Evidence map›Paper›PMID 22226846›Full record

ReviewInternational journal of medical microbiology : IJMM2012

Structure and function of OprD protein in Pseudomonas aeruginosa: from antibiotic resistance to novel therapies.

Hui Li, Yi-Feng Luo, Bryan J Williams, Timothy S Blackwell, Can-Mao Xie

Abstract readReview
In one paragraph

Review in International journal of medical microbiology : IJMM, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
130citing papers in PubMed, 1 pooled it
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

130 citing papers in PubMed, 1 synthesis or guideline pooled it, 247 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Characterization of two exoUBMC microbiology · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. TXA11114: Discovery of anAntibiotics (Basel, Switzerland) · 2026
    Article
  9. Review
  10. Antibiotic resistance inFrontiers in microbiology · 2026
    Review
  11. Within-host adaptation mutations associated with persistent colonization ofFrontiers in cellular and infection microbiology · 2026
    Article
  12. Whole-genome sequencing reveals molecular characterization of carbapenem-resistantFrontiers in cellular and infection microbiology · 2026
    Article
  13. Article
  14. Understanding Drug Permeability inLife (Basel, Switzerland) · 2025
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

70 more citing papers are in PubMed but not listed here.

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

5 authors at 4 institutions in 2 countries.

Hui LiDivision of Respiratory Medicine, The First Affiliated Hospital of Sun Yat-sen University, Guangzhou, Guangdong 510080, China.
Yi-Feng Luo
Bryan J Williams
Timothy S Blackwell
Can-Mao Xie
Sun Yat-sen University · CNThe First Affiliated Hospital, Sun Yat-sen University · CNUniversity of Minnesota · USVanderbilt University Medical Center · US

Funding

MOLECULAR REGULATION OF LUNG INFLAMMATION BY NF-KBR01HL061419 · NHLBI · VANDERBILT UNIVERSITY · PI BLACKWELL, TIMOTHY S · 1999 to 2006
$1.5M
NHLBI NIH HHS R01 HL061419
6 · The paper itself

Abstract

Pseudomonas aeruginosa (P. aeruginosa) is a common pathogen isolated from patients with nosocomial infections. Due to its intrinsic and acquired antimicrobial resistance, limited classes of antibiotics can be used for the treatment of infection with P. aeruginosa. Of these, the carbapenems are very important; however, the occurrence of carbapenem-resistant strains is gradually increasing over time. Deficiency of the outer membrane protein OprD confers P. aeruginosa a basal level of resistance to carbapenems, especially to imipenem. Functional studies have revealed that loops 2 and 3 in the OprD protein contain the entrance and/or binding sites for imipenem. Therefore, any mutation in loop 2 and/or loop 3 that causes conformational changes could result in carbapenem resistance. OprD is also a common channel for some amino acids and peptides, and competition with carbapenems through the channel may also occur. Furthermore, OprD is a highly regulated protein at transcriptional and post-transcriptional levels by some metals, small bioactive molecules, amino acids, and efflux pump regulators. Because of its hypermutability and highly regulated properties, OprD is thought to be the most prevalent mechanism for carbapenem resistance in P. aeruginosa. Developing new strategies to combat infection with carbapenem-resistant P. aeruginosa lacking OprD is an ongoing challenge.

Indexed as

Amino AcidsBiological TransportDrug Resistance, BacterialGene Expression Regulation, BacterialHumansImipenemPorinsPseudomonas aeruginosaPseudomonas InfectionsAmino AcidsImipenemOprD protein, Pseudomonas aeruginosaPorins

Identifiers

PMID22226846
PMCPMC3831278
OpenAlexW2044584162

What OpenQuestion holds

Textmetadata
LicenceTDM
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.