ReviewThe Biochemical journal2007
Structural and functional analysis of the Na+/H+ exchanger.
Review in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.
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.
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.
Who cites it
104 citing papers in PubMed, 246 citations in OpenAlex.
- Cryo-EM structure of human NaNature communications · 2026Article
- Revising NHE-1: From Cardiac Homeostasis to Heart Failure and Future Drug Development.Cell biochemistry and function · 2026Review
- Discovery of vasodilatory effects of NaActa pharmacologica Sinica · 2026Article
- Cystinosin regulates NaEMBO reports · 2026Article
- Review
- NaCells · 2025Article
- Structural and Functional Characterization of the Vacuolar-Type NaBiomolecules · 2025Article
- Rational design of tunable pH switches through shadow-strand hybridization-actuated displacement engineering.Nucleic acids research · 2025Article
- Structure and Inhibition of the Human NaInternational journal of molecular sciences · 2025Article
- PIPNature communications · 2025Article
- Cystinosin is involved in NabioRxiv : the preprint server for biology · 2025Article
- CARMIL1-AA selectively inhibits macropinocytosis while sparing autophagy.Molecular biology of the cell · 2025Article
- Hexamethylene amiloride induces lysosome-mediated cell death in multiple myeloma through transcription factor E3.Cell death discovery · 2024Article
- The Renoprotective Mechanisms of Sodium-Glucose Cotransporter-2 Inhibitors (SGLT2i)-A Narrative Review.International journal of molecular sciences · 2024Review
- Carbonic anhydrase, its inhibitors and vascular function.Frontiers in molecular biosciences · 2024Review
- ATP-mediated increase in HJournal of neurophysiology · 2024Article
- The SLC9C2 Gene Product (NaInternational journal of molecular sciences · 2023Article
- Acid-sensing ion channel blocker diminazene facilitates proton-induced excitation of afferent nerves in a similar manner that NaFrontiers in cellular neuroscience · 2023Article
- Lactate metabolism in human health and disease.Signal transduction and targeted therapy · 2022Review
- The Remaining Conundrum of the Role of the NaReviews in cardiovascular medicine · 2022Review
44 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mammalian NHE (Na+/H+ exchanger) is a ubiquitously expressed integral membrane protein that regulates intracellular pH by removing a proton in exchange for an extracellular sodium ion. Of the nine known isoforms of the mammalian NHEs, the first isoform discovered (NHE1) is the most thoroughly characterized. NHE1 is involved in numerous physiological processes in mammals, including regulation of intracellular pH, cell-volume control, cytoskeletal organization, heart disease and cancer. NHE comprises two domains: an N-terminal membrane domain that functions to transport ions, and a C-terminal cytoplasmic regulatory domain that regulates the activity and mediates cytoskeletal interactions. Although the exact mechanism of transport by NHE1 remains elusive, recent studies have identified amino acid residues that are important for NHE function. In addition, progress has been made regarding the elucidation of the structure of NHEs. Specifically, the structure of a single TM (transmembrane) segment from NHE1 has been solved, and the high-resolution structure of the bacterial Na+/H+ antiporter NhaA has recently been elucidated. In this review we discuss what is known about both functional and structural aspects of NHE1. We relate the known structural data for NHE1 to the NhaA structure, where TM IV of NHE1 shows surprising structural similarity with TM IV of NhaA, despite little primary sequence similarity. Further experiments that will be required to fully understand the mechanism of transport and regulation of the NHE1 protein are discussed.
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Registered trials
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.