ArticleComputational and mathematical methods in medicine2012
Membrane protein stability analyses by means of protein energy profiles in case of nephrogenic diabetes insipidus.
Article in Computational and mathematical methods in medicine, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- Pyridine Nucleotide Coenzyme Specificity ofFrontiers in microbiology · 2018Article
- The Trafficking of the Water Channel Aquaporin-2 in Renal Principal Cells-a Potential Target for Pharmacological Intervention in Cardiovascular Diseases.Frontiers in pharmacology · 2016Review
- A novel therapeutic effect of statins on nephrogenic diabetes insipidus.Journal of cellular and molecular medicine · 2015Review
- Nephrogenic diabetes insipidus: essential insights into the molecular background and potential therapies for treatment.Endocrine reviews · 2013Review
- eProS--a database and toolbox for investigating protein sequence-structure-function relationships through energy profiles.Nucleic acids research · 2013Article
- Tat peptide-mediated soluble expression of the membrane protein LSECtin-CRD in Escherichia coli.PloS one · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Diabetes insipidus (DI) is a rare endocrine, inheritable disorder with low incidences in an estimated one per 25,000-30,000 live births. This disease is characterized by polyuria and compensatory polydypsia. The diverse underlying causes of DI can be central defects, in which no functional arginine vasopressin (AVP) is released from the pituitary or can be a result of defects in the kidney (nephrogenic DI, NDI). NDI is a disorder in which patients are unable to concentrate their urine despite the presence of AVP. This antidiuretic hormone regulates the process of water reabsorption from the prourine that is formed in the kidney. It binds to its type-2 receptor (V2R) in the kidney induces a cAMP-driven cascade, which leads to the insertion of aquaporin-2 water channels into the apical membrane. Mutations in the genes of V2R and aquaporin-2 often lead to NDI. We investigated a structure model of V2R in its bound and unbound state regarding protein stability using a novel protein energy profile approach. Furthermore, these techniques were applied to the wild-type and selected mutations of aquaporin-2. We show that our results correspond well to experimental water ux analysis, which confirms the applicability of our theoretical approach to equivalent problems.
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