Hydrogen sulfide and hemeproteins: knowledge and mysteries - Wikidata - wikimedia - TriplyDB

Hydrogen sulfide and hemeproteins: knowledge and mysteries

Hydrogen sulfide and hemeproteins: knowledge and mysteries

http://www.wikidata.org/entity/Q35055729

about

Hydrogen sulfide chemical biology: pathophysiological roles and detection Hydrogen sulfide inhibits amyloid formation Cell-trappable fluorescent probes for endogenous hydrogen sulfide signaling and imaging H2O2-dependent H2S production.Redox chemistry and chemical biology of H2S, hydropersulfides, and derived species: implications of their possible biological activity and utility Interactions of hydrogen sulfide with myeloperoxidase Sulfide oxidation by a noncanonical pathway in red blood cells generates thiosulfate and polysulfides Role of Hydrogen Sulfide in Ischemia-Reperfusion Injury.Chemical probes for molecular imaging and detection of hydrogen sulfide and reactive sulfur species in biological systems.A Matter of Timing: Contrasting Effects of Hydrogen Sulfide on Oxidative Stress Response in Shewanella oneidensis.Biological signaling by small inorganic molecules The cytochrome bd oxidase of Escherichia coli prevents respiratory inhibition by endogenous and exogenous hydrogen sulfide.Molecular Cloning and Characterization of a (Lys)6-Tagged Sulfide-Reactive Hemoglobin I from Lucina pectinata.The complex effects of the slow-releasing hydrogen sulfide donor GYY4137 in a model of acute joint inflammation and in human cartilage cells.Hydrogen sulfide activation in hemeproteins: the sulfheme scenario.Redox Biology of Hydrogen Sulfide: Implications for Physiology, Pathophysiology, and Pharmacology.Chemical foundations of hydrogen sulfide biology.Fluorescence chemosensors for hydrogen sulfide detection in biological systems.Oxygen tension, H2S, and NO bioavailability: is there an interaction?H2S: A Novel Gasotransmitter that Signals by Sulfhydration.From yeast to human: exploring the comparative biology of methionine restriction in extending eukaryotic life span.Chemiluminescent detection of enzymatically produced H2S Cutting back on the essentials: Can manipulating intake of specific amino acids modulate health and lifespan?Sulfmyoglobin Conformational Change: A Role in the Decrease of Oxy-Myoglobin Functionality.Redox regulation of gasotransmission in the vascular system: A focus on angiogenesis.Effects of duration of vitamin C supplementation during the finishing period on postmortem protein degradation, tenderness, and meat color of the longissimus muscle of calf-fed steers consuming a 0.31 or 0.59% sulfur diet.Studies of iron(III) porphyrinates containing silanethiolate ligands.Chemiluminescent detection of enzymatically produced hydrogen sulfide: substrate hydrogen bonding influences selectivity for H2S over biological thiols.Regulation of soluble guanylyl cyclase redox state by hydrogen sulfide.A turn-on endoplasmic reticulum-targeted two-photon fluorescent probe for hydrogen sulfide and bio-imaging applications in living cells, tissues, and zebrafish.Hydrogen sulfide: redox metabolism and signaling.A review of hydrogen sulfide (H2S) donors: Chemistry and potential therapeutic applications.Structural and Mechanistic Insights into Hemoglobin-catalyzed Hydrogen Sulfide Oxidation and the Fate of Polysulfide Products.Spectroscopic investigations into the binding of hydrogen sulfide to synthetic picket-fence porphyrins.Engineered (Lys)6-Tagged Recombinant Sulfide-Reactive Hemoglobin I for Covalent Immobilization at Multiwalled Carbon Nanotubes.Chemical Biology of H2S Signaling through Persulfidation.Hydrogen sulfide inhibits Kir2 and Kir3 channels by decreasing sensitivity to the phospholipid PIP2.Reactions of persulfides with the heme cofactor of oxidized myoglobin and microperoxidase 11: reduction or coordination.Novel treatment strategies for chronic kidney disease: insights from the animal kingdom.Conversion of a heme-based oxygen sensor to a heme oxygenase by hydrogen sulfide: effects of mutations in the heme distal side of a heme-based oxygen sensor phosphodiesterase (Ec DOS).Effects of hydrogen sulfide on the heme coordination structure and catalytic activity of the globin-coupled oxygen sensor AfGcHK.

