Evidence map›Paper›PMID 23832211›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013

X-ray diffraction studies on merohedrally twinned Δ1-62NtNBCe1-A crystals of the sodium/bicarbonate cotransporter.

Harindarpal S Gill, Lauren Dutcher, Walter F Boron, Samir Patel, Lisa M Guay-Woodford

Abstract readComparative Study
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. 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

5 authors.

Harindarpal S GillDepartment of Medicine, The George Washington University, Washington, DC 20052, USA. hgill@gwu.edu
Lauren Dutcher
Walter F Boron
Samir Patel
Lisa M Guay-Woodford

Funding

PH REGULATION OF EXCITABLE INVERTEBRATE CELLSR01NS018400 · NINDS · YALE UNIVERSITY · PI BORON, WALTER F · 1985 to 2012
$5.1M
Physiology of Electrogenic Na/HCO3 CotransportersR37DK030344 · NIDDK · YALE UNIVERSITY · PI BORON, WALTER F · 2002 to 2011
$3.5M
Structure-function studies of the dimerization of the N-terminal domain of NBCe1-K01DK082646 · NIDDK · GEORGE WASHINGTON UNIVERSITY · PI GILL, HARRY SINGH · 2009 to 2014
$704k
NIDDK NIH HHS K01 DK082646NIDDK NIH HHS R37 DK030344NIDDK NIH HHS R37 DK30344NINDS NIH HHS R01 NS018400NINDS NIH HHS R01 NS18400
6 · The paper itself

Abstract

NBCe1-A membrane-embedded macromolecules that cotransport sodium and bicarbonate ions across the bilayer serve to maintain acid-base homeostasis throughout the body. Defects result in a number of renal and eye disorders, including type-II renal tubular acidosis and cataracts. Here, crystals of a human truncated mutant of the cytoplasmic N-terminal domain of NBCe1 (Δ1-62NtNBCe1-A) are reported that diffract X-rays to 2.4 Å resolution. The crystal symmetry of Δ1-62NtNBCe1-A is of space group P31 with pseudo-P3121 symmetry and it has a hemihedral twin fraction of 33.0%. The crystals may provide insight into the pathogenic processes observed in a subset of patients with truncating and point mutations in the gene encoding NBCe1.

Indexed as

X-Ray DiffractionAnisotropyBicarbonatesCrystallizationHumansMutant ProteinsMutationProtein Structure, TertiaryRecombinant ProteinsSequence DeletionSodiumSodium-Bicarbonate SymportersBicarbonatesMutant ProteinsRecombinant ProteinsSLC4A4 protein, humanSodiumSodium-Bicarbonate Symportersbicarbonate transportNBCe1

Identifiers

PMID23832211
PMCPMC3702328

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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.