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T G Jensen

Researcher at Aarhus University

Publications -  31
Citations -  1088

T G Jensen is an academic researcher from Aarhus University. The author has contributed to research in topics: Vasopressin & Transplantation. The author has an hindex of 19, co-authored 31 publications receiving 1050 citations. Previous affiliations of T G Jensen include Aarhus University Hospital.

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Side population cells in human and mouse epidermis lack stem cell characteristics

TL;DR: It is shown that mouse and human epidermis contain sp cells, and, to identify the origin of these cells, the expression of several marker genes are tested and it is found that Esp cells constitute a subpopulation of the alpha6 integrin-positive basal cells of the mouse epidersmis.
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Ethylmalonic Aciduria Is Associated with an Amino Acid Variant of Short Chain Acyl-Coenzyme A Dehydrogenase

TL;DR: The overrepresentation of the variant allele, a guanine to adenine polymorphism in the SCAD gene at position 625, and biochemical studies indicate that the A625 allele confers susceptibility to the development of ethylmalonic aciduria are indicated.
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Nanomedicine: Techniques, Potentials, and Ethical Implications

TL;DR: The use and potentials of emerging nanoscience techniques in medicine such as nanosurgery, tissue engineering, and targeted drug delivery are considered, and the ethical questions that these techniques raise are discussed.
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Molecular mechanisms in DM1 — a focus on foci

TL;DR: This review focuses on the homeostasis of DMPK mRNA foci and discusses how their dynamic regulation may affect disease-causing mechanisms in DM1.
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Clinical and molecular evidence of abnormal processing and trafficking of the vasopressin preprohormone in a large kindred with familial neurohypophyseal diabetes insipidus due to a signal peptide mutation.

TL;DR: Results provide independent confirmation that this Ala(-1)Thr mutation produces adFNDI by directing the production of a mutant preprohormone that accumulates in the endoplasmic reticulum, because it cannot be cleaved from the signal peptide and transported to neurosecretory vesicles for further processing and secretion.