Evidence map›Paper›PMID 41279639›Full record

ArticlebioRxiv : the preprint server for biology2025

Lipid bilayer thinning near a ubiquitin ligase selects ER membrane proteins for degradation.

Rudolf Pisa, Tom A Rapoport

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2025. 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

2 authors.

Rudolf PisaDepartment of Cell Biology, Harvard Medical School, and Howard Hughes Medical Institute; 240 Longwood Avenue, Boston, MA 02115, USA.ORCID 0000-0001-7571-7135
Tom A RapoportDepartment of Cell Biology, Harvard Medical School, and Howard Hughes Medical Institute; 240 Longwood Avenue, Boston, MA 02115, USA.ORCID 0000-0001-9911-4216

Funding

PROTEIN TRANSPORT INTO MAMMALIAN ENDOPLASMIC RETICULUMR01GM052586 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI Tom A Rapoport · 1995 to 2026
$11.9M
Mechanistic and Structural Studies of ERADK99GM154114 · NIGMS · HARVARD MEDICAL SCHOOL · PI PISA, RUDOLF · 2024 to 2025
$250k
NIGMS NIH HHS K99 GM154114NIGMS NIH HHS R01 GM052586
6 · The paper itself

Abstract

Misfolded or unassembled membrane proteins in the endoplasmic reticulum (ER) are polyubiquitinated, translocated into the cytosol, and degraded by the proteasome, a poorly understood process that is conserved in all eukaryotes. Here, we use

Identifiers

PMID41279639
PMCPMC12636353

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.