Relevant bibliographies by topics / Cysteines

Academic literature on the topic 'Cysteines'

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Published: 4 June 2021
Last updated: 6 July 2024

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Journal articles on the topic "Cysteines"

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Natesan, Ramakrishnan, Andrew B. Dykstra, Akash Banerjee, and Neeraj J. Agrawal. "Heterogeneity in Disulfide Bond Reduction in IgG1 Antibodies Is Governed by Solvent Accessibility of the Cysteines." Antibodies 12, no. 4 (December 13, 2023): 83. http://dx.doi.org/10.3390/antib12040083.

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We studied unpaired cysteine levels and disulfide bond susceptibility in four different γ-immunoglobulin antibodies using liquid chromatography–mass spectrometry. Our choice of differential alkylating agents ensures that the differential peaks are non-overlapping, thus allowing us to accurately quantify free cysteine levels. For each cysteine residue, we observed no more than 5% to be unpaired, and the free cysteine levels across antibodies were slightly higher in those containing lambda light chains. Interchain and hinge residues were highly susceptible to reducing stresses and showed a 100–1000-fold higher rate of reduction compared to intrachain cysteines. Estimations of the solvent-accessible surface for individual cysteines in IgG1, using an implicit all-atom molecular dynamics simulation, show that interchain and hinge cysteines have >1000-fold higher solvent accessibility compared to intrachain cysteines. Further analyses show that solvent accessibility and the rate of reduction are linearly correlated. Our work clearly establishes the fact that a cysteine’s accessibility to the surrounding solvent is one of the primary determinants of its disulfide bond stability.
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Kisty, Eleni A., Emma C. Saart, and Eranthie Weerapana. "Identifying Redox-Sensitive Cysteine Residues in Mitochondria." Antioxidants 12, no. 5 (April 25, 2023): 992. http://dx.doi.org/10.3390/antiox12050992.

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The mitochondrion is the primary energy generator of a cell and is a central player in cellular redox regulation. Mitochondrial reactive oxygen species (mtROS) are the natural byproducts of cellular respiration that are critical for the redox signaling events that regulate a cell’s metabolism. These redox signaling pathways primarily rely on the reversible oxidation of the cysteine residues on mitochondrial proteins. Several key sites of this cysteine oxidation on mitochondrial proteins have been identified and shown to modulate downstream signaling pathways. To further our understanding of mitochondrial cysteine oxidation and to identify uncharacterized redox-sensitive cysteines, we coupled mitochondrial enrichment with redox proteomics. Briefly, differential centrifugation methods were used to enrich for mitochondria. These purified mitochondria were subjected to both exogenous and endogenous ROS treatments and analyzed by two redox proteomics methods. A competitive cysteine-reactive profiling strategy, termed isoTOP-ABPP, enabled the ranking of the cysteines by their redox sensitivity, due to a loss of reactivity induced by cysteine oxidation. A modified OxICAT method enabled a quantification of the percentage of reversible cysteine oxidation. Initially, we assessed the cysteine oxidation upon treatment with a range of exogenous hydrogen peroxide concentrations, which allowed us to differentiate the mitochondrial cysteines by their susceptibility to oxidation. We then analyzed the cysteine oxidation upon inducing reactive oxygen species generation via the inhibition of the electron transport chain. Together, these methods identified the mitochondrial cysteines that were sensitive to endogenous and exogenous ROS, including several previously known redox-regulated cysteines and uncharacterized cysteines on diverse mitochondrial proteins.
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Kordyukova, Larisa V., Marina V. Serebryakova, Ludmila A. Baratova, and Michael Veit. "S Acylation of the Hemagglutinin of Influenza Viruses: Mass Spectrometry Reveals Site-Specific Attachment of Stearic Acid to a Transmembrane Cysteine." Journal of Virology 82, no. 18 (July 2, 2008): 9288–92. http://dx.doi.org/10.1128/jvi.00704-08.

