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Journal articles on the topic 'Thiol binding'

Author: Grafiati

Published: 4 June 2021

Last updated: 20 February 2023

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1

Lee, Duk-Shin, and Ji-Eun Kim. "PDI-Mediated Reduction of Disulfide Bond on PSD95 Increases Spontaneous Seizure Activity by Regulating NR2A–PSD95 Interaction in Epileptic Rats Independent of S-Nitrosylation." International Journal of Molecular Sciences 21, no. 6 (March 18, 2020): 2094. http://dx.doi.org/10.3390/ijms21062094.

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Postsynaptic density-95 (PSD95), a major scaffolding protein, is critical in coupling N-methyl-D-aspartate receptor (NMDAR) to cellular signaling networks in the central nervous system. A couple of cysteine residues in the N-terminus of PSD95 are potential sites for disulfide bonding, S-nitrosylation and/or palmitoylation. Protein disulfide isomerase (PDI) reduces disulfide bonds (S-S) to free thiol (-SH) on various proteins. However, the involvement of PDI in disulfide bond formation/S-nitrosylation of PSD95 and its role in epilepsy are still unknown. In the present study, acute seizure activ

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QUINLAN, Gregory J., Michael P. MARGARSON, Sharon MUMBY, Timothy W. EVANS, and John M. C. GUTTERIDGE. "Administration of albumin to patients with sepsis syndrome: a possible beneficial role in plasma thiol repletion." Clinical Science 95, no. 4 (October 1, 1998): 459–65. http://dx.doi.org/10.1042/cs0950459.

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1.Albumin is often administered intravenously to critically ill patients as a volume expander, to combat hypoalbuminaemia, and to decrease hyperbilirubinaemia. There is, however, an ongoing debate concerning the therapeutic benefit of the former which is an expensive form of treatment. 2.Albumin has several biological functions, in particular as a ligand binder. It also acts as an extracellular transition metal ion-binding and radical-scavenging antioxidant. These functions are influenced by the presence of an exposed thiol group (cys 34) on the surface of the albumin molecule. 3.The ability o

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Choi, Hiuwan, Khatira Aboulfatova, Henry J. Pownall, Richard Cook, and Jing-fei Dong. "Shear-induced Disulfide Bond Formation Regulates Adhesion Activity of von Willebrand Factor." Journal of Biological Chemistry 282, no. 49 (October 9, 2007): 35604–11. http://dx.doi.org/10.1074/jbc.m704047200.

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von Willebrand factor (VWF) is the largest multimeric adhesion ligand circulating in blood. Its adhesion activity is related to multimer size, with the ultra-large forms freshly released from the activated endothelial cells being most active, capable of spontaneously binding to platelets. In comparison, smaller plasma forms circulating in blood bind platelets only under high fluid shear stress or induced by modulators. The structure-function relationships that distinguish the two types of VWF multimers are not known. In this study, we demonstrate that some of the plasma VWF multimers contain s

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Lahav, Judith, Kerstin Jurk, Oded Hess, Michael J. Barnes, Richard W. Farndale, Jacob Luboshitz, and Beate E. Kehrel. "Sustained integrin ligation involves extracellular free sulfhydryls and enzymatically catalyzed disulfide exchange." Blood 100, no. 7 (October 1, 2002): 2472–78. http://dx.doi.org/10.1182/blood-2001-12-0339.

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Studies have suggested a pivotal role for free sulfhydryls in platelet integrin function, and enzyme-mediated reduction of disulfide bonds on platelets has been implicated. The platelet fibrinogen receptor αIIbβ3 is the best-studied platelet integrin and serves as a model system for studying the structure-function relation in this family of adhesion receptors. The demonstration of free sulfhydryls on the exofacial domain of purified αIIbβ3, specifically in its activated conformation, prompted us to explore the potential for activation-dependent, enzymatically catalyzed thiol expression on inta

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Ramasamy, Somasundaram, Tapan K. Kundu, William Antholine, Periakaruppan T. Manoharan, and Joseph M. Rifkind. "Internal spin trapping of thiyl radical during the complexation and reduction of cobalamin with glutathione and dithiothrietol." Journal of Porphyrins and Phthalocyanines 16, no. 01 (January 2012): 25–38. http://dx.doi.org/10.1142/s1088424611004051.

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The activation of cobalamin requires a reduction from cobalamin(III) to cobalamin(II). The reduction by glutathione and dithiothreitol was followed using visible spectroscopy and electron paramagnetic resonance. In addition the oxidation of glutathione was monitored. Glutathione first reacts with oxidized cobalamin(III). The binding of a second glutathione required for the reduction to cobalamin(II) is presumably located in the dimethyl benzimidazole ribonucleotide ligand cavity. The reduction of cobalamin(III) by dithiothreitol, which contains two thiols, is much faster even though no stable

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6

Jones, Dean P. "Radical-free biology of oxidative stress." American Journal of Physiology-Cell Physiology 295, no. 4 (October 2008): C849—C868. http://dx.doi.org/10.1152/ajpcell.00283.2008.

