Please use this identifier to cite or link to this item: https://doi.org/10.1007/s00018-016-2406-8
DC FieldValue
dc.titleH2S biosynthesis and catabolism: new insights from molecular studies
dc.contributor.authorRose P.
dc.contributor.authorMoore P.K.
dc.contributor.authorZhu Y.Z.
dc.date.accessioned2020-09-09T06:25:40Z
dc.date.available2020-09-09T06:25:40Z
dc.date.issued2017
dc.identifier.citationRose 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.issn1420-682X
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/175231
dc.description.abstractHydrogen 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.publisherBirkhauser Verlag AG
dc.sourceUnpaywall 20200831
dc.subject3 mercaptopyruvate sulfurtransferase
dc.subjectcystathionine beta synthase
dc.subjectcystathionine gamma lyase
dc.subjectcysteine dioxygenase
dc.subjecthydrogen sulfide
dc.subjectimmunoglobulin enhancer binding protein
dc.subjectreduced nicotinamide adenine dinucleotide (phosphate) dehydrogenase (quinone)
dc.subjectsulfide
dc.subject3-mercaptopyruvate sulphurtransferase
dc.subjectcystathionine beta synthase
dc.subjectcysteine dioxygenase
dc.subjectdioxygenase
dc.subjectETHE1 protein, mouse
dc.subjecthydrogen sulfide
dc.subjectlyase
dc.subjectmitochondrial protein
dc.subjectO-succinylhomoserine (thiol)-lyase
dc.subjectreduced nicotinamide adenine dinucleotide (phosphate) dehydrogenase (quinone)
dc.subjectsulfide quinone reductase
dc.subjectsulfurtransferase
dc.subjectbiosynthesis
dc.subjectbrain disease
dc.subjectcatabolism
dc.subjectchemical structure
dc.subjectdetoxification
dc.subjectdisease association
dc.subjectdisease model
dc.subjectdisease predisposition
dc.subjectenzyme activity
dc.subjectgas analysis
dc.subjecthuman
dc.subjectin vivo study
dc.subjectnonhuman
dc.subjectprotein expression
dc.subjectReview
dc.subjectsite directed mutagenesis
dc.subjecttransgenic animal
dc.subjectupregulation
dc.subjectanimal
dc.subjectgene expression regulation
dc.subjectgene inactivation
dc.subjectgenetics
dc.subjectmetabolism
dc.subjectprocedures
dc.subjectsignal transduction
dc.subjectAnimals
dc.subjectBiosynthetic Pathways
dc.subjectCarbon-Oxygen Lyases
dc.subjectCystathionine beta-Synthase
dc.subjectCysteine Dioxygenase
dc.subjectDioxygenases
dc.subjectGene Expression Regulation
dc.subjectGene Knockout Techniques
dc.subjectHumans
dc.subjectHydrogen Sulfide
dc.subjectMitochondrial Proteins
dc.subjectQuinone Reductases
dc.subjectSignal Transduction
dc.subjectSulfurtransferases
dc.typeReview
dc.contributor.departmentPHARMACOLOGY
dc.description.doi10.1007/s00018-016-2406-8
dc.description.sourcetitleCellular and Molecular Life Sciences
dc.description.volume74
dc.description.issue8
dc.description.page1391-1412
dc.published.statePublished
Appears in Collections:Staff Publications
Elements

Show simple item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
10_1007_s00018-016-2406-8.pdf688.64 kBAdobe PDF

OPEN

NoneView/Download

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.