Evidence map›Paper›PMID 16227429›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Evolutionary conservation and diversification of Rh family genes and proteins.

Cheng-Han Huang, Jianbin Peng

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

48 citing papers in PubMed, 143 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Expression and Functional Analysis ofAnimals : an open access journal from MDPI · 2023
    Article
  7. Article
  8. Article
  9. Mechanisms of NaFrontiers in physiology · 2022
    Review
  10. Article
  11. Article
  12. The lipid environment determines the activity of the Escherichia coli ammonium transporter AmtB.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  13. Article
  14. Article
  15. Heads you gain, tails you lose.American journal of physiology. Regulatory, integrative and comparative physiology · 2017
    Article
  16. Article
  17. Article
  18. Ammonia as a Potential Neurotoxic Factor in Alzheimer's Disease.Frontiers in molecular neuroscience · 2016
    Review
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Cheng-Han HuangLaboratory of Biochemistry and Molecular Genetics, Lindsley F. Kimball Research Institute, New York Blood Center, 310 East 67th Street, New York, NY 10021, USA. chuang@nybloodcenter.org
Jianbin Peng
New York Blood Center · US

Funding

RH PROTEIN AND THE RH BLOOD GROUP SYSTEMR01HL066274 · NHLBI · NEW YORK BLOOD CENTER · PI HUANG, CHEN-HAN · 2001 to 2004
$1.4M
NHLBI NIH HHS HL 66274NHLBI NIH HHS R01 HL066274NICHD NIH HHS HD 62704
6 · The paper itself

Abstract

Rhesus (Rh) proteins were first identified in human erythroid cells and recently in other tissues. Like ammonia transporter (Amt) proteins, their only homologues, Rh proteins have the 12 transmembrane-spanning segments characteristic of transporters. Many think Rh and Amt proteins transport the same substrate, NH(3)/NH(4)(+), whereas others think that Rh proteins transport CO(2) and Amt proteins NH(3). In the latter view, Rh and Amt are different biological gas channels. To reconstruct the phylogeny of the Rh family and study its coexistence with and relationship to Amt in depth, we analyzed 111 Rh genes and 260 Amt genes. Although Rh and Amt are found together in organisms as diverse as unicellular eukaryotes and sea squirts, Rh genes apparently arose later, because they are rare in prokaryotes. However, Rh genes are prominent in vertebrates, in which Amt genes disappear. In organisms with both types of genes, Rh had apparently diverged away from Amt rapidly and then evolved slowly over a long period. Functionally divergent amino acid sites are clustered in transmembrane segments and around the gas-conducting lumen recently identified in Escherichia coli AmtB, in agreement with Rh proteins having new substrate specificity. Despite gene duplications and mutations, the Rh paralogous groups all have apparently been subject to strong purifying selection indicating functional conservation. Genes encoding the classical Rh proteins in mammalian red cells show higher nucleotide substitution rates at nonsynonymous codon positions than other Rh genes, a finding that suggests a possible role for these proteins in red cell morphogenetic evolution.

Indexed as

Biological EvolutionAmino Acid SequenceAmmoniaBase SequenceCarbon DioxideCation Transport ProteinsMolecular Sequence DataMultigene FamilyRh-Hr Blood-Group SystemAmmoniaCarbon DioxideCation Transport ProteinsRh-Hr Blood-Group System

Identifiers

PMID16227429
PMCPMC1266151
OpenAlexW2063449571

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.