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Free radical-induced macromolecular damage has been studied extensively as a mechanism of oxidative stress, but large-scale intervention trials with free radical scavenging antioxidant supplements show little benefit in humans. The present review summarizes data supporting a complementary hypothesis for oxidative stress in disease that can occur without free radicals. This hypothesis, which is termed the “redox hypothesis,” is that oxidative stress occurs as a consequence of disruption of thiol redox circuits, which normally function in cell signaling and physiological regulation. The redox st

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7

Arican, Sule, Gulcin Hacibeyoglu, Sinan Oguzhan Ulukaya, Gamze Avcioglu, Ruhiye Reisli, Sema Tuncer Uzun, and Ozcan Erel. "Ischemia-modified albumin (IMA) and dynamic thiol-disulfide homeostasis in patients with postherpetic neuralgia." Journal of Laboratory Medicine 43, no. 5 (October 25, 2019): 257–63. http://dx.doi.org/10.1515/labmed-2018-0211.

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Abstract Background Ischemia-modified albumin (IMA) is an isotype of albumin that increases under oxidative stress, and plasma thiols are main defense mechanisms against oxidative stress. The objective of this study was to investigate thiol-disulfide homeostasis and serum IMA levels in postherpetic neuralgia (PHN) patients. Methods A total of 29 PHN patients and 30 healthy controls were included in the study. Serum total and native thiol concentrations and serum disulfide concentration were measured using the method described by Erel and Neselioglu. The albumin cobalt binding test was used to

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8

Tong, Ka-Chung, Chun-Nam Lok, Pui-Ki Wan, Di Hu, Yi Man Eva Fung, Xiao-Yong Chang, Song Huang, Haibo Jiang, and Chi-Ming Che. "An anticancer gold(III)-activated porphyrin scaffold that covalently modifies protein cysteine thiols." Proceedings of the National Academy of Sciences 117, no. 3 (January 2, 2020): 1321–29. http://dx.doi.org/10.1073/pnas.1915202117.

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Cysteine thiols of many cancer-associated proteins are attractive targets of anticancer agents. Herein, we unequivocally demonstrate a distinct thiol-targeting property of gold(III) mesoporphyrin IX dimethyl ester (AuMesoIX) and its anticancer activities. While the binding of cysteine thiols with metal complexes usually occurs via M–S bond formation, AuMesoIX is unique in that the meso-carbon atom of the porphyrin ring is activated by the gold(III) ion to undergo nucleophilic aromatic substitution with thiols. AuMesoIX was shown to modify reactive cysteine residues and inhibit the activities o

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Sokoloff, A. V., T. Whalley, and J. Zimmerberg. "Characterization of N-ethylmaleimide-sensitive thiol groups required for the GTP-dependent fusion of endoplasmic reticulum membranes." Biochemical Journal 312, no. 1 (November 15, 1995): 23–30. http://dx.doi.org/10.1042/bj3120023.

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The GTP-dependent fusion activity of endoplasmic reticulum membranes is thought to be required for the structural maintenance and post-mitotic regeneration of the endoplasmic reticulum. This fusion is sensitive to the thiol-alkylating agent N-ethylmaleimide. In many intracellular fusion events N-ethylmaleimide-sensitivity is associated with a homotrimeric ATPase called N-ethylmaleimide-sensitive fusion protein or NSF. The addition of cytosol containing NSF is known to restore fusion activity to N-ethylmaleimide-treated membranes. We found that the inhibition of fusion of rat liver endoplasmic

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White, Kylie, Gina Nicoletti, and Hugh Cornell. "Antibacterial Profile of a Microbicidal Agent Targeting Tyrosine Phosphatases and Redox Thiols, Novel Drug Targets." Antibiotics 10, no. 11 (October 27, 2021): 1310. http://dx.doi.org/10.3390/antibiotics10111310.

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The activity profile of a protein tyrosine phosphatase (PTP) inhibitor and redox thiol oxidant, nitropropenyl benzodioxole (NPBD), was investigated across a broad range of bacterial species. In vitro assays assessed inhibitory and lethal activity patterns, the induction of drug variants on long term exposure, the inhibitory interactions of NPBD with antibiotics, and the effect of plasma proteins and redox thiols on activity. A literature review indicates the complexity of PTP and redox signaling and suggests likely metabolic targets. NPBD was broadly bactericidal to pathogens of the skin, resp

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Solecka, Barbara, Birte Fuchs, Christoph Weise, and Christoph Kannicht. "Free Thiol Groups In Von Willebrand Factor (VWF) Are Required For Its Proper Function Under Physiological Flow Conditions." Blood 122, no. 21 (November 15, 2013): 2338. http://dx.doi.org/10.1182/blood.v122.21.2338.2338.