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ABSTRACT S acylation of cysteines located in the transmembrane and/or cytoplasmic region of influenza virus hemagglutinins (HA) contributes to the membrane fusion and assembly of virions. Our results from using mass spectrometry (MS) show that influenza B virus HA possessing two cytoplasmic cysteines contains palmitate, whereas HA-esterase-fusion glycoprotein of influenza C virus having one transmembrane cysteine is stearoylated. HAs of influenza A virus having one transmembrane and two cytoplasmic cysteines contain both palmitate and stearate. MS analysis of recombinant viruses with deletions of individual cysteines, as well as tandem-MS sequencing, revealed the surprising result that stearate is exclusively attached to the cysteine positioned in the transmembrane region of HA.
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Rainwater, R., D. Parks, M. E. Anderson, P. Tegtmeyer, and K. Mann. "Role of cysteine residues in regulation of p53 function." Molecular and Cellular Biology 15, no. 7 (July 1995): 3892–903. http://dx.doi.org/10.1128/mcb.15.7.3892.

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Previous studies of p53 have implicated cysteine residues in site-specific DNA binding via zinc coordination and redox regulation (P. Hainaut and J. Milner, Cancer Res. 53:4469-4473, 1993; T. R. Hupp, D. W. Meek, C. A. Midgley, and D. P. Lane, Nucleic Acids Res. 21:3167-3174, 1993). We show here that zinc binding and redox regulation are, at least in part, distinct determinants of the binding of p53 to DNA. Moreover, by substituting serine for each cysteine in murine p53, we have investigated the roles of individual cysteines in the regulation of p53 function. Substitution of serine for cysteine at position 40, 179, 274, 293, or 308 had little or no effect on p53 function. In contrast, replacement of cysteine at position 173, 235, or 239 markedly reduced in vitro DNA binding, completely blocked transcriptional activation, and led to a striking enhancement rather than a suppression of transformation by p53. These three cysteines have been implicated in zinc binding by X-ray diffraction studies (Y. Cho, S. Gorina, P.D. Jeffrey, and N.P. Pavletich, Science 265:346-355, 1994); our studies demonstrate the functional consequences of the inability of the central DNA-binding domain of p53 to studies demonstrate the functional consequences of the inability of the central DNA-binding domain of p53 to bind zinc. Lastly, substitutions for cysteines at position 121, 132, 138, or 272 partially blocked both transactivation and the suppression of transformation by p53. These four cysteines are located in the loop-sheet-helix region of the site-specific DNA-binding domain of p53. Like the cysteines in the zinc-binding region, therefore, these cysteines may cooperate to modulate the structure of the DNA-binding domain. Our findings argue that p53 is subject to more than one level of conformational modulation through oxidation-reduction of cysteines at or near the p53-DNA interface.
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Huang, Jingjing, Patrick Willems, Bo Wei, Caiping Tian, Renan B. Ferreira, Nandita Bodra, Santiago Agustín Martínez Gache, et al. "Mining for protein S-sulfenylation in Arabidopsis uncovers redox-sensitive sites." Proceedings of the National Academy of Sciences 116, no. 42 (October 2, 2019): 21256–61. http://dx.doi.org/10.1073/pnas.1906768116.

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Hydrogen peroxide (H2O2) is an important messenger molecule for diverse cellular processes. H2O2 oxidizes proteinaceous cysteinyl thiols to sulfenic acid, also known as S-sulfenylation, thereby affecting the protein conformation and functionality. Although many proteins have been identified as S-sulfenylation targets in plants, site-specific mapping and quantification remain largely unexplored. By means of a peptide-centric chemoproteomics approach, we mapped 1,537 S-sulfenylated sites on more than 1,000 proteins in Arabidopsis thaliana cells. Proteins involved in RNA homeostasis and metabolism were identified as hotspots for S-sulfenylation. Moreover, S-sulfenylation frequently occurred on cysteines located at catalytic sites of enzymes or on cysteines involved in metal binding, hinting at a direct mode of action for redox regulation. Comparison of human and Arabidopsis S-sulfenylation datasets provided 155 conserved S-sulfenylated cysteines, including Cys181 of the Arabidopsis MITOGEN-ACTIVATED PROTEIN KINASE4 (AtMAPK4) that corresponds to Cys161 in the human MAPK1, which has been identified previously as being S-sulfenylated. We show that, by replacing Cys181 of recombinant AtMAPK4 by a redox-insensitive serine residue, the kinase activity decreased, indicating the importance of this noncatalytic cysteine for the kinase mechanism. Altogether, we quantitatively mapped the S-sulfenylated cysteines in Arabidopsis cells under H2O2 stress and thereby generated a comprehensive view on the S-sulfenylation landscape that will facilitate downstream plant redox studies.
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Bartosz-Bechowski, H., R. Miedzybrodzki, and S. Szymaniec. "Novel nociceptin analogues." Acta Biochimica Polonica 48, no. 4 (December 31, 2001): 1155–58. http://dx.doi.org/10.18388/abp.2001_3883.

