ArticleActa crystallographica. Section F, Structural biology and crystallization communications2005
Crystallization and preliminary crystallographic analysis of the human calcineurin homologous protein CHP2 bound to the cytoplasmic region of the Na+/H+ exchanger NHE1.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- A Novel Peptide Prevents Enterotoxin- and Inflammation-Induced Intestinal Fluid Secretion by Stimulating Sodium-Hydrogen Exchanger 3 Activity.Gastroenterology · 2023Article
- Involvement of CHP2 in the Development of Non-Small Cell Lung Cancer and Patients' Poor Prognosis.Applied immunohistochemistry & molecular morphology : AIMM · 2020Article
- Trafficking Ion Transporters to the Apical Membrane of Polarized Intestinal Enterocytes.Cold Spring Harbor perspectives in biology · 2018Review
- NHE3 regulatory complexes.The Journal of experimental biology · 2009Review
- Crystal structure of CHP2 complexed with NHE1-cytosolic region and an implication for pH regulation.The EMBO journal · 2006Article
- SLC9/NHE gene family, a plasma membrane and organellar family of Na⁺/H⁺ exchangers.Molecular aspects of medicineReview
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calcineurin homologous protein (CHP) is a Ca2+-binding protein that directly interacts with and regulates the activity of all plasma-membrane Na+/H+-exchanger (NHE) family members. In contrast to the ubiquitous isoform CHP1, CHP2 is highly expressed in cancer cells. To understand the regulatory mechanism of NHE1 by CHP2, the complex CHP2-NHE1 (amino acids 503-545) has been crystallized by the sitting-drop vapour-diffusion method using PEG 3350 as precipitant. The crystals diffract to 2.7 A and belong to a tetragonal space group, with unit-cell parameters a = b = 49.96, c = 103.20 A.
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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.