scholarly journals Discovery of a Macropinocytosis‐Inducing Peptide Potentiated by Medium‐Mediated Intramolecular Disulfide Formation

2021 ◽  
Author(s):  
Jan Vincent V. Arafiles ◽  
Hisaaki Hirose ◽  
Yusuke Hirai ◽  
Masashi Kuriyama ◽  
Maxwell Mamfe Sakyiamah ◽  
...  
Keyword(s):  
Disulfide Formation

scholarly journals New insights into the disulfide bond formation enzymes in epidithiodiketopiperazine alkaloids

2021 ◽  
Vol 12 (11) ◽  
pp. 4132-4138
Author(s):  
Huan Liu ◽  
Jie Fan ◽  
Peng Zhang ◽  
Youcai Hu ◽  
Xingzhong Liu ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Bond Formation ◽  
Disulfide Bond Formation ◽  
Disulfide Formation

A FAD-dependent oxidoreductase TdaR was responsible for α, β-disulfide formation in the biosynthesis of pretrichodermamide A. TdaR, together with its homologs AclT and GliT, catalysed not only α, α- but also α, β-disulfide formation in fungi.

Two-Step Synthesis of Tungsten and Molybdenum Disulfides

2016 ◽  
Vol 685 ◽  
pp. 511-515
Author(s):  
Yuriy Irtegov ◽  
Vladimir An ◽  
Ksenia Machekhina ◽  
Nikolay Lemachko
Keyword(s):  
Surface Area ◽  
Combustion Process ◽  
Wire Length ◽  
Reaction Products ◽  
Disulfide Formation ◽  
Sulphur Concentration ◽  
Free Sulphur ◽  
Elementary Sulphur ◽  
Metal Nanopowders

Efficient two-step technique of tungsten and molybdenum disulfides obtaining from metal nanopowders produced by EEW and elementary sulphur is described. Tungsten and molybdenum nanopowders surface area dependence on wire length is studied. Features of metal and sulphur combustion process are discussed. It is determined sulphur excess in reagents 15 wt.% results in mono-phase metal disulfide formation with small free sulphur concentration in reaction products.

scholarly journals Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS

2004 ◽  
Vol 23 (14) ◽  
pp. 2872-2881 ◽  
Author(s):  
Yoshiaki Furukawa ◽  
Andrew S Torres ◽  
Thomas V O'Halloran
Keyword(s):  
Copper Chaperone ◽  
Disulfide Formation

In vitro folding of methionine-arginine human lyspro-proinsulin S-sulfonate-Disulfide formation pathways and factors controlling yield

2010 ◽  
Vol 26 (5) ◽  
pp. 1332-1343 ◽  
Author(s):  
Shuang Chen ◽  
Lawrence Adijanto ◽  
Nien-Hwa Linda Wang
Keyword(s):  
Disulfide Formation

Disulfide-Mediated Bioconjugation: Disulfide Formation and Restructuring on the Surface of Nanomanufactured (Microfluidics) Nanoparticles

2019 ◽  
Vol 11 (30) ◽  
pp. 26607-26618 ◽  
Author(s):  
Mike Geven ◽  
Hanying Luo ◽  
Donghun Koo ◽  
Gangadhar Panambur ◽  
Roberto Donno ◽  
...  
Keyword(s):  
Disulfide Formation

scholarly journals Precursor Oxidation by Mia40 and Erv1 Promotes Vectorial Transport of Proteins into the Mitochondrial Intermembrane Space

2008 ◽  
Vol 19 (1) ◽  
pp. 226-236 ◽  
Author(s):  
Judith M. Müller ◽  
Dusanka Milenkovic ◽  
Bernard Guiard ◽  
Nikolaus Pfanner ◽  
Agnieszka Chacinska
Keyword(s):  
Experimental Evidence ◽  
Cysteine Residues ◽  
Intermembrane Space ◽  
Disulfide Formation ◽  
Precursor Proteins ◽  
Mitochondrial Intermembrane Space ◽  
Vectorial Transport ◽  
Tim Proteins

The mitochondrial intermembrane space contains chaperone complexes that guide hydrophobic precursor proteins through this aqueous compartment. The chaperones consist of hetero-oligomeric complexes of small Tim proteins with conserved cysteine residues. The precursors of small Tim proteins are synthesized in the cytosol. Import of the precursors requires the essential intermembrane space proteins Mia40 and Erv1 that were proposed to form a relay for disulfide formation in the precursor proteins. However, experimental evidence for a role of Mia40 and Erv1 in the oxidation of intermembrane space precursors has been lacking. We have established a system to directly monitor the oxidation of precursors during import into mitochondria and dissected distinct steps of the import process. Reduced precursors bind to Mia40 during translocation into mitochondria. Both Mia40 and Erv1 are required for formation of oxidized monomers of the precursors that subsequently assemble into oligomeric complexes. Whereas the reduced precursors can diffuse back into the cytosol, the oxidized precursors are retained in the intermembrane space. Thus, oxidation driven by Mia40 and Erv1 determines vectorial transport of the precursors into the mitochondrial intermembrane space.

scholarly journals Phosphodiesterase 5 Inhibition Limits Doxorubicin-induced Heart Failure by Attenuating Protein Kinase G Iα Oxidation

2016 ◽  
Vol 291 (33) ◽  
pp. 17427-17436 ◽  
Author(s):  
Oleksandra Prysyazhna ◽  
Joseph Robert Burgoyne ◽  
Jenna Scotcher ◽  
Steven Grover ◽  
David Kass ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Pde5 Inhibitor ◽  
Cardiac Injury ◽  
Left Ventricular ◽  
Loss Of Function ◽  
Doxorubicin Treatment ◽  
Disulfide Formation ◽  
Additional Protection ◽  
Phosphodiesterase 5

Phosphodiesterase 5 (PDE5) inhibitors limit myocardial injury caused by stresses, including doxorubicin chemotherapy. cGMP binding to PKG Iα attenuates oxidant-induced disulfide formation. Because PDE5 inhibition elevates cGMP and protects from doxorubicin-induced injury, we reasoned that this may be because it limits PKG Iα disulfide formation. To investigate the role of PKG Iα disulfide dimerization in the development of apoptosis, doxorubicin-induced cardiomyopathy was compared in male wild type (WT) or disulfide-resistant C42S PKG Iα knock-in (KI) mice. Echocardiography showed that doxorubicin treatment caused loss of myocardial tissue and depressed left ventricular function in WT mice. Doxorubicin also reduced pro-survival signaling and increased apoptosis in WT hearts. In contrast, KI mice were markedly resistant to the dysfunction induced by doxorubicin in WTs. In follow-on experiments the influence of the PDE5 inhibitor tadalafil on the development of doxorubicin-induced cardiomyopathy in WT and KI mice was investigated. In WT mice, co-administration of tadalafil with doxorubicin reduced PKG Iα oxidation caused by doxorubicin and also protected against cardiac injury and loss of function. KI mice were again innately resistant to doxorubicin-induced cardiotoxicity, and therefore tadalafil afforded no additional protection. Doxorubicin decreased phosphorylation of RhoA (Ser-188), stimulating its GTPase activity to activate Rho-associated protein kinase (ROCK) in WTs. These pro-apoptotic events were absent in KI mice and were attenuated in WTs co-administered tadalafil. PKG Iα disulfide formation triggers cardiac injury, and this initiation of maladaptive signaling can be blocked by pharmacological therapies that elevate cGMP, which binds kinase to limit its oxidation.

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