Evidence map›Paper›PMID 15014910›Full record

ReviewThe Journal of membrane biology2004

Molecular mechanisms of electrogenic sodium bicarbonate cotransport: structural and equilibrium thermodynamic considerations.

I Kurtz, D Petrasek, S Tatishchev

Abstract readReview
PubMed Publisher
In one paragraph

Review in The Journal of membrane biology, 2004. 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
–field-weighted citation impact
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.

  1. Review
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  11. Article
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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.

I KurtzDivision of Nephrology, David Geffen School of Medicine at UCLA, Los Angeles, California 90095-1689, USA. ikurtz@mednet.ucla.edu
D Petrasek
S Tatishchev

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
Physiological Model of Parathyroid Hormone SecretionK08DK060071 · NIDDK · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI PETRASEK, DANNY · 2002 to 2006
$675k
NIDDK NIH HHS DK07789NIDDK NIH HHS DK58563NIDDK NIH HHS DK60071NIDDK NIH HHS DK63125
6 · The paper itself

Abstract

The electrogenic Na(+)-HCO(3)(-) cotransporters play an essential role in regulating intracellular pH and extracellular acid-base homeostasis. Of the known members of the bicarbonate transporter superfamily (BTS), NBC1 and NBC4 proteins have been shown to be electrogenic. The electrogenic nature of these transporters results from the unequal coupling of anionic and cationic fluxes during each transport cycle. This unique property distinguishes NBC1 and NBC4 proteins from other sodium bicarbonate cotransporters and members of the bicarbonate transporter superfamily that are known to be electroneutral. Structure-function studies have played an essential role in revealing the basis for the modulation of the coupling ratio of NBC1 proteins. In addition, the recent transmembrane topographic analysis of pNBC1 has shed light on the potential structural determinants that are responsible for ion permeation through the cotransporter. The experimentally difficult problem of determining the nature of anionic species being transported by these proteins (HCO(3)(-) versus CO(3)(2-)) is analyzed using a theoretical equilibrium thermodynamics approach. Finally, our current understanding of the molecular mechanisms responsible for the regulation of ion coupling and flux through electrogenic sodium bicarbonate cotransporters is reviewed in detail.

Indexed as

Acid-Base EquilibriumAmino Acid SequenceAnimalsBiological TransportGene ExpressionHumansMolecular Sequence DataProtein BindingProtein IsoformsRatsSequence AlignmentSequence Homology, Amino AcidSodium BicarbonateSodium-Bicarbonate SymportersStructure-Activity RelationshipThermodynamicsProtein IsoformsSodium BicarbonateSodium-Bicarbonate Symporters

Identifiers

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.