Evidence map›Paper›PMID 11274128›Full record

ArticleJournal of bacteriology2001

Twelve-transmembrane-segment (TMS) version (DeltaTMS VII-VIII) of the 14-TMS Tet(L) antibiotic resistance protein retains monovalent cation transport modes but lacks tetracycline efflux capacity.

J Jin, A A Guffanti, C Beck, T A Krulwich

Abstract read
In one paragraph

Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Review
  3. Regulation of Amino Acid Transport in Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2019
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Alkaline pH homeostasis in bacteria: new insights.Biochimica et biophysica acta · 2005
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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.

J JinDepartment of Biochemistry and Molecular Biology, Mount Sinai School of Medicine, New York, New York 10029, USA.
A A Guffanti
C Beck
T A Krulwich

Funding

Tet Efflux Proteins: Implications of Multiple FunctionsR01GM052837 · NIGMS · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI KRULWICH, TERRY ANN · 1996 to 2004
$1.2M
NIGMS NIH HHS GM52837NIGMS NIH HHS R01 GM052837
6 · The paper itself

Abstract

A "Tet(L)-12" version of Tet(L), a tetracycline efflux protein with 14 transmembrane segments (TMS), was constructed by deletion of two central TMS. Tet(L)-12 catalyzed Na+/H+ antiport and antiport with K+ as a coupling ion as well as or better than wild-type Tet(L) but exhibited no tetracycline-Me2+/H+ antiport in Escherichia coli vesicles.

Indexed as

Escherichia coli ProteinsTetracycline ResistanceAmino Acid SequenceAntiportersBacterial ProteinsCarrier ProteinsEscherichia coliGene DeletionHydrogenIon TransportMembrane ProteinsMolecular Sequence DataMutationPotassiumSodiumSodium-Hydrogen ExchangersAntiportersBacterial ProteinsCarrier ProteinsEscherichia coli ProteinsHydrogenMembrane ProteinsPotassiumSodiumSodium-Hydrogen Exchangerstet(K) protein, Staphylococcus aureusTet(L) protein, E coliTetracycline

Identifiers

PMID11274128
PMCPMC95185

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.