Evidence map›Paper›PMID 41796444›Full record

ReviewTrends in biochemical sciences2026

Magical moments in protease biology: proteasome autocatalytic activation and PI31-mediated inhibition.

Tamayanthi Rajakumar, Erignacio Fermin Perez, Darlene Fung, Shaun Rawson, Richard M Walsh, John Hanna

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Trends in biochemical sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Tamayanthi RajakumarDepartment of Pathology, Harvard Medical School and Brigham and Women's Hospital, Boston, MA, USA.
Erignacio Fermin PerezDepartment of Pathology, Harvard Medical School and Brigham and Women's Hospital, Boston, MA, USA.
Darlene FungDepartment of Pathology, Harvard Medical School and Brigham and Women's Hospital, Boston, MA, USA.
Shaun RawsonHarvard Cryo-Electron Microscopy Center for Structural Biology, Harvard Medical School, Boston, MA, USA; Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA.
Richard M WalshHarvard Cryo-Electron Microscopy Center for Structural Biology, Harvard Medical School, Boston, MA, USA; Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA.
John HannaDepartment of Pathology, Harvard Medical School and Brigham and Women's Hospital, Boston, MA, USA. Electronic address: jwhanna@bwh.harvard.edu.

Funding

Structural and Functional Analysis of Proteasome Core Particle BiogenesisR01GM144367 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI HANNA, JOHN W · 2022 to 2025
$1.6M
Role of very long chain fatty acids in protein quality control and membrane homeostasisR01GM135337 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI HANNA, JOHN W · 2020 to 2023
$1.6M
NIGMS NIH HHS R01 GM135337NIGMS NIH HHS R01 GM144367
6 · The paper itself

Abstract

Proteases regulate nearly every aspect of cellular function. Spatial and temporal control of protease activity contributes to this functional versatility and includes both zymogen activation mechanisms and the existence of dedicated protease inhibitors. Unlike conventional proteases, the proteasome harbors six individual proteases within a single macromolecular complex. This unique arrangement poses formidable challenges by requiring simultaneous activation or inhibition of all six active sites. Recent work from multiple labs has uncovered key aspects of assembly-coupled autocatalytic activation as well as the mechanism of proteasome inhibition by the endogenous inhibitor PI31 (proteasome inhibitor 31 kDa). These elegant mechanisms highlight and expand the remarkable complexity and beauty of protease biology.

Indexed as

Proteasome Endopeptidase ComplexAnimalsEnzyme ActivationHumansProteasome Endopeptidase Complexautocatalytic activationcatalytic triadmultiple myelomaproteaseprotease inhibitorproteasome

Identifiers

PMID41796444
PMCPMC12974239

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.