Evidence map›Paper›PMID 36352784›Full record

ArticleBiophysical journal2023

Lipid membrane mimetics and oligomerization tune functional properties of proteorhodopsin.

Chung-Ta Han, Khanh Dinh Quoc Nguyen, Maxwell W Berkow, Sunyia Hussain, Ahmad Kiani, Maia Kinnebrew, Matthew N Idso, Naomi Baxter, Evelyn Chang, Emily Aye and 7 more

Open access · greenAbstract read
In one paragraph

Article in Biophysical journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 39% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

17 authors at 2 institutions in 1 country.

Chung-Ta HanDepartment of Chemical Engineering, University of California, Santa Barbara, Santa Barbara, California.
Khanh Dinh Quoc NguyenDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, Santa Barbara, California.
Maxwell W BerkowDepartment of Chemical Engineering, University of California, Santa Barbara, Santa Barbara, California.
Sunyia HussainDepartment of Chemical Engineering, University of California, Santa Barbara, Santa Barbara, California.
Ahmad KianiC. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, West Virginia.
Maia KinnebrewCollege of Creative Studies, Biology Department, University of California, Santa Barbara, Santa Barbara, California.
Matthew N IdsoDepartment of Chemical Engineering, University of California, Santa Barbara, Santa Barbara, California.
Naomi BaxterDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, Santa Barbara, California.
Evelyn ChangDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, Santa Barbara, California.
Emily AyeDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, Santa Barbara, California.
Elsa WinslowDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, Santa Barbara, California.
Mohammad RahmanC. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, West Virginia.
Susanna SeppäläDepartment of Chemical Engineering, University of California, Santa Barbara, Santa Barbara, California.
Michelle A O'MalleyDepartment of Chemical Engineering, University of California, Santa Barbara, Santa Barbara, California.
Bradley F ChmelkaDepartment of Chemical Engineering, University of California, Santa Barbara, Santa Barbara, California.
Blake MertzC. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, West Virginia.
Songi HanDepartment of Chemical Engineering, University of California, Santa Barbara, Santa Barbara, California; Department of Chemistry and Biochemistry, University of California, Santa Barbara, Santa Barbara, California. Electronic address: songi@chem.ucsb.edu.
University of California, Santa Barbara · USWest Virginia University · US

Funding

Water as essential building blocks to direct protein structure and functionR35GM136411 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI Songi Han · 2020 to 2026
$2.4M
NIGMS NIH HHS R35 GM136411
6 · The paper itself

Abstract

The functional properties of proteorhodopsin (PR) have been found to be strongly modulated by oligomeric distributions and lipid membrane mimetics. This study aims to distinguish and explain their effects by investigating how oligomer formation impacts PR's function of proton transport in lipid-based membrane mimetic environments. We find that PR forms stable hexamers and pentamers in both E. coli membranes and synthetic liposomes. Compared with the monomers, the photocycle kinetics of PR oligomers is ∼2 and ∼4.5 times slower for transitions between the K and M and the M and N photointermediates, respectively, indicating that oligomerization significantly slows PR's rate of proton transport in liposomes. In contrast, the apparent pKa of the key proton acceptor residue D97 (pKa

Indexed as

Escherichia coliLiposomesLipidsProtonsRhodopsins, MicrobialLipidsLiposomesproteorhodopsinProtonsRhodopsins, Microbial

Identifiers

PMID36352784
PMCPMC9822798
OpenAlexW4308682562

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.