Intermolecular disulfide bond to modulate protein function as a redox-sensing switch.
about
A disulphide bond in the E2 enzyme Pex4p modulates ubiquitin-conjugating activityStructures of the Ets Protein DNA-binding Domains of Transcription Factors Etv1, Etv4, Etv5, and Fev: DETERMINANTS OF DNA BINDING AND REDOX REGULATION BY DISULFIDE BOND FORMATION.Redox biology: computational approaches to the investigation of functional cysteine residuesInvolvement of the Azotobacter vinelandii rhodanese-like protein RhdA in the glutathione regeneration pathway.Playing with cardiac "redox switches": the "HNO way" to modulate cardiac function.The functions of crucial cysteine residues in the arsenite methylation catalyzed by recombinant human arsenic (III) methyltransferaseRational design of a fusion protein to exhibit disulfide-mediated logic gate behavior.Prediction of reversible disulfide based on features from local structural signatures.Electrochemical activation of engineered protein switches.A case of mistaken identity: are reactive oxygen species actually reactive sulfide species?Anticancer activity of metal complexes: involvement of redox processes.Nitroxyl (HNO) for treatment of acute heart failure.A Cysteine-Rich Protein Kinase Associates with a Membrane Immune Complex and the Cysteine Residues Are Required for Cell Death.TGF-β1 conjugated to gold nanoparticles results in protein conformational changes and attenuates the biological function.Catalytic site cysteines of thiol enzyme: sulfurtransferases.Sulfur- and seleno-containing amino acidsMultiple role of 3-mercaptopyruvate sulfurtransferase: antioxidative function, H2 S and polysulfide production and possible SOx production.Delineation of the molecular mechanism for disulfide stress-induced aluminium toxicity.Sulfhydryl-dependent dimerization of soluble guanylyl cyclase modulates the relaxation of porcine pulmonary arteries to nitric oxide.Redox-Dependent Conformational Switching of Diphenylacetylenes
P2860
Q27685286-C018E3F5-56B9-4633-A4A2-71339E0BEFD5Q30373611-D7ACB0CC-0BF1-4D50-B208-57A2CF0A7372Q30393259-503AEC45-68EE-49D7-BC3A-280B439A49E9Q34438013-E137A808-FD2C-44FB-872E-7A1525ACF98EQ34735841-735CCB7B-68D2-4971-8EF3-12F8A03CC685Q35370790-F7098E8D-3360-406C-80AE-D8FB9214C558Q35541987-424D0F96-A136-4E31-A2A6-8840AF9E2A9AQ36334693-DBAB8179-3BF7-4D92-8E45-D2A5AF6DCCD4Q36486885-4B2A35A9-59F9-47D7-BE60-314710FDC31EQ36902539-AEF9C7AE-D276-4847-8535-25BE7AD6C267Q37833099-BF027C0D-13BB-4905-82F3-60E6B0367F06Q38224809-7236C5DB-BF39-45F0-BE2C-51C93E3EB027Q39182340-762305BF-0019-4268-8A55-66CBB06BA74DQ39207556-45D7615E-0D7B-4B55-9E06-F98540DC93B4Q40973262-F1DFA802-48DE-4E04-8D65-DB21EED14E60Q42732249-A82E989D-C0CA-4064-B5B5-CF812006E016Q47384127-7CB06E2B-E79D-45D8-9CB4-9F9D6AF7577DQ53647553-FCFFD1EA-DF43-4C61-9370-B465AF0145A0Q54472380-8267D7A6-674A-4A9A-B163-352F53A409B6Q58213204-D1ACB7B5-A267-4B0A-8C76-EEC53E9F17CE
P2860
Intermolecular disulfide bond to modulate protein function as a redox-sensing switch.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 24 February 2010
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Intermolecular disulfide bond to modulate protein function as a redox-sensing switch.
@en
Intermolecular disulfide bond to modulate protein function as a redox-sensing switch.
@nl
type
label
Intermolecular disulfide bond to modulate protein function as a redox-sensing switch.
@en
Intermolecular disulfide bond to modulate protein function as a redox-sensing switch.
@nl
prefLabel
Intermolecular disulfide bond to modulate protein function as a redox-sensing switch.
@en
Intermolecular disulfide bond to modulate protein function as a redox-sensing switch.
@nl
P2860
P1433
P1476
Intermolecular disulfide bond to modulate protein function as a redox-sensing switch.
@en
P2093
N Nagahara
P2860
P2888
P356
10.1007/S00726-010-0508-4
P577
2010-02-24T00:00:00Z