Evidence map›Paper›PMID 29395045›Full record

ArticleBiophysical journal2018

Effect of Grafting on Aggregation of Intrinsically Disordered Proteins.

Dino Osmanovic, Yitzhak Rabin

Abstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

2 authors.

Dino OsmanovicDepartment of Physics of Living Systems, MIT, Cambridge, Massachusetts; Department of Physics, Bar-Ilan University, Ramat-Gan, Israel. Electronic address: d.osmanovic@ucl.ac.uk.
Yitzhak RabinDepartment of Physics, Bar-Ilan University, Ramat-Gan, Israel.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A significant part of the proteome is composed of intrinsically disordered proteins (IDPs). These proteins do not fold into a well-defined structure and behave like ordinary polymers. In this work, we consider IDPs that have the tendency to aggregate, model them as heteropolymers that contain a small number of associating monomers, and use computer simulations to compare the aggregation of such IDPs that are grafted to a surface or free in solution. We then discuss how such grafting may affect the analysis of in vitro experiments and could also be used to suppress harmful aggregation.

Indexed as

Models, BiologicalProtein AggregatesHumansIntrinsically Disordered ProteinsProtein ConformationProtein MultimerizationIntrinsically Disordered ProteinsProtein Aggregates

Identifiers

PMID29395045
PMCPMC5985032

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.