Evidence map›Paper›PMID 30833452›Full record

ReviewCold Spring Harbor perspectives in biology2020

The Proteasome and Its Network: Engineering for Adaptability.

Daniel Finley, Miguel A Prado

Abstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed, 2 pooled it
–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

61 citing papers in PubMed, 2 syntheses or guidelines pooled it.

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1 more citing papers are in PubMed but not listed here.

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

2 authors.

Daniel FinleyDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115.
Miguel A PradoDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115.ORCID 0000-0002-4914-1619

Funding

UBIQUITIN-PROTEIN CONJUGATES AND FUSIONSR01GM043601 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI FINLEY, DANIEL J · 1990 to 2020
$4.3M
NIGMS NIH HHS R01 GM043601
6 · The paper itself

Abstract

The proteasome, the most complex protease known, degrades proteins that have been conjugated to ubiquitin. It faces the unique challenge of acting enzymatically on hundreds and perhaps thousands of structurally diverse substrates, mechanically unfolding them from their native state and translocating them vectorially from one specialized compartment of the enzyme to another. Moreover, substrates are modified by ubiquitin in myriad configurations of chains. The many unusual design features of the proteasome may have evolved in part to endow this enzyme with a robust ability to process substrates regardless of their identity. The proteasome plays a major role in preserving protein homeostasis in the cell, which requires adaptation to a wide variety of stress conditions. Modulation of proteasome function is achieved through a large network of proteins that interact with it dynamically, modify it enzymatically, or fine-tune its levels. The resulting adaptability of the proteasome, which is unique among proteases, enables cells to control the output of the ubiquitin-proteasome pathway on a global scale.

Indexed as

Gene Expression RegulationAdenosine TriphosphateAnimalsCaenorhabditis elegansCryoelectron MicroscopyCytoplasmDNA-Binding ProteinsHomeostasisHumansModels, MolecularMolecular ConformationNuclear Respiratory Factor 1Proteasome Endopeptidase ComplexProtein DenaturationProtein EngineeringProtein FoldingAdenosine TriphosphateATP dependent 26S proteaseDNA-Binding ProteinsNRF1 protein, humanNuclear Respiratory Factor 1Proteasome Endopeptidase ComplexRPN4 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsUbiquitinUbiquitin ThiolesteraseUSP14 protein, human

Identifiers

PMID30833452
PMCPMC6829053

What OpenQuestion holds

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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.