Please use this identifier to cite or link to this item:
https://doi.org/10.1007/s00018-016-2406-8
DC Field | Value | |
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dc.title | H2S biosynthesis and catabolism: new insights from molecular studies | |
dc.contributor.author | Rose P. | |
dc.contributor.author | Moore P.K. | |
dc.contributor.author | Zhu Y.Z. | |
dc.date.accessioned | 2020-09-09T06:25:40Z | |
dc.date.available | 2020-09-09T06:25:40Z | |
dc.date.issued | 2017 | |
dc.identifier.citation | Rose P., Moore P.K., Zhu Y.Z. (2017). H2S biosynthesis and catabolism: new insights from molecular studies. Cellular and Molecular Life Sciences 74 (8) : 1391-1412. ScholarBank@NUS Repository. https://doi.org/10.1007/s00018-016-2406-8 | |
dc.identifier.issn | 1420-682X | |
dc.identifier.uri | https://scholarbank.nus.edu.sg/handle/10635/175231 | |
dc.description.abstract | Hydrogen sulfide (H2S) has profound biological effects within living organisms and is now increasingly being considered alongside other gaseous signalling molecules, such as nitric oxide (NO) and carbon monoxide (CO). Conventional use of pharmacological and molecular approaches has spawned a rapidly growing research field that has identified H2S as playing a functional role in cell-signalling and post-translational modifications. Recently, a number of laboratories have reported the use of siRNA methodologies and genetic mouse models to mimic the loss of function of genes involved in the biosynthesis and degradation of H2S within tissues. Studies utilising these systems are revealing new insights into the biology of H2S within the cardiovascular system, inflammatory disease, and in cell signalling. In light of this work, the current review will describe recent advances in H2S research made possible by the use of molecular approaches and genetic mouse models with perturbed capacities to generate or detoxify physiological levels of H2S gas within tissues. © 2016, The Author(s). | |
dc.publisher | Birkhauser Verlag AG | |
dc.source | Unpaywall 20200831 | |
dc.subject | 3 mercaptopyruvate sulfurtransferase | |
dc.subject | cystathionine beta synthase | |
dc.subject | cystathionine gamma lyase | |
dc.subject | cysteine dioxygenase | |
dc.subject | hydrogen sulfide | |
dc.subject | immunoglobulin enhancer binding protein | |
dc.subject | reduced nicotinamide adenine dinucleotide (phosphate) dehydrogenase (quinone) | |
dc.subject | sulfide | |
dc.subject | 3-mercaptopyruvate sulphurtransferase | |
dc.subject | cystathionine beta synthase | |
dc.subject | cysteine dioxygenase | |
dc.subject | dioxygenase | |
dc.subject | ETHE1 protein, mouse | |
dc.subject | hydrogen sulfide | |
dc.subject | lyase | |
dc.subject | mitochondrial protein | |
dc.subject | O-succinylhomoserine (thiol)-lyase | |
dc.subject | reduced nicotinamide adenine dinucleotide (phosphate) dehydrogenase (quinone) | |
dc.subject | sulfide quinone reductase | |
dc.subject | sulfurtransferase | |
dc.subject | biosynthesis | |
dc.subject | brain disease | |
dc.subject | catabolism | |
dc.subject | chemical structure | |
dc.subject | detoxification | |
dc.subject | disease association | |
dc.subject | disease model | |
dc.subject | disease predisposition | |
dc.subject | enzyme activity | |
dc.subject | gas analysis | |
dc.subject | human | |
dc.subject | in vivo study | |
dc.subject | nonhuman | |
dc.subject | protein expression | |
dc.subject | Review | |
dc.subject | site directed mutagenesis | |
dc.subject | transgenic animal | |
dc.subject | upregulation | |
dc.subject | animal | |
dc.subject | gene expression regulation | |
dc.subject | gene inactivation | |
dc.subject | genetics | |
dc.subject | metabolism | |
dc.subject | procedures | |
dc.subject | signal transduction | |
dc.subject | Animals | |
dc.subject | Biosynthetic Pathways | |
dc.subject | Carbon-Oxygen Lyases | |
dc.subject | Cystathionine beta-Synthase | |
dc.subject | Cysteine Dioxygenase | |
dc.subject | Dioxygenases | |
dc.subject | Gene Expression Regulation | |
dc.subject | Gene Knockout Techniques | |
dc.subject | Humans | |
dc.subject | Hydrogen Sulfide | |
dc.subject | Mitochondrial Proteins | |
dc.subject | Quinone Reductases | |
dc.subject | Signal Transduction | |
dc.subject | Sulfurtransferases | |
dc.type | Review | |
dc.contributor.department | PHARMACOLOGY | |
dc.description.doi | 10.1007/s00018-016-2406-8 | |
dc.description.sourcetitle | Cellular and Molecular Life Sciences | |
dc.description.volume | 74 | |
dc.description.issue | 8 | |
dc.description.page | 1391-1412 | |
dc.published.state | Published | |
Appears in Collections: | Staff Publications Elements |
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