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Abstract Background The multimeric plasma glycoprotein von Willebrand factor (VWF) is exceptionally rich in cysteine, and its structure is largely determined by inter- and intramolecular disulfide bonding. Additionally, VWF was shown to contain unpaired cysteine residues potentially affecting protein function. The significance of free thiols on the surface of plasmatic VWF has been confirmed previously with respect to platelet binding under pathologically high shear stress. Furthermore their potential involvement in functional VWF self-association occurring at elevated shear stress has been su

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12

Nikolaev, Anton, Iryna Makarchuk, Alexander Thesseling, Jo Hoeser, Thorsten Friedrich, Frédéric Melin, and Petra Hellwig. "Stabilization of the Highly Hydrophobic Membrane Protein, Cytochrome bd Oxidase, on Metallic Surfaces for Direct Electrochemical Studies." Molecules 25, no. 14 (July 16, 2020): 3240. http://dx.doi.org/10.3390/molecules25143240.

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The cytochrome bd oxidase catalyzes the reduction of oxygen to water in bacteria and it is thus an interesting target for electrocatalytic studies and biosensor applications. The bd oxidase is completely embedded in the phospholipid membrane. In this study, the variation of the surface charge of thiol-modified gold nanoparticles, the length of the thiols and the other crucial parameters including optimal phospholipid content and type, have been performed, giving insight into the role of these factors for the optimal interaction and direct electron transfer of an integral membrane protein. Impo

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13

Park, Jun Hyung, Buyng Su Park, Gu Huh, Seung Hyun Lee, Hyun Sook Lee, Il Hoon Cho, Se Hwan Paek, and Hai Won Lee. "Specific Immobilization of Streptavidin on Mixed Self-Assembled Monolayers as Mixing Ratio." Solid State Phenomena 121-123 (March 2007): 495–98. http://dx.doi.org/10.4028/www.scientific.net/ssp.121-123.495.

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We report on the distribution of mixed self-assembled monolayers (SAMs) composed of biotinylated and diluent alkylthiolates for streptavidin immobilization. Two thiol derivatives, 11-mercapto-1-undecanol (MUOH) and 11-mercaptoundecanoic-(8-biotinylamido-3,6-dioxaoctyl) amide (MBDA), were employed for mixed SAM. These thiols formed self-assembled monolayer without local domain, and streptavidins were immobilized onto biotinylated gold surface without nonspecific binding. In order to find the optimized condition of immobilization of streptavidin, we controlled the mixing ratio of two kind thiols

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14

Hou, Yong, Qingyou Xia, and Y. Adam Yuan. "Crystal structure of Bombyx mori nucleopolyhedrovirus ORF75 reveals a pseudo-dimer of thiol oxidase domains with a putative substrate-binding pocket." Journal of General Virology 93, no. 10 (October 1, 2012): 2142–51. http://dx.doi.org/10.1099/vir.0.042747-0.

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Bombyx mori nucleopolyhedrovirus (BmNPV) triggers the global shutdown of host silkworm gene expression and protein synthesis approximately 12–18 h post-infection. Genome sequence analysis suggests that BmNPV ORF75 could be a flavin adenine dinucleotide (FAD)-linked thiol oxidase essential for virion assembly and virus propagation. Here, we report the crystal structure of BmNPV ORF75 at 2.1 Å (0.21 nm). The structure of BmNPV ORF75 resembles that of the thiol oxidase domain of human quiescin thiol oxidase (QSOX), displaying a pseudo-dimer of canonical and non-canonical thiol oxidase domains. Ho

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15

Li, Zhipeng, Wei Xiong, Xiaojun He, Xiaoliang Qi, Feng Ding, and Jianliang Shen. "A novel strategy for rhodamine B-based fluorescent probes with a selective glutathione response for bioimaging in living cells." Analyst 145, no. 12 (2020): 4239–44. http://dx.doi.org/10.1039/d0an00582g.

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The aim of this study was to overcome the reported shortcomings of the glutathione (GSH) detection of rhodamine-based fluorescent probes, such as poor selectivity to thiol groups and reversible unstable covalent binding with the thiol groups.

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16

Salvarezza, Roberto Carlos, and Pilar Carro. "Exploring the core level shift origin of sulfur and thiolates on Pd(111) surfaces." Physical Chemistry Chemical Physics 17, no. 37 (2015): 24349–55. http://dx.doi.org/10.1039/c5cp04180e.

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DFT calculations show that the core level shift (CLS) of the S 2p binding energy of thiol and sulfur atoms on different thiol–Pd(111) surfaces strongly depends on the adsorbed or subsurface state of sulfur atoms.

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17

Xu, Yan, Xiao-Sheng Yan, Si-Bo Zhang, Shao-Wei Li, Ning-Shao Xia, Tao Jiang, Zhao Li, and Yun-Bao Jiang. "Nanospheres from coordination polymers of Ag⁺ with a highly hydrophilic thiol ligand formed in situ from dynamic covalent binding and a hydrophobic thiol." New Journal of Chemistry 45, no. 42 (2021): 19957–62. http://dx.doi.org/10.1039/d1nj03609b.

