ArticleThe protein journal2006
Molecular cloning, sequence, function and structural basis of human heart 150 kDa oxygen-regulated protein, an ER chaperone.
Article in The protein journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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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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.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- ER proteostasis failure in HYOU1 deficiency alters B cells, neutrophils, and interferon signalling.Journal of human immunity · 2026Article
- Circular RNA 0025984 Ameliorates Ischemic Stroke Injury and Protects Astrocytes Through miR-143-3p/TET1/ORP150 Pathway.Molecular neurobiology · 2021Article
- Biological Function of HYOU1 in Tumors and Other Diseases.OncoTargets and therapy · 2021Review
- The role of heat shock proteins in atherosclerosis.Nature reviews. Cardiology · 2014Review
- HIV-1 Vpr modulates macrophage metabolic pathways: a SILAC-based quantitative analysis.PloS one · 2013Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Apoptosis of heart tissues followed by hypoxia and ischemia leads finally to cardiac insufficiency. The full-length coding sequence of 3301 bp including cDNA(s) of the ER chaperone ORP150, which was specifically induced by hypoxia stress, was cloned from human cardiac infarct. Phylogenetic analyses reveal that human heart ORP150 shares a highly conserved N-terminal ATPase domain among its related family members. Moreover, hydropathic profiling reveals that their ca. 70 N-terminal residues and unique C-terminal halves exhibit similar hydropathy profiles among members. These findings suggest that ORP150 is structurally and functionally well conserved in distant species.
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Registered trials
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