P2860

Q26824672-FB0B1BA7-1D6E-482D-A6A9-280AD7D5DB94 Q27335684-08AEFF88-45CE-4A3E-96EA-68C94B80D817 Q30539574-7158ED42-7076-41F3-9820-1A6100FAD078 Q34646825-C8873109-335B-4C2F-B16D-E293F3FD255C Q35204852-9648FE32-4A41-40FA-B733-E87E16B17AF0 Q35221567-BC28842A-243A-445B-B4F3-04300CAE1876 Q35647095-7E8EAF71-CF15-4CDC-BEF6-1FEA11D812F4 Q35685352-5195307C-7B45-4F8B-A8DC-8CEE6C687194 Q36208042-403B7E1E-83D4-4EF0-9978-517606DAA7D9 Q36376440-71ABAC7D-B204-41FD-BF33-278C6B95AF2F Q37047929-C66EF932-24A1-4D19-90A0-68D57577208B Q37075970-207D2870-42F2-4A51-A8D0-F7E9F563F376 Q37295023-BAA9CDBD-EFCF-46F9-B078-3AD339B64149 Q37691508-E6756B31-F294-429C-8275-ED045B2425D1 Q38116513-CB219138-3108-49E1-9306-A3D3F451290B Q38121347-D7AB245C-10EA-419F-B899-AC04DBA4F8A6 Q38295883-30534B1E-150F-4A04-9FF6-BE3CB1660898 Q38589017-FE426ED9-791A-470F-BEC6-685D73272E3C Q38600019-4775E6A1-9D94-4AD2-A986-A8B9E88E62A7 Q38782067-A94DE31D-C318-4E88-AF13-5E356E1E1BC7 Q38905201-683E7330-8715-4088-BB1D-F69E8AA19AB6 Q38939563-37DF0B55-6B31-47E1-8A46-27CACF0451AA Q38990740-DCC8DE32-DACF-4D71-ADD1-CCCA49DAAC6A Q39256530-8912E9B3-CCC3-4701-A61C-C2531DC20532 Q40894076-F35F9DD6-8775-4D15-9847-DAFFC4373D85 Q41855679-397CDDFC-0874-48B9-8EDD-4BD4EB0F8256 Q41884764-DB29334F-A250-4587-B9EB-FCE17F7C249A Q42361109-EFF88F69-547A-40F2-BC35-4B099869D124 Q42374847-6D676AF1-C8C3-4A9C-B6FD-402E316C361F Q42764772-5F7A6355-1C69-4421-8CEA-A662D939B174 Q45073955-02E572EB-8BA8-485C-AEFE-F5C28C0309D3 Q46416014-F2F38312-F674-4D0F-85FA-AB46DD4E2316 Q46597109-D9197019-1B36-48EC-BB3B-E30355BF52EE Q47137892-E851D3B5-C4EB-40EF-9C39-66385FFD206A Q47430972-E20B85DB-3E8F-4427-97FF-03183097EA97 Q47873570-14CF6F55-0A8C-4FA6-95A5-9EA523AE357A Q48292784-B83FA26A-9D68-402E-AA77-C9D09D909E83 Q50051044-1D16546D-D86A-4254-8FB9-802FB7F3C3B4 Q50936799-E99A1878-DCE4-49E7-904F-3F522F4CCC14 Q53001265-49F82379-4A6D-45BE-8EE1-A17E8B7D9DEC

P2860

Hydrogen sulfide and hemeproteins: knowledge and mysteries

http://www.wikidata.org/entity/Q35055729

description

2011 nî lūn-bûn

@nan

2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Hydrogen sulfide and hemeproteins: knowledge and mysteries