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A supramolecular nanosphere with a diameter of 8.7 nm is obtained in an aqueous alkaline solution via glucose binding to a boronic acid-based thiol (4-MPBA) as a hydrophilic ligand, together with a hydrophobic thiol ligand n-C8H17SH.

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18

LJUNGQUIST, Charlotta, Birger JANSSON, Tomas MOKS, and Mathias UHLEN. "Thiol-directed immobilization of recombinant IgG-binding receptors." European Journal of Biochemistry 186, no. 3 (December 1989): 557–61. http://dx.doi.org/10.1111/j.1432-1033.1989.tb15244.x.

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19

Palmer, M. "The family of thiol-activated, cholesterol-binding cytolysins." Toxicon 39, no. 11 (November 2001): 1681–89. http://dx.doi.org/10.1016/s0041-0101(01)00155-6.

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20

Billinge, Simon J. L., Emily J. McKimmy, Mouath Shatnawi, HyunJeong Kim, Valeri Petkov, Didier Wermeille, and Thomas J. Pinnavaia. "Mercury Binding Sites in Thiol-Functionalized Mesostructured Silica." Journal of the American Chemical Society 127, no. 23 (June 2005): 8492–98. http://dx.doi.org/10.1021/ja0506859.

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21

Krzykawska, A., J. Ossowski, T. Żaba, and P. Cyganik. "Binding groups for highly ordered SAM formation: carboxylic versus thiol." Chemical Communications 53, no. 42 (2017): 5748–51. http://dx.doi.org/10.1039/c7cc01939d.

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22

Chillé, Donatella, Viviana Mollica-Nardo, Ottavia Giuffrè, Rosina Celeste Ponterio, Franz Saija, Jiří Sponer, Sebastiano Trusso, Giuseppe Cassone, and Claudia Foti. "Binding of Arsenic by Common Functional Groups: An Experimental and Quantum-Mechanical Study." Applied Sciences 12, no. 6 (March 21, 2022): 3210. http://dx.doi.org/10.3390/app12063210.

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Arsenic is a well-known contaminant present in different environmental compartments and in human organs and tissues. Inorganic As(III) represents one of the most dangerous arsenic forms. Its toxicity is attributed to its great affinity with the thiol groups of proteins. Considering the simultaneous presence in all environmental compartments of other common functional groups, we here present a study aimed at evaluating their contribution to the As(III) complexation. As(III) interactions with four (from di- to hexa-) carboxylic acids, five (from mono- to penta-) amines, and four amino acids were

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23

Zhou, Zhou, Hiuwan Choi, Zhenyin Tao, Khatira Aboulfatova, Leticia Nolasco, Joel L. Moake, and Jing-fei Dong. "ADAMTS-13 Has a Disulfide Bond Reduction Activity on Von Willebrand Factor." Blood 112, no. 11 (November 16, 2008): 3934. http://dx.doi.org/10.1182/blood.v112.11.3934.3934.

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Abstract Von Willebrand factor (VWF) multimers tether platelets to subendothelium exposed at the site of vessel injury to initiate the bleeding arrest. Upon synthesized, VWF multimers are either constitutively secreted or packed into the storage granules, where they are enriched in ultra-large (UL) multimers that are active in forming spontaneous high strength bonds with the GP Ib-IX-V complex on platelets. This hyper-reactivity of ULVWF multimers is in contrast to VWF multimers circulating in plasma (pVWF) that need to be activated by modulators or high fluid shear stress to aggregate platele

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Morgan, M. S., R. M. Darrow, M. A. Nafz, and P. T. Varandani. "Participation of cellular thiol/disulphide groups in the uptake, degradation and bioactivity of insulin in primary cultures of rat hepatocytes." Biochemical Journal 225, no. 2 (January 15, 1985): 349–56. http://dx.doi.org/10.1042/bj2250349.

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The effects on the uptake (cell-associated 125I) and degradation (125I-labelled products released into the medium) of 125I-insulin and bioactivity (protein, glycogen and lipid synthesis) of insulin caused by altering the cellular thiol/disulphide status in primary cultures of rat hepatocytes were studied. Incubation of hepatocyte cultures with various exogenous thiol compounds (reduced glutathione, 2-mercaptoethanol, cysteamine, dithiothreitol) resulted in increased insulin binding, but markedly decreased degradation and bioactivity. These effects could be reversed by washing or by the additio

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Wang, Yifan, Ian Davis, Yan Chan, Sunil G. Naik, Wendell P. Griffith, and Aimin Liu. "Characterization of the nonheme iron center of cysteamine dioxygenase and its interaction with substrates." Journal of Biological Chemistry 295, no. 33 (June 28, 2020): 11789–802. http://dx.doi.org/10.1074/jbc.ra120.013915.

