Evidence map›Paper›PMID 10839820›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2000

A functional-phylogenetic classification system for transmembrane solute transporters.

M H Saier

Open access · greenAbstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 288 papers.

0numbers the graph read from it
0cells of the map it votes in
288citing papers in PubMed
23.4field-weighted citation impact, top 1% 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

288 citing papers in PubMed, 820 citations in OpenAlex.

  1. Review
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  11. Bacteria Under Metal Stress-Molecular Mechanisms of Metal Tolerance.International journal of molecular sciences · 2025
    Review
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  14. What Can Be Learned by Knowing Only the Amino Acid Composition of Proteins?International journal of molecular sciences · 2024
    Article
  15. Article
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  18. Review
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  20. Article

228 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

1 author at 1 institution in 1 country.

M H SaierDepartment of Biology, University of California at San Diego, La Jolla, California 92093-0116, USA. msaier@ucsd.edu
University of California, San Diego · US

Funding

ATP DEPENDENT PROTEIN KINASES IN GRAM POSITIVE BACTERIAR01GM055434 · NIGMS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI SAIER, MILTON H. · 1997 to 2004
$1.1M
ATP-DEPENDENT PROTEIN KINASES IN STREPTOCOCCIR01AI021702 · NIAID · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI SAIER, MILTON H. · 1985 to 1996
–
NIAID NIH HHS 5RO1 AI21702NIGMS NIH HHS 9RO1 GM55434NIGMS NIH HHS R01 GM055434
6 · The paper itself

Abstract

A comprehensive classification system for transmembrane molecular transporters has been developed and recently approved by the transport panel of the nomenclature committee of the International Union of Biochemistry and Molecular Biology. This system is based on (i) transporter class and subclass (mode of transport and energy coupling mechanism), (ii) protein phylogenetic family and subfamily, and (iii) substrate specificity. Almost all of the more than 250 identified families of transporters include members that function exclusively in transport. Channels (115 families), secondary active transporters (uniporters, symporters, and antiporters) (78 families), primary active transporters (23 families), group translocators (6 families), and transport proteins of ill-defined function or of unknown mechanism (51 families) constitute distinct categories. Transport mode and energy coupling prove to be relatively immutable characteristics and therefore provide primary bases for classification. Phylogenetic grouping reflects structure, function, mechanism, and often substrate specificity and therefore provides a reliable secondary basis for classification. Substrate specificity and polarity of transport prove to be more readily altered during evolutionary history and therefore provide a tertiary basis for classification. With very few exceptions, a phylogenetic family of transporters includes members that function by a single transport mode and energy coupling mechanism, although a variety of substrates may be transported, sometimes with either inwardly or outwardly directed polarity. In this review, I provide cross-referencing of well-characterized constituent transporters according to (i) transport mode, (ii) energy coupling mechanism, (iii) phylogenetic grouping, and (iv) substrates transported. The structural features and distribution of recognized family members throughout the living world are also evaluated. The tabulations should facilitate familial and functional assignments of newly sequenced transport proteins that will result from future genome sequencing projects.

Indexed as

PhylogenyAnimalsBiological TransportCarrier ProteinsCell MembraneHumansIon ChannelsProtein ConformationSubstrate SpecificityTerminology as TopicToxins, BiologicalCarrier ProteinsIon ChannelsToxins, Biological

Identifiers

PMID10839820
PMCPMC98997
OpenAlexW2109318635

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.