Evidence map›Paper›PMID 27658480›Full record

ArticleScientific reports2016

Transmembrane Helices Tilt, Bend, Slide, Torque, and Unwind between Functional States of Rhodopsin.

Zhong Ren, Peter X Ren, Rohith Balusu, Xiaojing Yang

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

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  14. Mcl-1 and Bok transmembrane domains: Unexpected players in the modulation of apoptosis.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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  18. Structural basis of molecular logic OR in a dual-sensor histidine kinase.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. 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

4 authors.

Zhong RenDepartment of Chemistry, University of Illinois at Chicago, Chicago, IL 60607, USA.
Peter X RenHinsdale Central High School, Hinsdale, IL 60521, USA.
Rohith BalusuHinsdale Central High School, Hinsdale, IL 60521, USA.
Xiaojing YangDepartment of Chemistry, University of Illinois at Chicago, Chicago, IL 60607, USA.

Funding

Structures, Dynamics and Signaling Mechanisms of Modular PhotoreceptorsR01EY024363 · NEI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI YANG, XIAOJING · 2014 to 2021
$2.9M
NEI NIH HHS R01 EY024363
6 · The paper itself

Abstract

The seven-helical bundle of rhodopsin and other G-protein coupled receptors undergoes structural rearrangements as the transmembrane receptor protein is activated. These structural changes are known to involve tilting and bending of various transmembrane helices. However, the cause and effect relationship among structural events leading to a cytoplasmic crevasse for G-protein binding is less well defined. Here we present a mathematical model of the protein helix and a simple procedure to determine multiple parameters that offer precise depiction of a helical conformation. A comprehensive survey of bovine rhodopsin structures shows that the helical rearrangements during the activation of rhodopsin involve a variety of angular and linear motions such as torsion, unwinding, and sliding in addition to the previously reported tilting and bending. These hitherto undefined motion components unify the results obtained from different experimental approaches, and demonstrate conformational similarity between the active opsin structure and the photoactivated structures in crystallo near the retinal anchor despite their marked differences.

Identifiers

PMID27658480
PMCPMC5034245

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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.