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Cysteamine dioxygenase (ADO) has been reported to exhibit two distinct biological functions with a nonheme iron center. It catalyzes oxidation of both cysteamine in sulfur metabolism and N-terminal cysteine-containing proteins or peptides, such as regulator of G protein signaling 5 (RGS5). It thereby preserves oxygen homeostasis in a variety of physiological processes. However, little is known about its catalytic center and how it interacts with these two types of primary substrates in addition to O2. Here, using electron paramagnetic resonance (EPR), Mössbauer, and UV-visible spectroscopies,

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Davies, Joshua, Carol Thomas, Mohammad Rizwan, and Christopher Gwenin. "Development of Electrochemical DNA Biosensor for Equine Hindgut Acidosis Detection." Sensors 21, no. 7 (March 26, 2021): 2319. http://dx.doi.org/10.3390/s21072319.

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The pH drop in the hindgut of the horse is caused by lactic acid-producing bacteria which are abundant when a horse’s feeding regime is excessively carbohydrate rich. This drop in pH below six causes hindgut acidosis and may lead to laminitis. Lactic acid-producing bacteria Streptococcus equinus and Mitsuokella jalaludinii have been found to produce high amounts of L-lactate and D-lactate, respectively. Early detection of increased levels of these bacteria could allow the horse owner to tailor the horse’s diet to avoid hindgut acidosis and subsequent laminitis. Therefore, 16s ribosomal ribonuc

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Khan, Samir A., Ana M. Rossi, Andrew M. Riley, Barry V. L. Potter, and Colin W. Taylor. "Subtype-selective regulation of IP3 receptors by thimerosal via cysteine residues within the IP3-binding core and suppressor domain." Biochemical Journal 451, no. 2 (March 28, 2013): 177–84. http://dx.doi.org/10.1042/bj20121600.

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IP3R (IP3 [inositol 1,4,5-trisphosphate] receptors) and ryanodine receptors are the most widely expressed intracellular Ca2+ channels and both are regulated by thiol reagents. In DT40 cells stably expressing single subtypes of mammalian IP3R, low concentrations of thimerosal (also known as thiomersal), which oxidizes thiols to form a thiomercurylethyl complex, increased the sensitivity of IP3-evoked Ca2+ release via IP3R1 and IP3R2, but inhibited IP3R3. Activation of IP3R is initiated by IP3 binding to the IBC (IP3-binding core; residues 224–604) and proceeds via re-arrangement of an interface

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Edmonds, S., A. Gibb, and E. Sim. "Effect of thiol compounds on human complement component C4." Biochemical Journal 289, no. 3 (February 1, 1993): 801–5. http://dx.doi.org/10.1042/bj2890801.

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Thiol compounds have been investigated as inhibitors of the covalent binding reaction of human complement protein C4 using Sepharose-C1s as a combined activating and binding surface. o- and p-substituted aminothiophenols are equally effective inhibitors, whereas the m-substituted compound is a less potent inhibitor. The anti-hypertensive drug captopril is also shown to inhibit the covalent binding reaction. A comparison of the effects of these compounds on the covalent binding reaction of isolated C4A and C4B has been made. Results suggest that a Pro-to-Leu substitution in C4B is likely to acc

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Gargantilla, Marta, José López-Fernández, Maria-Jose Camarasa, Leentje Persoons, Dirk Daelemans, Eva-Maria Priego, and María-Jesús Pérez-Pérez. "Inhibition of XPO-1 Mediated Nuclear Export through the Michael-Acceptor Character of Chalcones." Pharmaceuticals 14, no. 11 (November 6, 2021): 1131. http://dx.doi.org/10.3390/ph14111131.

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The nuclear export receptor exportin-1 (XPO1, CRM1) mediates the nuclear export of proteins that contain a leucine-rich nuclear export signal (NES) towards the cytoplasm. XPO1 is considered a relevant target in different human diseases, particularly in hematological malignancies, tumor resistance, inflammation, neurodegeneration and viral infections. Thus, its pharmacological inhibition is of significant therapeutic interest. The best inhibitors described so far (leptomycin B and SINE compounds) interact with XPO1 through a covalent interaction with Cys528 located in the NES-binding cleft of X

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Grill, V., and K. Fåk. "Influence of thiol groups, calcium, and glucose metabolism on cholinergic-induced insulin release and on methylscopolamine binding to muscarinic receptors in pancreatic islets of the rat." Acta Endocrinologica 109, no. 3 (July 1985): 355–60. http://dx.doi.org/10.1530/acta.0.1090355.

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Abstract. Short-term regulation of [3H]methylscopolamine binding to muscarinic receptors and acetylcholineinduced stimulation of insulin release was investigated in pancreatic islets of the rat. Binding of methylscopolamine was reversible; 47% of label was displaced 10 min and 70% 30 min after addition of unlabelled substance. 0.1 mm chloromercuribensoic acid, when present during binding incubations, inhibited binding by 54%, whereas acetylcholine-induced insulin release was unaffected by the presence of the thiol reactant. Pre-incubation for 60 min in a calcium-deprived medium or in the prese

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Müller, Andreas, and Burkhard König. "Vesicular aptasensor for the detection of thrombin." Chem. Commun. 50, no. 84 (2014): 12665–68. http://dx.doi.org/10.1039/c4cc05221h.

