Evidence map›Paper›PMID 26666296›Full record

ArticleBiology direct2015

A novel RING finger in the C-terminal domain of the coatomer protein α-COP.

Gurmeet Kaur, Srikrishna Subramanian

Abstract read
In one paragraph

Article in Biology direct, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Coat/Tether Interactions-Exception or Rule?Frontiers in cell and developmental biology · 2016
    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.

Gurmeet KaurCSIR-Institute of Microbial Technology (IMTECH), Sector 39-A, Chandigarh, 160036, India. gurmeetkaur@imtech.res.in.
Srikrishna SubramanianCSIR-Institute of Microbial Technology (IMTECH), Sector 39-A, Chandigarh, 160036, India. krishna@imtech.res.in.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The C-terminal domain of α-COP, an essential subunit of the COPI coatomer complex, is composed of an all α-helical region and a small β-sheet domain. We show that this β-sheet domain is a Really Interesting New Gene (RING)-like treble clef zinc finger. The zinc-binding residues are substituted by other aminoacids in many homologs including the structurally-characterized proteins from Saccharomyces cerevisiae and Bos taurus. This RING-like domain is possibly related to those of other vesicle membrane-associated complexes, such as CORVET, HOPS and SEA, and likely mediates interactions with Dsl1p and assist in coat oligomerization.

Indexed as

Zinc FingersAmino Acid SequenceAnimalsCattleCoatomer ProteinProtein Structure, SecondarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentCoatomer ProteinSaccharomyces cerevisiae Proteins

Identifiers

PMID26666296
PMCPMC4678705

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.