Evidence map›Paper›PMID 32223019›Full record

ReviewProtein science : a publication of the Protein Society2020

Cellular functions and intrinsic attributes of the ATP-binding Eps15 homology domain-containing proteins.

Soumya Bhattacharyya, Thomas J Pucadyil

Open access · greenAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 33% of its field
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

6 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Energy and Dynamics of Caveolae Trafficking.Frontiers in cell and developmental biology · 2020
    Review
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 at 1 institution in 1 country.

Soumya BhattacharyyaDepartment of Biology, Indian Institute of Science Education and Research, Pune, India.
Thomas J PucadyilDepartment of Biology, Indian Institute of Science Education and Research, Pune, India.ORCID 0000-0002-2907-9889
Indian Institute of Science Education and Research Pune · IN

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Several cellular processes rely on a cohort of dedicated proteins that manage tubulation, fission, and fusion of membranes. A notably large number of them belong to the dynamin superfamily of proteins. Among them is the evolutionarily conserved group of ATP-binding Eps15-homology domain-containing proteins (EHDs). In the two decades since their discovery, EHDs have been linked to a range of cellular processes that require remodeling or maintenance of specific membrane shapes such as during endocytic recycling, caveolar biogenesis, ciliogenesis, formation of T-tubules in skeletal muscles, and membrane resealing after rupture. Recent work has shed light on their structure and the unique attributes they possess in linking ATP hydrolysis to membrane remodeling. This review summarizes some of these recent developments and reconciles intrinsic protein functions to their cellular roles.

Indexed as

Adenosine TriphosphateAnimalsHumansHydrolysisProtein DomainsVesicular Transport ProteinsAdenosine TriphosphateVesicular Transport ProteinsATPasescaveolaeciliadynamin superfamilyendocytic recyclingEps15-homology domainmembrane fissionmembrane tubulationT-tubules

Identifiers

PMID32223019
PMCPMC7255522
OpenAlexW3013145282

What OpenQuestion holds

Textmetadata
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.