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  • 1
    Publication Date: 2008-10-14
    Description: Human primordial germ cells and mouse neonatal and adult germline stem cells are pluripotent and show similar properties to embryonic stem cells. Here we report the successful establishment of human adult germline stem cells derived from spermatogonial cells of adult human testis. Cellular and molecular characterization of these cells revealed many similarities to human embryonic stem cells, and the germline stem cells produced teratomas after transplantation into immunodeficient mice. The human adult germline stem cells differentiated into various types of somatic cells of all three germ layers when grown under conditions used to induce the differentiation of human embryonic stem cells. We conclude that the generation of human adult germline stem cells from testicular biopsies may provide simple and non-controversial access to individual cell-based therapy without the ethical and immunological problems associated with human embryonic stem cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Conrad, Sabine -- Renninger, Markus -- Hennenlotter, Jorg -- Wiesner, Tina -- Just, Lothar -- Bonin, Michael -- Aicher, Wilhelm -- Buhring, Hans-Jorg -- Mattheus, Ulrich -- Mack, Andreas -- Wagner, Hans-Joachim -- Minger, Stephen -- Matzkies, Matthias -- Reppel, Michael -- Hescheler, Jurgen -- Sievert, Karl-Dietrich -- Stenzl, Arnulf -- Skutella, Thomas -- England -- Nature. 2008 Nov 20;456(7220):344-9. doi: 10.1038/nature07404. Epub 2008 Oct 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Anatomy, Department of Experimental Embryology, Tubingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18849962" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Animals ; Biomarkers/metabolism ; Cell Culture Techniques ; Cell Differentiation ; Cell Line ; Cell Lineage ; Cells, Cultured ; Embryonic Stem Cells/cytology/metabolism ; Epigenesis, Genetic ; Gene Expression Profiling ; Humans ; Male ; Mice ; Mice, Nude ; Neoplasm Transplantation ; Pluripotent Stem Cells/*cytology/metabolism ; Spermatogonia/cytology/ultrastructure ; Teratoma/pathology ; Testis/*cytology
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2017-07-21
    Description: Hsp100 polypeptide translocases are conserved members of the AAA+ family (adenosine triphosphatases associated with diverse cellular activities) that maintain proteostasis by unfolding aberrant and toxic proteins for refolding or proteolytic degradation. The Hsp104 disaggregase from Saccharomyces cerevisiae solubilizes stress-induced amorphous aggregates and amyloids. The structural basis for substrate recognition and translocation is unknown. Using a model substrate (casein), we report cryo–electron microscopy structures at near-atomic resolution of Hsp104 in different translocation states. Substrate interactions are mediated by conserved, pore-loop tyrosines that contact an 80-angstrom-long unfolded polypeptide along the axial channel. Two protomers undergo a ratchet-like conformational change that advances pore loop–substrate interactions by two amino acids. These changes are coupled to activation of specific nucleotide hydrolysis sites and, when transmitted around the hexamer, reveal a processive rotary translocation mechanism and substrate-responsive flexibility during Hsp104-catalyzed disaggregation.
    Keywords: Biochemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Geosciences , Computer Science , Medicine , Natural Sciences in General , Physics
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