Evidence mapPaperPMID 41318327Full record

ReviewTrends in biochemical sciences2026

Protein codes and mobility together shape cellular function and disease.

Henry R Kilgore, Shannon Moreno, Richard A Young

Abstract readReview
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. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

3 authors.

Henry R KilgoreWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA; Current address: Faculty of Pharmaceutical Sciences, The University of British Columbia, 2405 Wesbrook Mall, Vancouver, BC, V6T 1Z3, Canada. Electronic address: hkilgore@wi.mit.edu.
Shannon MorenoWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.
Richard A YoungWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. Electronic address: young@wi.mit.edu.

Funding

Project 4: Targeting genomic instability and evolution in myelomaP01CA155258 · NCI · DANA-FARBER CANCER INST · 2023 to 2025
$7.4M
Transcriptional regulation in mammalian cellsR35GM144283 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · 2022 to 2025
$1.6M
NCI NIH HHS P01 CA155258NIGMS NIH HHS R35 GM144283NIH HHS S10 OD028520
6 · The paper itself

Abstract

Cells organize their biochemical activities by assembling proteins into both membrane-bound organelles and membrane-less condensates. These compartments enable specialized chemical environments that support unique biochemical functions. Recent evidence indicates that proteins carry encoded instructions for not only protein folding, but also selective distribution into condensate compartments. The dynamic movement of proteins into and within compartments is essential for normal function, while disruptions that reduce protein mobility can impair biochemical rates and cause dysfunction and disease. Here, we review these principles of condensate compartmentalization, emphasizing how encoded protein properties, chemical environments, and dynamic movement shape both cellular health and disease pathology.

Indexed as

ProteinsAnimalsHumansOrganellesProtein FoldingProtein TransportProteinsbiomolecular condensatescollision-limited reactionsmacromolecular crowdingoxidative stressprotein solvation environmentsproteolethargy

Identifiers

PMID41318327
PMCPMC12703758

What Socratic holds

Textmetadata
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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 Socratic graph.