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A series of new nociceptin analogues containing cysteine was tested for their nociceptive effects in tail-flick test on mice after icv injection. The cysteines were introduced in order to get irreversibly binding analogues based on the assumption that the cysteines in the ligand can interact with the cysteines from the receptor to form an S-S bridge. In vivo tests revealed that Cys1-nociceptin (1-13)-NH2 (Cys1-NC) is an antagonist, whereas Cys7-NC is an agonist. Gly1[Phe(p-NO2)]4-NC was less active indicating that the antagonist properties of Cys1-NC are associated with the presence of the sulfhydryl group of cysteine. The analogues D-Cys2 and Cys3 were also almost inactive.
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Morgan, Sarah J., Emily L. French, Joshua J. Thomson, Craig P. Seaborn, Christian A. Shively, and Eric S. Krukonis. "Formation of an Intramolecular Periplasmic Disulfide Bond in TcpP Protects TcpP and TcpH from Degradation in Vibrio cholerae." Journal of Bacteriology 198, no. 3 (November 16, 2015): 498–509. http://dx.doi.org/10.1128/jb.00338-15.

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ABSTRACTTcpP and ToxR coordinately regulate transcription oftoxT, the master regulator of numerous virulence factors inVibrio cholerae. TcpP and ToxR are membrane-localized transcription factors, each with a periplasmic domain containing two cysteines. In ToxR, these cysteines form an intramolecular disulfide bond and a cysteine-to-serine substitution affects activity. We determined that the two periplasmic cysteines of TcpP also form an intramolecular disulfide bond. Disruption of this intramolecular disulfide bond by mutation of either cysteine resulted in formation of intermolecular disulfide bonds. Furthermore, disruption of the intramolecular disulfide bond in TcpP decreased the stability of TcpP. While the decreased stability of TcpP-C207S resulted in a nearly complete loss oftoxTactivation and cholera toxin (CT) production, the second cysteine mutant, TcpP-C218S, was partially resistant to proteolytic degradation and maintained ∼50%toxTactivation capacity. TcpP-C218S was also TcpH independent, since deletion oftcpHdid not affect the stability of TcpP-C218S, whereas wild-type TcpP was degraded in the absence of TcpH. Finally, TcpH was also unstable when intramolecular disulfides could not be formed in TcpP, suggesting that the single periplasmic cysteine in TcpH may assist with disulfide bond formation in TcpP by interacting with the periplasmic cysteines of TcpP. Consistent with this finding, a TcpH-C114S mutant was unable to stabilize TcpP and was itself unstable. Our findings demonstrate a periplasmic disulfide bond in TcpP is critical for TcpP stability and virulence gene expression.IMPORTANCETheVibrio choleraetranscription factor TcpP, in conjunction with ToxR, regulates transcription oftoxT, the master regulator of numerous virulence factors inVibrio cholerae. TcpP is a membrane-localized transcription factor with a periplasmic domain containing two cysteines. We determined that the two periplasmic cysteines of TcpP form an intramolecular disulfide bond and disruption of the intramolecular disulfide bond in TcpP decreased the stability of TcpP and reduced virulence gene expression. Normally TcpH, another membrane-localized periplasmic protein, protects TcpP from degradation. However, we found that TcpH was also unstable when intramolecular disulfides could not be formed in TcpP, indicating that the periplasmic cysteines of TcpP are required for functional interaction with TcpH and that this interaction is required for both TcpP and TcpH stability.
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Bocedi, Cattani, Gambardella, Ticconi, Cozzolino, Di Fusco, Pucci, and Ricci. "Ultra-Rapid Glutathionylation of Ribonuclease: Is this the Real Incipit of its Oxidative Folding?" International Journal of Molecular Sciences 20, no. 21 (October 31, 2019): 5440. http://dx.doi.org/10.3390/ijms20215440.