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Gonzalez-Fernandez, Federico, Dongjin Sung, Karen M. Haswell, Andrew Tsin, and Debashis Ghosh. "Thiol-dependent antioxidant activity of interphotoreceptor retinoid-binding protein." Experimental Eye Research 120 (March 2014): 167–74. http://dx.doi.org/10.1016/j.exer.2014.01.002.

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Basch, Harold, and Mark A. Ratner. "Molecular binding at gold transport interfaces. IV. Thiol chemisorption." Journal of Chemical Physics 120, no. 12 (March 22, 2004): 5771–80. http://dx.doi.org/10.1063/1.1650294.

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Rogers, Arlin B., Kathleen S. Cormier, and James G. Fox. "Thiol-reactive compounds prevent nonspecific antibody binding in immunohistochemistry." Laboratory Investigation 86, no. 5 (March 13, 2006): 526–33. http://dx.doi.org/10.1038/labinvest.3700407.

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Wu, X., N. H. Bishopric, D. J. Discher, B. J. Murphy, and K. A. Webster. "Physical and functional sensitivity of zinc finger transcription factors to redox change." Molecular and Cellular Biology 16, no. 3 (March 1996): 1035–46. http://dx.doi.org/10.1128/mcb.16.3.1035.

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Redox regulation of DNA-binding proteins through the reversible oxidation of key cysteine sulfhydryl groups has been demonstrated to occur in vitro for a range of transcription factors. The direct redox regulation of DNA binding has not been described in vivo, possibly because most protein thiol groups are strongly buffered against oxidation by the highly reduced intracellular environment mediated by glutathione, thioredoxin, and associated pathways. For this reason, only accessible protein thiol groups with high thiol-disulfide oxidation potentials are likely to be responsive to intracellular

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Yamauchi, Akira, and Eda T. Bloom. "Control of Cell Cycle Progression in Human Natural Killer Cells Through Redox Regulation of Expression and Phosphorylation of Retinoblastoma Gene Product Protein." Blood 89, no. 11 (June 1, 1997): 4092–99. http://dx.doi.org/10.1182/blood.v89.11.4092.

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Abstract Using thiol deprivation, we have previously shown that the response of natural killer (NK) cells to interleukin-2 (IL-2) is subject to redox regulation downstream of IL-2 binding and internalization. We have now used the IL-2–dependent cell line, NK3.3 to study redox regulation of NK cells further, and found that NK3.3 cells neither incorporated [3H]-thymidine nor completed the G1-S phase transition in medium lacking the thiol-related compounds, L-cystine, and glutathione, despite the presence of sufficient IL-2. Thiol deprivation did not alter the induction of DNA interferon-γ activa

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Shiri, Fereshteh, Somaye Shahraki, Sadegh Baneshi, Massoud Nejati-Yazdinejad, and Mostafa Heidari Majd. "Synthesis, characterization, in vitro cytotoxicity, in silico ADMET analysis and interaction studies of 5-dithiocarbamato-1,3,4-thiadiazole-2-thiol and its zinc(ii) complex with human serum albumin: combined spectroscopy and molecular docking investigations." RSC Advances 6, no. 108 (2016): 106516–26. http://dx.doi.org/10.1039/c6ra17322e.

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Astorga, Bethzaida, Theresa M. Wunz, Mark Morales, Stephen H. Wright, and Ryan M. Pelis. "Differences in the substrate binding regions of renal organic anion transporters 1 (OAT1) and 3 (OAT3)." American Journal of Physiology-Renal Physiology 301, no. 2 (August 2011): F378—F386. http://dx.doi.org/10.1152/ajprenal.00735.2010.

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This study examined the selectivity of organic anion transporters OAT1 and OAT3 for structural congeners of the heavy metal chelator 2,3-dimercapto-1-propanesulfonic acid (DMPS). Thiol-reactive reagents were also used to test structural predictions based on a homology model of OAT1 structure. DMPS was near equipotent in its ability to inhibit OAT1 (IC50 = 83 μM) and OAT3 (IC50 = 40 μM) expressed in Chinese hamster ovary cells. However, removal of a thiol group (3-mercapto-1-propanesulfonic acid) resulted in a 2.5-fold increase in IC50 toward OAT1 vs. a ∼55-fold increase in IC50 toward OAT3. Th

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39

Hinchliffe, Philip, Mariano M. González, Maria F. Mojica, Javier M. González, Valerie Castillo, Cecilia Saiz, Magda Kosmopoulou та ін. "Cross-class metallo-β-lactamase inhibition by bisthiazolidines reveals multiple binding modes". Proceedings of the National Academy of Sciences 113, № 26 (14 червня 2016): E3745—E3754. http://dx.doi.org/10.1073/pnas.1601368113.

