Evidence map›Paper›PMID 36100040›Full record

ReviewThe Journal of biological chemistry2022

Still rocking in the structural era: A molecular overview of the small multidrug resistance (SMR) transporter family.

Olive E Burata, Trevor Justin Yeh, Christian B Macdonald, Randy B Stockbridge

Open access · goldAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.8field-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

25 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Protonated Structure of EmrE Reveals C-terminal Tail Gating Mechanism.bioRxiv : the preprint server for biology · 2026
    Article
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  17. Peripheral positions encode transport specificity in the small multidrug resistance exporters.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  18. Article
  19. Conformational free-energy landscapes of a NaProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. A Small Multidrug Resistance Transporter inbioRxiv : the preprint server for biology · 2024
    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 at 1 institution in 1 country.

Olive E BurataProgram in Chemical Biology, University of Michigan, Ann Arbor, Michigan, USA.
Trevor Justin YehProgram in Biophysics, University of Michigan, Ann Arbor, Michigan, USA.
Christian B MacdonaldProgram in Biophysics, University of Michigan, Ann Arbor, Michigan, USA.
Randy B StockbridgeProgram in Chemical Biology, University of Michigan, Ann Arbor, Michigan, USA; Program in Biophysics, University of Michigan, Ann Arbor, Michigan, USA; Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan, USA. Electronic address: stockbr@umich.edu.
University of Michigan · US

Funding

Structural and functional analysis of novel microbial membrane proteinsR35GM128768 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Randy B. Stockbridge · 2018 to 2026
$3.7M
NIGMS NIH HHS R35 GM128768
6 · The paper itself

Abstract

The small multidrug resistance (SMR) family is composed of widespread microbial membrane proteins that fulfill different transport functions. Four functional SMR subtypes have been identified, which variously transport the small, charged metabolite guanidinium, bulky hydrophobic drugs and antiseptics, polyamines, and glycolipids across the membrane bilayer. The transporters possess a minimalist architecture, with ∼100-residue subunits that require assembly into homodimers or heterodimers for transport. In part because of their simple construction, the SMRs are a tractable system for biochemical and biophysical analysis. Studies of SMR transporters over the last 25 years have yielded deep insights for diverse fields, including membrane protein topology and evolution, mechanisms of membrane transport, and bacterial multidrug resistance. Here, we review recent advances in understanding the structures and functions of SMR transporters. New molecular structures of SMRs representing two of the four functional subtypes reveal the conserved structural features that have permitted the emergence of disparate substrate transport functions in the SMR family and illuminate structural similarities with a distantly related membrane transporter family, SLC35/DMT.

Indexed as

ATP-Binding Cassette, Sub-Family C ProteinsDrug Resistance, MultipleMembrane Transport ProteinsBiological TransportMembrane ProteinsProtein ConformationATP-Binding Cassette, Sub-Family C ProteinsMembrane ProteinsMembrane Transport Proteinsevolutionflippaseguanidiniummembrane transportmultidrug transporterpolyaminequaternary ammonium cationsSLC35structure-functionsubstrate specificity

Identifiers

PMID36100040
PMCPMC9574504
OpenAlexW4295241432

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.