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Many details of oxidative folding of proteins remain obscure, in particular, the role of oxidized glutathione (GSSG). This study reveals some unknown aspects. When a reduced ribonuclease A refolds in the presence of GSSG, most of its eight cysteines accomplish a very fast glutathionylation. In particular, one single cysteine, identified as Cys95 by mass spectrometry, displays 3600 times higher reactivity when compared with an unperturbed protein cysteine. Furthermore, the other five cysteines show 40–50 times higher reactivity toward GSSG. This phenomenon is partially due to a low pKa value of most of these cysteines (average pKa = 7.9), but the occurrence of a reversible GSSG-ribonuclease complex (KD = 0.12 mM) is reasonably responsible for the extraordinary hyper-reactivity of Cys95. Neither hyper-reactivity nor some protein-disulfide complexes have been found by reacting a reduced ribonuclease with other natural disulfides i.e., cystine, cystamine, and homocystine. Hyper-reactivity of all cysteines was observed toward 5,5’-dithiobis-(2-nitrobenzoic acid). Given that GSSG is present in high concentrations in the endoplasmic reticulum, this property may shed light on the early step of its oxidative folding. The ultra-rapid glutathionylation of cysteines, only devoted to form disulfides, is a novel property of the molten globule status of the ribonuclease.
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Betakova, Tatiana, and Bernard Moss. "Disulfide Bonds and Membrane Topology of the Vaccinia Virus A17L Envelope Protein." Journal of Virology 74, no. 5 (March 1, 2000): 2438–42. http://dx.doi.org/10.1128/jvi.74.5.2438-2442.2000.

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ABSTRACT The envelope protein encoded by the vaccinia virus A17L open reading frame is essential for virion assembly. Our mutagenesis studies indicated that cysteines 101 and 121 form an intramolecular disulfide bond and that cysteine 178 forms an intermolecular disulfide linking two A17L molecules. This arrangement of disulfide bonds has important implications for the topology of the A17L protein and supports a two-transmembrane model in which cysteines 101 and 121 are intraluminal and cysteine 178 is cytoplasmic. The structure of the A17L protein, however, was not dependent on these disulfide bonds, as a recombinant vaccinia virus with all three cysteine codons mutated to serines retained infectivity.
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MEULLER, Johan, Junwei ZHANG, Cynthia HOU, Philip D. BRAGG, and Jan RYDSTRÖM. "Properties of a cysteine-free proton-pumping nicotinamide nucleotide transhydrogenase." Biochemical Journal 324, no. 2 (June 1, 1997): 681–87. http://dx.doi.org/10.1042/bj3240681.

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Nicotinamide nucleotide transhydrogenase from Escherichia coli was investigated with respect to the roles of its cysteine residues. This enzyme contains seven cysteines, of which five are located in the α subunit and two are in the β subunit. All cysteines were replaced by site-directed mutagenesis. The final construct (αC292T, αC339T, αC395S, αC397T, αC435S, βC147S, βC260S) was inserted normally in the membrane and underwent the normal NADPH-dependent conformational change of the β subunit to a trypsin-sensitive state. Reduction of NADP+ by NADH driven by ATP hydrolysis or respiration was between 32% and 65% of the corresponding wild-type activities. Likewise, the catalytic and proton pumping activities of the purified cysteine-free enzyme were at least 30% of the purified wild-type enzyme activities. The H+/H- ratio for both enzymes was 0.5, although the cysteine-free enzyme appeared to be more stable than the wild-type enzyme in proteoliposomes. No bound NADP(H) was detected in the enzymes. Modification of transhydrogenase by diethyl pyrocarbonate and the subsequent inhibition of the enzyme were unaffected by removal of the cysteines, indicating a lack of involvement of cysteines in this process. Replacement of cysteine residues in the α subunit resulted in no or little change in activity, suggesting that the basis for the decreased activity was probably the modification of the conserved β-subunit residue Cys-260 or (less likely) the non-conserved β-subunit residue Cys-147. It is concluded that the cysteine-free transhydrogenase is structurally and mechanistically very similar to the wild-type enzyme, with minor modifications of the properties of the NADP(H) site, possibly mediated by the βC260S mutation. The cysteine-free construct will be a valuable tool for studying structure–function relationships of transhydrogenases.
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Dissertations / Theses on the topic "Cysteines"

