Evidence map›Paper›PMID 31618110›Full record

ArticleMolecular biology of the cell2019

Activity of a ubiquitin ligase adaptor is regulated by disordered insertions in its arrestin domain.

Matthew G Baile, Evan L Guiney, Ethan J Sanford, Jason A MacGurn, Marcus B Smolka, Scott D Emr

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular biology of the cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. α-Arrestins and Their Functions: From Yeast to Human Health.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Article
  8. Article
  9. [A Review of Research Progress in the Pathophysiological Mechanism of Stress-related Mental Disorders].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2021
    Review
  10. 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

6 authors.

Matthew G BaileWeill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853.
Evan L GuineyWeill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853.
Ethan J SanfordWeill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853.
Jason A MacGurnDepartment of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37212.
Marcus B SmolkaWeill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853.
Scott D EmrWeill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853.

Funding

Cellular Responses to DNA Replication StressR01GM097272 · NIGMS · CORNELL UNIVERSITY · PI SMOLKA, MARCUS · 2011 to 2020
$2.7M
Substrate Targeting Mechanisms of Nedd4 Family Ubiquitin LigasesR00GM101077 · NIGMS · VANDERBILT UNIVERSITY · PI MACGURN, JASON A · 2014 to 2016
$747k
NIGMS NIH HHS R00 GM101077NIGMS NIH HHS R01 GM097272
6 · The paper itself

Abstract

The protein composition of the plasma membrane is rapidly remodeled in response to changes in nutrient availability or cellular stress. This occurs, in part, through the selective ubiquitylation and endocytosis of plasma membrane proteins, which in the yeast

Indexed as

ArrestinsCell MembraneDNA-Binding ProteinsEndocytosisEndosomal Sorting Complexes Required for TransportMembrane ProteinsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsUbiquitinUbiquitinationUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesArrestinsDNA-Binding ProteinsEndosomal Sorting Complexes Required for TransportMembrane ProteinsRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSWI4 protein, S cerevisiaeTranscription FactorsUbiquitinUbiquitin-Protein Ligase ComplexesUbiquitin-Protein Ligases

Identifiers

PMID31618110
PMCPMC6880881

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.