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Metallo-β-lactamases (MBLs) hydrolyze almost all β-lactam antibiotics and are unaffected by clinically available β-lactamase inhibitors (βLIs). Active-site architecture divides MBLs into three classes (B1, B2, and B3), complicating development of βLIs effective against all enzymes. Bisthiazolidines (BTZs) are carboxylate-containing, bicyclic compounds, considered as penicillin analogs with an additional free thiol. Here, we show both l- and d-BTZ enantiomers are micromolar competitive βLIs of all MBL classes in vitro, with Kis of 6–15 µM or 36–84 µM for subclass B1 MBLs (IMP-1 and BcII, respec

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Sadowitz, Peter D., Bradley A. Hubbard, James C. Dabrowiak, Jerry Goodisman, Kirk A. Tacka, Mehmet K. Aktas, Mary J. Cunningham, Ronald L. Dubowy, and Abdul-Kader Souid. "Kinetics of Cisplatin Binding to Cellular DNA and Modulations by Thiol-Blocking Agents and Thiol Drugs." Drug Metabolism and Disposition 30, no. 2 (February 1, 2002): 183–90. http://dx.doi.org/10.1124/dmd.30.2.183.

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Qian, Yue-Cheng, Peng-Cheng Chen, Xue-Yan Zhu, and Xiao-Jun Huang. "Click synthesis of ionic strength-responsive polyphosphazene hydrogel for reversible binding of enzymes." RSC Advances 5, no. 55 (2015): 44031–40. http://dx.doi.org/10.1039/c5ra06649b.

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42

Paroo, Zain, Michael J. Meredith, Marius Locke, James V. Haist, Morris Karmazyn, and Earl G. Noble. "Redox signaling of cardiac HSF1 DNA binding." American Journal of Physiology-Cell Physiology 283, no. 2 (August 1, 2002): C404—C411. http://dx.doi.org/10.1152/ajpcell.00051.2002.

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Experiments involving chemical induction of the heat shock response in simple biological systems have generated the hypothesis that protein denaturation and consequential binding of heat shock transcription factor 1 (HSF1) to proximal heat shock elements (HSEs) on heat shock protein ( hsp) genes are the result of oxidation and/or depletion of intracellular thiols. The purpose of the present investigation was to determine the role of redox signaling of HSF1 in the intact animal in response to physiological and pharmacological perturbations. Heat shock and exercise induced HSF1-HSE DNA binding i

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Chen, C. C., W. J. Guo, and K. J. Isselbacher. "Rat intestinal trehalase. Studies of the active site." Biochemical Journal 247, no. 3 (November 1, 1987): 715–24. http://dx.doi.org/10.1042/bj2470715.

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Rat intestinal trehalase was solubilized, purified and reconstituted into proteoliposomes. With octyl glucoside as the solubilizing detergent, the purified protein appeared as a single band on SDS/polyacrylamide-gel electrophoresis with an apparent molecular mass of 67 kDa. Kinetic studies indicated that the active site of this enzyme can be functionally divided into two adjacent regions, namely a binding site (with pKa 4.8) and a catalytic site (with pKa 7.2). Other findings suggested that the catalytic site contains a functional thiol group, which is sensitive to inhibition by N-ethylmaleimi

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Muhammad Arfan, Muhammad Arfan, Sabahat Zahra Siddiqui Sabahat Zahra Siddiqui, Muhammad Athar Abbasi Muhammad Athar Abbasi, Aziz ur Rehman Aziz ur Rehman, Syed Adnan Ali Shah Syed Adnan Ali Shah, Muhammad Ashraf Muhammad Ashraf, Khalid Mohammed Khan Khalid Mohammed Khan, and Rahman Shah Zaib Saleem and Amna Shah Zaib Rahman Shah Zaib Saleem and Amna Shah Zaib. "Synthesis, Spectral Evaluation and in Silico Studies of S-Aralkylated 5-(4-methoxyphenyl)-4-phenyl-4H-1,2,4-triazole-3-thiols: As suitable Alzheimerand#39;s disease drug candidates." Journal of the chemical society of pakistan 43, no. 6 (2021): 694. http://dx.doi.org/10.52568/000974/jcsp/43.06.2021.

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Our efforts lay emphasis on synthesis of S-aralkylated 5-(4-OMeC6H5)-4-phenyl-4H-1,2,4-triazol-3-thiols like pharmacologically active candidates to counter neurodegenerative disorder; Alzheimerand#39;s disease. A synthetic strategy was instigated by esterifying 4-methoxybenzoic acid through Fisher esterificationand#39;s methodology. Hydrazinolysis of corresponding ester was performed under reflux with methanolic hydrated hydrazine to afford 4-methoxybenzohydrazide (I) which refluxing with phenyl isothiocyanate (II) in MeOH to yield a reactive intermediate (III). The later underwent base-cataly

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45

Lang, John D., Mario Figueroa, Phillip Chumley, Mutay Aslan, John Hurt, Margaret M. Tarpey, Beatriz Alvarez, Rafael Radi, and Bruce A. Freeman. "Albumin and Hydroxyethyl Starch Modulate Oxidative Inflammatory Injury to Vascular Endothelium." Anesthesiology 100, no. 1 (January 1, 2004): 51–58. http://dx.doi.org/10.1097/00000542-200401000-00012.

