World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

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

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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