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Takeda, Armelle-Natsuo. "Role of intracellular cysteines in ENaC function." Paris 6, 2009. http://www.theses.fr/2009PA066110.

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Le canal épithélial sodique ENaC est responsable de la réabsorption du sodium dans les cellules principales du tubule collecteur rénal. La cristallisation d'ASIC, un autre membre de la famille ENaC/Deg, a été publiée mais la constitution du pore interne reste indéterminée. La mutation aS589C du filtre de sélectivité d'ENaC permet le passage du Cd2+ externe capable d'inhiber le canal muté. Nous avons montré que la chaine latérale de la aSer589 n'est pas orientée vers l'intérieur du pore, permettant au Cd2+ de traverser le canal et d'interagir avec la cysteine gCys546. Puis nous nous sommes intéressés au mécanisme d'inhibition d'ENaC par les réactifs sulfhydryl (MTS) internes. Nous avons mis en place une nouvelle approche couplant la méthode d'analyse par substitution de cystéines avec des perfusions internes de MTSEA-biotine. Ainsi, nous pouvons mettre en corrélation les acides aminés accessibles aux MTS internes et ceux qui sont importants dans la fonction du canal.
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Du, Aiguo. "Prediction of Oxidation States of Cysteines and Disulphide Connectivity." Digital Archive @ GSU, 2007. http://digitalarchive.gsu.edu/cs_diss/28.

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Knowledge on cysteine oxidation state and disulfide bond connectivity is of great importance to protein chemistry and 3-D structures. This research is aimed at finding the most relevant features in prediction of cysteines oxidation states and the disulfide bonds connectivity of proteins. Models predicting the oxidation states of cysteines are developed with machine learning techniques such as Support Vector Machines (SVMs) and Associative Neural Networks (ASNNs). A record high prediction accuracy of oxidation state, 95%, is achieved by incorporating the oxidation states of N-terminus cysteines, flanking sequences of cysteines and global information on the protein chain (number of cysteines, length of the chain and amino acids composition of the chain etc.) into the SVM encoding. This is 5% higher than the current methods. This indicates to us that the oxidation states of amino terminal cysteines infer the oxidation states of other cysteines in the same protein chain. Satisfactory prediction results are also obtained with the newer and more inclusive SPX dataset, especially for chains with higher number of cysteines. Compared to literature methods, our approach is a one-step prediction system, which is easier to implement and use. A side by side comparison of SVM and ASNN is conducted. Results indicated that SVM outperform ASNN on this particular problem. For the prediction of correct pairings of cysteines to form disulfide bonds, we first study disulfide connectivity by calculating the local interaction potentials between the flanking sequences of the cysteine pairs. The obtained interaction potential is further adjusted by the coefficients related to the binding motif of enzymes during disulfide formation and also by the linear distance between the cysteine pairs. Finally, maximized weight matching algorithm is applied and performance of the interaction potentials evaluated. Overall prediction accuracy is unsatisfactory compared with the literature. SVM is used to predict the disulfide connectivity with the assumption that oxidation states of cysteines on the protein are known. Information on binding region during disulfide formation, distance between cysteine pairs, global information of the protein chain and the flanking sequences around the cysteine pairs are included in the SVM encoding. Prediction results illustrate the advantage of using possible anchor region information.
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Hall, Christopher. "The synthesis, enzymic and chemical reactivity of S-glycosyl cysteines." Thesis, University of Surrey, 2005. http://epubs.surrey.ac.uk/842924/.

