Evidence map›Paper›PMID 26703751›Full record

ReviewBiology2015

Cell Adhesion Molecules and Ubiquitination-Functions and Significance.

Mirka Homrich, Ingo Gotthard, Hilke Wobst, Simone Diestel

Open access · goldAbstract readReview
In one paragraph

Review in Biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

9 citing papers in PubMed, 53 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Mirka HomrichDepartment of Human Metabolomics, Institute of Nutrition and Food Sciences, University of Bonn, Katzenburgweg 9a, Bonn 53115, Germany. mhomrich@uni-bonn.de.
Ingo GotthardDepartment of Human Metabolomics, Institute of Nutrition and Food Sciences, University of Bonn, Katzenburgweg 9a, Bonn 53115, Germany. s7ingott@uni-bonn.de.
Hilke WobstDepartment of Human Metabolomics, Institute of Nutrition and Food Sciences, University of Bonn, Katzenburgweg 9a, Bonn 53115, Germany. h.wobst@uni-bonn.de.
Simone DiestelDepartment of Human Metabolomics, Institute of Nutrition and Food Sciences, University of Bonn, Katzenburgweg 9a, Bonn 53115, Germany. s.diestel@uni-bonn.de.
University of Bonn · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell adhesion molecules of the immunoglobulin (Ig) superfamily represent the biggest group of cell adhesion molecules. They have been analyzed since approximately 40 years ago and most of them have been shown to play a role in tumor progression and in the nervous system. All members of the Ig superfamily are intensively posttranslationally modified. However, many aspects of their cellular functions are not yet known. Since a few years ago it is known that some of the Ig superfamily members are modified by ubiquitin. Ubiquitination has classically been described as a proteasomal degradation signal but during the last years it became obvious that it can regulate many other processes including internalization of cell surface molecules and lysosomal sorting. The purpose of this review is to summarize the current knowledge about the ubiquitination of cell adhesion molecules of the Ig superfamily and to discuss its potential physiological roles in tumorigenesis and in the nervous system.

Indexed as

cell adhesion moleculesendocytosisimmunoglobulin superfamilyintracellular traffickingposttranslational modificationubiquitination

Identifiers

PMID26703751
PMCPMC4810158
OpenAlexW2206274026

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.