Evidence map›Paper›PMID 8786953›Full record

ReviewPharmaceutical research1995

Biology of membrane transport proteins.

W Sadée, V Drübbisch, G L Amidon

Abstract readReview
PubMed Publisher
In one paragraph

Review in Pharmaceutical research, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

14 citing papers in PubMed, 53 citations in OpenAlex.

  1. Trial
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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

3 authors at 1 institution in 1 country.

W SadéeSchool of Pharmacy, University of California, San Francisco 94143-0446, USA.
V Drübbisch
G L Amidon
University of California, San Francisco · US

Funding

USE OF MUCCOSAL CELL CARRIERS/EYZYMES IN ORAL ABSORPTIONR01GM037188 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI AMIDON, GORDON L · 1986 to 2013
$4.4M
NIGMS NIH HHS GM37188
6 · The paper itself

Abstract

Membrane transporter proteins are encoded by numerous genes that can be classified into several superfamilies, on the basis of sequence identity and biological function. Prominent examples include facilitative transporters, the secondary active symporters and antiporters driven by ion gradients, and active ABC (ATP binding cassette) transporters involved in multiple-drug resistance and targeting of antigenic peptides to MHC Class I molecules. Transported substrates range from nutrients and ions to a broad variety of drugs, peptides and proteins. Deleterious mutations of transporter genes may lead to genetic diseases or loss of cell viability. Transporter structure, function and regulation, genetic factors, and pharmaceutical implications are summarized in this review.

Indexed as

AnimalsATP-Binding Cassette TransportersCloning, MolecularDopamineMolecular StructureSequence AnalysisATP-Binding Cassette TransportersDopamine

Identifiers

PMID8786953
OpenAlexW7258459

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.