Evidence map›Paper›PMID 15817634›Full record

ArticleThe Journal of physiology2005

Critical amino acid residues involved in the electrogenic sodium-bicarbonate cotransporter kNBC1-mediated transport.

Natalia Abuladze, Rustam Azimov, Debra Newman, Pakan Sassani, Weixin Liu, Sergei Tatishchev, Alexander Pushkin, Ira Kurtz

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

25 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Cation-coupled bicarbonate transporters.Comprehensive Physiology · 2014
    Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. SLC4A transporters.Current topics in membranes · 2012
    Article
  14. Article
  15. Article
  16. Defective membrane expression of the Na(+)-HCO(3)(-) cotransporter NBCe1 is associated with familial migraine.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  17. Article
  18. Article
  19. Modular structure of sodium-coupled bicarbonate transporters.The Journal of experimental biology · 2009
    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

8 authors at 1 institution in 1 country.

Natalia AbuladzeDivision of Nephrology, David Geffen School of Medicine at UCLA, 10833 Le Conte Avenue, Room 7-155 Factor Building, Los Angeles, CA 90095, USA.
Rustam Azimov
Debra Newman
Pakan Sassani
Weixin Liu
Sergei Tatishchev
Alexander Pushkin
Ira Kurtz
University of California, Los Angeles · US

Funding

BIOLOGY OF SODIUM BICARBONATE TRANSPORTR01DK058563 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KURTZ, IRA · 2001 to 2011
$3.1M
Modulation of Electrogenic Sodium Bicarbonate TransportR01DK063125 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KURTZ, IRA · 2003 to 2007
$1.8M
NEPHROLOGY SCIENTIST TRAINING GRANTT32DK007789 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KURTZ, IRA · 2000 to 2017
$1.5M
NIDDK NIH HHS DK07789NIDDK NIH HHS DK58563NIDDK NIH HHS DK63125NIDDK NIH HHS R01 DK058563NIDDK NIH HHS R01 DK063125NIDDK NIH HHS T32 DK007789
6 · The paper itself

Abstract

We have previously reported a topological model of the electrogenic Na(+)-HCO(3)(-) cotransporter (NBC1) in which the cotransporter spans the plasma membrane 10 times with N- and C-termini localized intracellularly. An analysis of conserved amino acid residues among members of the SLC4 superfamily in both the transmembrane segments (TMs) and intracellular/extracellular loops (ILs/ELs) provided the basis for the mutagenesis approach taken in the present study to determine amino acids involved in NBC1-mediated ion transport. Using large-scale mutagenesis, acidic and basic amino acids putatively involved in ion transport mediated by the predominant variant of NBC1 expressed in the kidney (kNBC1) were mutated to neutral and/or oppositely charged amino acids. All mutant kNBC1 cotransporters were expressed in HEK-293T cells and the Na(+)-dependent base flux of the mutants was determined using intracellular pH measurements with 2',7'-bis-(carboxyethyl)-5(6)-carboxyfluorescein (BCECF). Critical glutamate, aspartate, lysine, arginine and histidine residues in ILs/ELs and TMs were detected that were essential for kNBC1-mediated Na(+)-dependent base transport. In addition, critical phenylalanine, serine, tyrosine, threonine and alanine residues in TMs and ILs/ELs were detected. Furthermore, several amino acid residues in ILs/ELs and TMs were shown to be essential for membrane targeting. The data demonstrate asymmetry of distribution of kNBC1 charged amino acids involved in ion recognition in putative outward-facing and inward-facing conformations. A model summarizing key amino acid residues involved in kNBC1-mediated ion transport is presented.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionBicarbonatesCell LineElectrochemistryHumansKidneyMolecular Sequence DataMutagenesis, Site-DirectedProtein Structure, TertiarySodiumSodium-Bicarbonate SymportersBicarbonatesSLC4A4 protein, humanSodiumSodium-Bicarbonate Symporters

Identifiers

PMID15817634
PMCPMC1464572
OpenAlexW1532109973

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.