@ast

Hydrogen sulfide and hemeproteins: knowledge and mysteries

@en

type

label

Hydrogen sulfide and hemeproteins: knowledge and mysteries

@ast

Hydrogen sulfide and hemeproteins: knowledge and mysteries

@en

prefLabel

Hydrogen sulfide and hemeproteins: knowledge and mysteries

@ast

Hydrogen sulfide and hemeproteins: knowledge and mysteries

@en

P1433

Q35055729-0FF4179E-3C4C-4445-9BA0-B1B1F2292851

P1476

Q35055729-E2EDA97A-2380-4062-9F7D-06CCEFDFD296

P2093

Q35055729-923CAEF2-EAB0-400F-8500-C34BB6CF4477

Q35055729-95654700-A855-4796-8929-8F5B48E3A93F

Q35055729-AFAE3211-2B35-494E-A422-842C660049FA

P2860

Q35055729-0746CD02-E145-45B5-90B2-25F6852381C6

Q35055729-0A74F671-E911-4BD1-9F74-CF285E74FB72

Q35055729-0AC6125E-D146-4983-B90A-496ABA5C661C

Q35055729-0B2B087A-F4E7-45EE-8314-DECE5C94CF22

Q35055729-0B32D926-BD77-4E3D-9FAF-39C4D4B0CE0F

Q35055729-0B8071FB-CF36-402B-8707-7E2455EF11D5

Q35055729-1233E236-EE20-428E-A26C-C907FE064827

Q35055729-176B0D24-0BAA-4351-9B04-BB8679475AE7

Q35055729-1E1B886B-726A-408B-9AA7-754608FA3EEE

Q35055729-22AE7C6F-2AB6-4A38-B1FA-CEBA834D1FE9

P304

Q35055729-368C6742-6082-4DA2-BDF7-7ED0A60C596D

P31

Q35055729-F6FD4ED8-6434-4D03-A519-37260F2496D1

P356

Q35055729-1BA9CF40-3197-4115-AD1F-5382C9F84144

P433

Q35055729-5623658B-8D01-4423-BABF-AB3E4CED162D

P478

Q35055729-E9D47975-85C6-443D-A480-AF3242A80551

P577

Q35055729-7F518685-18D9-49FB-8CFE-9F98DE567CC6

P5875

Q35055729-64AC62A3-7C32-4738-8353-CE2E013FC8BC

P698

Q35055729-417629C1-4171-4AD1-89B4-FA39AEB19F8E

P932

Q35055729-11B6AF3C-10A4-4BAA-A155-196DC261E560

P356

P1433

Antioxidants & Redox Signaling

P1476

Hydrogen sulfide and hemeproteins: knowledge and mysteries

@en

P2093

Elddie Román-Morales

http://www.w3.org/2001/XMLSchema#string

Juan López-Garriga

http://www.w3.org/2001/XMLSchema#string

Ruth Pietri

http://www.w3.org/2001/XMLSchema#string

P2860

Dynamics of carbon monoxide binding to cystathionine beta-synthase

Hydrogen sulfide mediates the vasoactivity of garlic

Structural bases for sulfide recognition in Lucina pectinata hemoglobin I

Solution and crystal structures of a sperm whale myoglobin triple mutant that mimics the sulfide-binding hemoglobin from Lucina pectinata

Relative contributions of cystathionine beta-synthase and gamma-cystathionase to H2S biogenesis via alternative trans-sulfuration reactions.

Redox regulation and reaction mechanism of human cystathionine-beta-synthase: a PLP-dependent hemesensor protein

H2S biogenesis by human cystathionine gamma-lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia.

Using a functional enzyme model to understand the chemistry behind hydrogen sulfide induced hibernation.

Hydrosulfide (HS-) coordination in iron porphyrinates.

Redox biochemistry of hydrogen sulfide.

P304

393-404

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1089/ARS.2010.3698

http://www.w3.org/2001/XMLSchema#string

P433

2

http://www.w3.org/2001/XMLSchema#string

P478

15

http://www.w3.org/2001/XMLSchema#string

P577

2011-04-08T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

47677773

http://www.w3.org/2001/XMLSchema#string

P698

21050142

http://www.w3.org/2001/XMLSchema#string

P932

3118656

http://www.w3.org/2001/XMLSchema#string