PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25359234-6 2015 Recently, AQP3, AQP9, AQP10 and AQP11 were additionally identified in human adipocytes and proposed as additional glycerol pathways in these cells. Glycerol 114-122 aquaporin 10 Homo sapiens 22-27 30420639-0 2018 Human adipose glycerol flux is regulated by a pH gate in AQP10. Glycerol 14-22 aquaporin 10 Homo sapiens 57-62 23382902-0 2013 Aquaporin-10 represents an alternative pathway for glycerol efflux from human adipocytes. Glycerol 51-59 aquaporin 10 Homo sapiens 0-12 25008241-2 2014 Aquaglyceroporins (AQP3, AQP7, AQP9 and AQP10) encompass a subfamily of aquaporins that allow the movement of water, but also of small solutes, such as glycerol, across cell membranes. Glycerol 152-160 aquaporin 10 Homo sapiens 40-45 23677388-3 2013 AQP3 and AQP10 are aqua-glyceroporins, known to transport glycerol as well as water. Glycerol 58-66 aquaporin 10 Homo sapiens 9-14 23382902-10 2013 Aquaporin-10 silencing in human differentiated adipocytes resulted in a 50% decrease of glycerol and osmotic water permeability. Glycerol 88-96 aquaporin 10 Homo sapiens 0-12 34699768-1 2022 Human aquaporin 10 (hAQP10) is an aquaglyceroporin that assists in maintaining glycerol flux in adipocytes during lipolysis at low pH. Glycerol 79-87 aquaporin 10 Homo sapiens 6-18 21733844-1 2011 Human aquaporin10 (hAQP10) is a transmembrane facilitator of both water and glycerol transport in the small intestine. Glycerol 76-84 aquaporin 10 Homo sapiens 6-17 21733844-1 2011 Human aquaporin10 (hAQP10) is a transmembrane facilitator of both water and glycerol transport in the small intestine. Glycerol 76-84 aquaporin 10 Homo sapiens 19-25 21733844-5 2011 All three forms of hAQP10 where found to facilitate the transport of water, glycerol, erythritol, and xylitol, and glycosylation had little effect on functionality. Glycerol 76-84 aquaporin 10 Homo sapiens 19-25 21691092-4 2011 RESULTS: The transport of glycerol by hAQP10 was found to be highly saturable with a Michaelis constant of 10.4 muM and specifically inhibited by several glycerol analogs such as monoacetin. Glycerol 26-34 aquaporin 10 Homo sapiens 38-44 21691092-4 2011 RESULTS: The transport of glycerol by hAQP10 was found to be highly saturable with a Michaelis constant of 10.4 muM and specifically inhibited by several glycerol analogs such as monoacetin. Glycerol 154-162 aquaporin 10 Homo sapiens 38-44 21691092-5 2011 Furthermore, when glycerol was preloaded in hAQP10-expressing oocytes, its efflux was trans-stimulated by extracellular glycerol. Glycerol 18-26 aquaporin 10 Homo sapiens 44-50 21691092-5 2011 Furthermore, when glycerol was preloaded in hAQP10-expressing oocytes, its efflux was trans-stimulated by extracellular glycerol. Glycerol 120-128 aquaporin 10 Homo sapiens 44-50 21691092-6 2011 These results indicate the involvement of a carrier-mediated mechanism in glycerol transport by hAQP10. Glycerol 74-82 aquaporin 10 Homo sapiens 96-102 21691092-7 2011 Interestingly, a channel mechanism was also found to be involved in part in hAQP10-mediated glycerol transport. Glycerol 92-100 aquaporin 10 Homo sapiens 76-82 11573934-7 2001 Although AQP10 belongs to the AQP subfamily, which has been characterized by permeability to water and neutral solutes such as urea and glycerol, it was not permeable to urea nor glycerol. Glycerol 136-144 aquaporin 10 Homo sapiens 9-14 34627746-2 2022 The aquaglyceroporins (AQP3, AQP7, AQP9 and AQP10) represent key glycerol channels, enabling glycerol flux across the membranes of cells. Glycerol 65-73 aquaporin 10 Homo sapiens 44-49 34627746-2 2022 The aquaglyceroporins (AQP3, AQP7, AQP9 and AQP10) represent key glycerol channels, enabling glycerol flux across the membranes of cells. Glycerol 93-101 aquaporin 10 Homo sapiens 44-49 34699768-1 2022 Human aquaporin 10 (hAQP10) is an aquaglyceroporin that assists in maintaining glycerol flux in adipocytes during lipolysis at low pH. Glycerol 79-87 aquaporin 10 Homo sapiens 20-26 34699768-3 2022 Control of hAQP10-mediated glycerol flux has been linked to the cytoplasmic end of the channel, where a unique loop is regulated by the protonation status of histidine 80 (H80). Glycerol 27-35 aquaporin 10 Homo sapiens 11-17 34468767-1 2021 The inhibition of glycerol permeation via human aquaporin-10 (hAQP10) by organometallic gold complexes has been studied by fluorescence stopped-flow spectroscopy, and its mechanism has been described using molecular modelling and atomistic simulations. Glycerol 18-26 aquaporin 10 Homo sapiens 48-60 34468767-1 2021 The inhibition of glycerol permeation via human aquaporin-10 (hAQP10) by organometallic gold complexes has been studied by fluorescence stopped-flow spectroscopy, and its mechanism has been described using molecular modelling and atomistic simulations. Glycerol 18-26 aquaporin 10 Homo sapiens 62-68 34468767-4 2021 The obtained computational results by metadynamics show that the local arylation of Cys209 in hAQP10 by one of the gold inhibitors is mapped into a global change of the overall free energy of glycerol translocation across the channel. Glycerol 192-200 aquaporin 10 Homo sapiens 94-100