about
The Role of Copper Chaperone Atox1 in Coupling Redox Homeostasis to Intracellular Copper DistributionAntireduction: an ancient strategy fit for futureOxidative Stress in the Healthy and Wounded Hepatocyte: A Cellular Organelles PerspectiveThe basics of thiols and cysteines in redox biology and chemistryGlutathione redox control of asthma: from molecular mechanisms to therapeutic opportunitiesDepletion of cyclophilins B and C leads to dysregulation of endoplasmic reticulum redox homeostasisRedox regulation of mitochondrial functionThioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signalingReactive oxygen species, cellular redox systems, and apoptosisProtective mechanisms of mitochondria and heart function in diabetesThe effects of chromium(VI) on the thioredoxin system: implications for redox regulationc-Myc and AMPK Control Cellular Energy Levels by Cooperatively Regulating Mitochondrial Structure and FunctionSulfenic acid chemistry, detection and cellular lifetimeMitochondria and cancerSmart micro/nanoparticles in stimulus-responsive drug/gene delivery systems.Current Multistage Drug Delivery Systems Based on the Tumor Microenvironment.From structure to redox: The diverse functional roles of disulfides and implications in disease.Disulfide bond formation in the herpes simplex virus 1 UL6 protein is required for portal ring formation and genome encapsidation.Disulfide bond formation contributes to herpes simplex virus capsid stability and retention of pentons.Disulfide bond formation at the C termini of vaccinia virus A26 and A27 proteins does not require viral redox enzymes and suppresses glycosaminoglycan-mediated cell fusion.Systemic remodeling of the redox regulatory network due to RNAi perturbations of glutaredoxin 1, thioredoxin 1, and glucose-6-phosphate dehydrogenaseMultifractal analysis for nutritional assessment.Calculation of the relative metastabilities of proteins in subcellular compartments of Saccharomyces cerevisiaeOxidative stress, antioxidants and intestinal calcium absorption.Protein redox modification as a cellular defense mechanism against tissue ischemic injury.Transient glutathione depletion determines terminal differentiation in HL-60 cells.A systems biology perspective on Nrf2-mediated antioxidant responseTargeted radionuclide therapy with astatine-211: Oxidative dehalogenation of astatobenzoate conjugates.Hydrogen peroxide probes directed to different cellular compartments.Oxidation of plasma cysteine/cystine and GSH/GSSG redox potentials by acetaminophen and sulfur amino acid insufficiency in humansDegradable Controlled-Release Polymers and Polymeric Nanoparticles: Mechanisms of Controlling Drug Release.Single cell-resolution western blotting.Mechanisms of pathogenesis in drug hepatotoxicity putting the stress on mitochondria.Inhibition of glutathione synthesis distinctly alters mitochondrial and cytosolic redox poiseReactive oxygen species and redox compartmentalizationCharacterization of apical and basal thiol-disulfide redox regulation in human colonic epithelial cells.Redox control systems in the nucleus: mechanisms and functions.Regulation of mitochondrial processes by protein S-nitrosylation.Redox sensing: orthogonal control in cell cycle and apoptosis signalling.Thioredoxin-1 redox signaling regulates cell survival in response to hyperoxia.
P2860
Q26740516-D2F8A156-325C-4C32-991C-43CB8F85D06EQ26748119-24A372A8-946C-4170-9145-CEBE4F007B38Q26770805-0C2270F4-0266-4C6B-A14E-D6396A62D126Q26991843-57B3E4DD-792F-470B-9A43-A14F3FC958A7Q27694579-D04DC148-F9AD-4806-9E8A-F2F9A67F2CAAQ28243241-31C85333-8EA6-4F06-8542-98CBA99FE33FQ28383361-1453F51D-307A-4CBB-BED0-7AE192F639B5Q28389739-49C5535C-E8F1-4EDA-9553-6A39C05D997BQ28393669-05CFF7EA-6C9C-4359-BDC4-BC1A86F193C1Q28395215-853DA81A-6798-4305-9C71-5914DD35212AQ28397704-9E62E1BE-BF39-4F16-8FA6-C6484B7C82FFQ28546968-F7AFDA67-F655-4778-9C24-EB5304D5ABF5Q29011150-2421F717-1562-4E7E-97B9-E5CDDAA8EA02Q29616610-F1C71C9A-906D-4386-8B93-9EC6CD308BA5Q30361646-46A4189B-4ED5-4CD0-8DB2-42C2E62740FCQ30362001-0702B7AB-6310-4327-A5BE-7E7F636D5838Q30397007-FFD553E8-B762-4153-BC35-E5DB20137A56Q30428140-6E59DC71-EAB4-470B-869F-26A127B2F833Q30428144-B938B405-8252-4825-83CA-A4B7F1763342Q30488301-6114DCDC-ED85-40C5-B2E8-6E1B6C54389EQ31034705-9A1EC886-AFE6-40CB-A0EE-C7E9F1B8A820Q31130295-713BC8AC-FE01-454A-B1EE-E6292F19413EQ33483697-6C19E923-80F0-4EB3-A65A-168F73D77E42Q33628380-17B85EE8-8456-4775-BECB-B5F99536FDE9Q33634920-682A6236-B134-4836-9D38-868A24FDD947Q33716911-FB782E71-4AAC-4075-8F01-555821B7AAC4Q33724409-D048EFC0-388E-48AC-A3C9-EECF744B80FEQ33746975-FED5D940-EDF1-4FF3-9D8C-F91F2231419DQ33809202-E1FA74FD-4C0C-4C7E-A640-E18AB60C74C4Q33890898-EAB9D225-A741-46DB-9E85-71A54B3BD1EBQ33902253-DB567833-3DDE-44B1-B878-6503096674E6Q33906901-FBE9D99F-EE4D-4951-9AE8-D8CEE5654696Q33954265-43E7B4F3-E6BA-4671-9496-9FC745D668DFQ33997792-77731662-F770-4BD0-9F5B-F6669347ED96Q34034025-07A71A48-88B7-4E94-8470-2F50998A3839Q34085272-8938F320-2036-420A-85C4-68C347239984Q34110120-AB6C17E7-0A2A-48BF-BC13-BF3F81B718F3Q34170269-5C6FD6F9-C405-4BCB-8D2E-D0C14C2E373BQ34237228-1501D294-E9E8-486D-9C44-687EA8FCBD51Q34240142-B64F6C36-2C1A-4CBA-8E27-0A96B771402A
P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 26 January 2008
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Redox compartmentalization in eukaryotic cells
@en
Redox compartmentalization in eukaryotic cells.
@nl
type
label
Redox compartmentalization in eukaryotic cells
@en
Redox compartmentalization in eukaryotic cells.
@nl
prefLabel
Redox compartmentalization in eukaryotic cells
@en
Redox compartmentalization in eukaryotic cells.
@nl
P2860
P1476
Redox compartmentalization in eukaryotic cells
@en
P2093
Dean P Jones
Young-Mi Go
P2860
P304
P356
10.1016/J.BBAGEN.2008.01.011
P407
P577
2008-01-26T00:00:00Z