Evidence map›Paper›PMID 35451616›Full record

ReviewThe Journal of membrane biology2022

Insights into Membrane Curvature Sensing and Membrane Remodeling by Intrinsically Disordered Proteins and Protein Regions.

Chandra Has, P Sivadas, Sovan Lal Das

Open access · bronzeAbstract readReview
In one paragraph

Review in The Journal of membrane biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

16 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
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  8. Intrinsically disordered region amplifies membrane remodeling to augment selective ER-phagy.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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

3 authors at 1 institution in 1 country.

Chandra HasPhysical and Chemical Biology Laboratory and Department of Mechanical Engineering, Indian Institute of Technology Palakkad, Palakkad, Kerala, 678623, India.ORCID 0000-0002-3943-0935
P SivadasPhysical and Chemical Biology Laboratory and Department of Physics, Indian Institute of Technology Palakkad, Palakkad, Kerala, 678623, India.ORCID 0000-0001-9717-1380
Sovan Lal DasPhysical and Chemical Biology Laboratory and Department of Mechanical Engineering, Indian Institute of Technology Palakkad, Palakkad, Kerala, 678623, India. sovan@iitpkd.ac.in.ORCID 0000-0002-1301-4255
Indian Institute of Technology Palakkad · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular membranes are highly dynamic in shape. They can rapidly and precisely regulate their shape to perform various cellular functions. The protein's ability to sense membrane curvature is essential in various biological events such as cell signaling and membrane trafficking. As they are bound, these curvature-sensing proteins may also change the local membrane shape by one or more curvature driving mechanisms. Established curvature-sensing/driving mechanisms rely on proteins with specific structural features such as amphipathic helices and intrinsically curved shapes. However, the recent discovery and characterization of many proteins have shattered the protein structure-function paradigm, believing that the protein functions require a unique structural feature. Typically, such structure-independent functions are carried either entirely by intrinsically disordered proteins or hybrid proteins containing disordered regions and structured domains. It is becoming more apparent that disordered proteins and regions can be potent sensors/inducers of membrane curvatures. In this article, we outline the basic features of disordered proteins and regions, the motifs in such proteins that encode the function, membrane remodeling by disordered proteins and regions, and assays that may be employed to investigate curvature sensing and generation by ordered/disordered proteins.

Indexed as

Intrinsically Disordered ProteinsCell MembraneMembranesProtein Structure, SecondaryIntrinsically Disordered ProteinsDisordered proteinsEntropic effectMembrane curvatureProtein–membrane interactions

Identifiers

PMID35451616
PMCPMC9028910
OpenAlexW4224216856

What Socratic 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 Socratic graph.