Shaw

  • Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome

    David M. Rubin;Michael H. Glickman;Christopher N. Larsen;Sadhana Dhruvakumar

  • A Stress-Responsive System for Mitochondrial Protein Degradation

    Jin Mi Heo;Nurit Livnat-Levanon;Eric B. Taylor;Kevin T. Jones

  • Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome

    Hongyong Fu;Noa Reis;Yenfen Lee;Michael H. Glickman

  • MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function

    Vered Maytal-Kivity;Noa Reis;Kay Hofmann;Michael H Glickman

  • UBQLN2 mediates autophagy-independent protein aggregate clearance by the proteasome

    Roland Hjerpe;John S. Bett;John S. Bett;Matthew J. Keuss;Alexandra Solovyova

  • Multiubiquitin Chain Binding and Protein Degradation Are Mediated by Distinct Domains within the 26 S Proteasome Subunit Mcb1

    Hongyong Fu;Seth Sadis;David M. Rubin;Michael Glickman

  • Ubiquitin–Proteasome System and mitochondria — Reciprocity

    Nurit Livnat-Levanon;Michael H. Glickman

  • Unified nomenclature for the COP9 signalosome and its subunits: an essential regulator of development

    XW Deng;W Dubiel;N Wei;K Hofmann

  • Experimental Evidence for Extensive Tunneling of Hydrogen in the Lipoxygenase Reaction: Implications for Enzyme Catalysis

    Thorlakur Jonsson;Michael H. Glickman;Shujun Sun,§,‖ and;Judith P. Klinman

  • Complementary Roles for Rpn11 and Ubp6 in Deubiquitination and Proteolysis by the Proteasome

    Adi Guterman;Michael H. Glickman

  • Proteasome disassembly and downregulation is correlated with viability during stationary phase

    Monika Bajorek;Daniel Finley;Michael H. Glickman

  • Nature of Rate-Limiting Steps in the Soybean Lipoxygenase-1 Reaction

    Michael H. Glickman;Judith P. Klinman

  • The Zinc Finger of the CSN-Associated Deubiquitinating Enzyme USP15 Is Essential to Rescue the E3 Ligase Rbx1

    Bettina K.J. Hetfeld;Annett Helfrich;Barbara Kapelari;Hartmut Scheel

Frequent Co-Authors

Daniel Finley
Daniel Finley Harvard University
David Fushman
David Fushman University of Maryland, College Park
David T. Rubin
David T. Rubin University of Chicago
Richard D. Vierstra
Richard D. Vierstra Washington University in St. Louis
Judith P. Klinman
Judith P. Klinman University of California, Berkeley
Ashraf Brik
Ashraf Brik Technion – Israel Institute of Technology
Kay Hofmann
Kay Hofmann University of Cologne
Thomas Sommer
Thomas Sommer Max Delbrück Center for Molecular Medicine
Aaron Ciechanover
Aaron Ciechanover Technion – Israel Institute of Technology
Steven P. Gygi
Steven P. Gygi Harvard University

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