Evidence map›Paper›PMID 11872735›Full record

ArticleJournal of bacteriology2002

Site-directed mutagenesis studies of selected motif and charged residues and of cysteines of the multifunctional tetracycline efflux protein Tet(L).

Jie Jin, Terry A Krulwich

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

8 citing papers in PubMed, 19 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Jie JinDepartment of Pharmacology and Biological Chemistry, Mount Sinai School of Medicine, New York, New York 10029, USA.
Terry A Krulwich
Icahn School of Medicine at Mount Sinai · US

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

All of the transmembrane glutamates of Tet(L) are essential for tetracycline (TET) resistance, and E397 has been shown to be essential for all catalytic modes, i.e., TET-Me(2+) and Na(+) efflux and K(+) uptake. Loop residues D74 and G70 are essential for TET flux but not for Na(+) or K(+) flux. A cysteineless Tet(L) protein exhibits all activities.

Indexed as

Escherichia coli ProteinsAntiportersCysteineEscherichia coliGlutamatesIon TransportMembrane ProteinsMutagenesis, Site-DirectedPotassiumSodiumTetracycline ResistanceAntiportersCysteineEscherichia coli ProteinsGlutamatesMembrane ProteinsPotassiumSodiumTet(L) protein, E coli

Identifiers

PMID11872735
PMCPMC134896
OpenAlexW2068742211

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.