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Background Human serum albumin is used clinically to maintain colloid osmotic pressure and is viewed to serve an antioxidant role in the vascular compartment via binding of redox-active metal complexes, transport of nitric oxide, and the oxidant-scavenging reactions of the single thiol of human serum albumin, cys34. Because of these potentially desirable adjunctive actions, we evaluated the purity and thiol redox state and compared the relative effects of clinically available 25% human serum albumin preparations with a starch-derived colloid, 6% hydroxyethyl starch, in in vitro models of infla

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Taylor, Neil C., Gary Hessman, Holger B. Kramer, and Joanna F. McGouran. "Probing enzymatic activity – a radical approach." Chemical Science 11, no. 11 (2020): 2967–72. http://dx.doi.org/10.1039/c9sc05258e.

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Zucker, Marjorie B., and Evelyn A. Mauss. "Modification of Platelet Functions by Monobromobimane, a Fluorescent Thiol Group Label." Thrombosis and Haemostasis 55, no. 02 (1986): 228–34. http://dx.doi.org/10.1055/s-0038-1661527.

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SummaryMonobromobimane (mBBr, bimane), a compound that penetrates cells and forms a fluorescent adduct with thiol groups, was used to assess the significance of thiols in platelet function. Exposure of washed platelets for 1 min to 100 μM mBBr abolished ADP-induced aggregation; shape change was not inhibited by 500 μM mBBr. The nonpenetrating compound monobromotrimethylammoniobimane was ineffective. Established ADP-induced aggregation was reversed by bimane, and fibrinogen binding to ADP-stimulated platelets was inhibited, an effect mainly due to decreased number of binding sites. Aggregation

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López, María I., Dolores Esquivel, César Jiménez-Sanchidrián, Pascal Van Der Voort, and Francisco J. Romero-Salguero. "Thiol-Functionalized Ethylene Periodic Mesoporous Organosilica as an Efficient Scavenger for Palladium: Confirming the Homogeneous Character of the Suzuki Reaction." Materials 13, no. 3 (January 30, 2020): 623. http://dx.doi.org/10.3390/ma13030623.

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This work describes the synthesis of thiol-functionalized periodic mesoporous organosilicas (PMOs) prepared using the precursor 1-thiol-1,2-bis(triethoxysilyl)ethane, alone or mixed with 1,2-bis(triethoxysilyl)ethane. The thiol groups incorporated into the structure were found to be efficient for palladium binding. This has allowed these materials to be used as catalysts in the Suzuki cross-coupling reaction of bromobenzene and phenylboronic acid. Their performance has been compared to palladium-supported periodic mesoporous (organo)silicas and important differences have been observed between

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Zumbrennen, Kimberly B., Michelle L. Wallander, S. Joshua Romney, and Elizabeth A. Leibold. "Cysteine Oxidation Regulates the RNA-Binding Activity of Iron Regulatory Protein 2." Molecular and Cellular Biology 29, no. 8 (February 17, 2009): 2219–29. http://dx.doi.org/10.1128/mcb.00004-09.

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ABSTRACT Iron regulatory protein 2 (IRP2) is an RNA-binding protein that regulates the posttranscriptional expression of proteins required for iron homeostasis such as ferritin and transferrin receptor 1. IRP2 RNA-binding activity is primarily regulated by iron-mediated proteasomal degradation, but studies have suggested that IRP2 RNA binding is also regulated by thiol oxidation. We generated a model of IRP2 bound to RNA and found that two cysteines (C512 and C516) are predicted to lie in the RNA-binding cleft. Site-directed mutagenesis and thiol modification show that, while IRP2 C512 and C51

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Laroussi, Arwa, Małgorzata Kot, Jan Ingo Flege, Noureddine Raouafi, and Vladimir Mirsky. "Self-Assembled Monolayers from Symmetrical Di-Thiols: Preparation, Characterization and Application for the Assembly of Electrochemically Active Films." Engineering Proceedings 6, no. 1 (May 17, 2021): 17. http://dx.doi.org/10.3390/i3s2021dresden-10112.

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1,3-dimercaptopropan-2-ol, a symmetrical di-thiol, has been synthesized and applied as a new type of anchor molecule to prepare a self-assembled monolayer (SAM) on a gold surface. The formed monolayers were studied by cyclic voltammetry, impedance spectroscopy, X-ray photoelectron spectroscopy, kinetic capacitance, and contact angle measurements. The SAM structure depends on the adsorption conditions. A short incubation time of the electrode at high concentration of this di-thiol leads to the predominating binding through one thiol group of the adsorbate to the gold surface, while a long incub

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