Evidence map›Paper›PMID 23506896›Full record

ReviewMolecular aspects of medicine

Characteristics of mammalian Rh glycoproteins (SLC42 transporters) and their role in acid-base transport.

Nazih L Nakhoul, L Lee Hamm

Open access · greenAbstract readReview
In one paragraph

Review in Molecular aspects of medicine. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

20 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Cognitive Effects ofPathogens (Basel, Switzerland) · 2024
    Article
  6. Article
  7. Article
  8. NBCe1-A is required for the renal ammonia and KAmerican journal of physiology. Renal physiology · 2020
    Article
  9. Acid-Base Basics.Seminars in nephrology · 2019
    Review
  10. Applied and environmental microbiology · 2016
    Article
  11. Article
  12. Acid-Base Homeostasis.Clinical journal of the American Society of Nephrology : CJASN · 2015
    Review
  13. Mechanisms of ammonia and ammonium transport by rhesus-associated glycoproteins.American journal of physiology. Cell physiology · 2015
    Article
  14. Effect of dietary protein restriction on renal ammonia metabolism.American journal of physiology. Renal physiology · 2015
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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.

Nazih L NakhoulDepartment of Medicine, Section of Nephrology, Tulane Hypertension and Renal Center of Excellence, Tulane University School of Medicine New Orleans, LA 70112, United States. nakhoul@tulane.edu
L Lee Hamm
Tulane University · US

Funding

Membrane Transport of NH3 and NH4+R01DK062295 · NIDDK · TULANE UNIVERSITY OF LOUISIANA · PI NAKHOUL, NAZIH · 2003 to 2008
$1.5M
NIDDK NIH HHS R01 DK062295NIDDK NIH HHS R01-DK-6229
6 · The paper itself

Abstract

The mammalian Rh glycoproteins belong to the solute transporter family SLC42 and include RhAG, present in red blood cells, and two non-erythroid members RhBG and RhCG that are expressed in various tissues, including kidney, liver, skin and the GI tract. The Rh proteins in the red blood cell form an "Rh complex" made up of one D-subunit, one CE-subunit and two RhAG subunits. The Rh complex has a well-known antigenic effect but also contributes to the stability of the red cell membrane. RhBG and RhCG are related to the NH4(+) transporters of the yeast and bacteria but their exact function is yet to be determined. This review describes the expression and molecular properties of these membrane proteins and their potential role as NH3/NH4(+) and CO2 transporters. The likelihood that these proteins transport gases such as CO2 or NH3 is novel and significant. The review also describes the physiological importance of these proteins and their relevance to human disease.

Indexed as

Models, MolecularBlood ProteinsCarbon DioxideCation Transport ProteinsGlycoproteinsHumansMembrane GlycoproteinsMembrane Transport ProteinsModels, GeneticMultigene FamilyProtein ConformationQuaternary Ammonium CompoundsSkinSubstrate SpecificityVisceraBlood ProteinsCarbon DioxideCation Transport ProteinsGlycoproteinsMembrane GlycoproteinsMembrane Transport ProteinsQuaternary Ammonium CompoundsRHAG protein, humanRHBG protein, humanRHCG protein, human

Identifiers

PMID23506896
PMCPMC3602798
OpenAlexW2054886733

What OpenQuestion holds

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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.