M
Michael H. Glickman
Researcher at Technion – Israel Institute of Technology
Publications - 107
Citations - 14561
Michael H. Glickman is an academic researcher from Technion – Israel Institute of Technology. The author has contributed to research in topics: Proteasome & Ubiquitin. The author has an hindex of 53, co-authored 101 publications receiving 13596 citations. Previous affiliations of Michael H. Glickman include University of California, Berkeley & University of Wisconsin-Madison.
Papers
More filters
Journal ArticleDOI
The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction
TL;DR: It is clear now that degradation of cellular proteins is a highly complex, temporally controlled, and tightly regulated process that plays major roles in a variety of basic pathways during cell life and death as well as in health and disease.
Journal ArticleDOI
A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3.
Michael H. Glickman,David T. Rubin,Olivier Coux,Inge Wefes,Günter Pfeifer,Zdenka Cjeka,Wolfgang Baumeister,Victor A. Fried,Daniel Finley +8 more
TL;DR: The lid subunits share sequence motifs with components of the COP9/signalosome complex and eIF3, suggesting that these functionally diverse particles have a common evolutionary ancestry.
Journal ArticleDOI
A gated channel into the proteasome core particle.
Michael Groll,Monica Bajorek,Alwin Köhler,Luis Moroder,David T. Rubin,Robert Huber,Michael H. Glickman,Daniel Finley +7 more
TL;DR: Crystallographic analysis showed that deletion of the tail of the α3-subunit opens a channel into the proteolytically active interior chamber of the CP, thus derepressing peptide hydrolysis.
Journal ArticleDOI
The Regulatory Particle of the Saccharomyces cerevisiae Proteasome
TL;DR: Overall, regulatory particles from yeasts and mammals are remarkably similar, suggesting that the specific mechanistic features of the proteasome have been closely conserved over the course of evolution.
Journal ArticleDOI
The base of the proteasome regulatory particle exhibits chaperone-like activity.
Beate Braun,Michael H. Glickman,Regine Kraft,Burkhardt Dahlmann,Peter M. Kloetzel,Daniel Finley,Marion Schmidt,Marion Schmidt +7 more
TL;DR: A model in which ubiquitin–protein conjugates are initially tethered to the proteasome by specific recognition of their ubiquit in chains is suggested; this step is followed by a nonspecific interaction between the base and the target protein, which promotes substrate unfolding and translocation.