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A number of N-acetyl-S-glycosyl cysteine derivatives have been prepared through the development of a general and simply applicable synthetic pathway, by modifying existing literature methods. The coupling of N-acetyl-L-cysteine and a carbohydrate is desirable as it may improve the efficacy of the labile N-acetyl-L-cysteine as a drug. The S-glycosyl cysteines prepared are as follows: N-acetyl-S-D-glucopyranosyl-L-cysteine, alpha and beta-anomers, N-acetyl-S-beta-D-ribopyranosyl-L-cysteine, N-acetyl-S-alpha-D-mannopyranosyl-L-cysteine and N-acetyl-O-methyl-S-(2,3,4,6-tetra-O-benzoyl-beta-D-galactopyranosyl)-L-cysteine. The coupling reaction was designed to yield both a and beta-anomers in the same step, and this was observed in the synthesis of the glucose derivatives. However, the other carbohydrates chosen appear to couple more selectively. The preparation of N-acetyl-O-methyl-S-alpha-D-glucopyranosyl-L-cysteine was also carried out by a different method, but this proved to be more involved and resulted in lower yields. The stability of N-acetyl-S-beta-D-glucopyranosyl-L-cysteine towards the thioglycosidase enzyme myrosinase was studied. N-acetyl-S-beta-D-glucopyranosyl-L- cysteine was found to be stable to hydrolysis by myrosinase, but some inhibition of a standard sinigrin-myrosinase hydrolysis was observed. The thioglycosidic linkage (-SH) of N-acetyl-S-beta-D-glucopyranosyl-L-cysteine is stable to hydrolysis in acidic media, which is contrary to previous work reported in the literature. However, the hydrolysis of the amide group of the cysteine side chain occurred in acidic solution giving the apparently acid-stable S-beta-D-glucopyranosyl-L-cysteine. A kinetic study of this acetyl cleavage was undertaken and a second order rate constant of 5.96 +/- 0.24 x 10-4 dm3 mol-1 hours-1 was obtained.
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Du, Aiguo. "Prediction of oxidation states of cysteines and disulphide bridges in proteins." unrestricted, 2007. http://etd.gsu.edu/theses/available/etd-11272007-024411/.

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Thesis (Ph. D.)--Georgia State University, 2007.
Title from file title page. Y. Pan, committee chair; G. Qin, A. Bourgeois, A. Zelikovski, committee members. Electronic text (124 p. : ill. (some col.)) : digital, PDF file. Description based on contents viewed June 3, 2008. Includes bibliographical references (p. 111-124).
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Lacey, Brian. "Investigation Into the Role of the C-Terminal Vicinal Cysteine Residues in High MR Thioredoxin Reductases." ScholarWorks @ UVM, 2008. http://scholarworks.uvm.edu/graddis/130.

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Mammalian thioredoxin reductase (TR) contains the rare amino acid selenocysteine (Sec), which is essential for the enzyme’s catalytic activity. Substitution of the catalytic Sec residue for a cysteine (Cys) residue, results in a drop in kcat of 100- fold. Homologous high molecular weight TRs from other eukaryotes such as D. melanogaster and C. elegans, have naturally evolved a Sec to Cys substitution in their active sites and these enzymes function with high catalytic activity without the need for a Sec residue. Thus, various TRs can catalyze an identical reaction with either a Cys or Sec residue. A natural assumption in the field has always been that the lower nucleophilicity of a Cys thiol, relative to the selenol of Sec, is the reason for the much lower activity of the mammalian Cys-containing mutant. However, here I provide an alternative explanation. High Mr TRs contain either a Cys-Cys or Cys-Sec dyad that forms an eight-membered ring in the oxidized state during the redox cycle of the enzyme. These eight-membered ring structures are rare in protein structures, presumably due to the strain induced in the intervening peptide bond between the Cys residues. Here I take a “chemical approach” to studying the enzyme mechanism of TR by breaking it into two pieces. This approach is possible because of TR’s structural and mechanistic similarity to glutathione reductase (GR). In comparison to GR, TR contains an additional thiol-disulfide exchange step resulting from the presence of a sixteen amino acid C-terminal extension containing either a vicinal disulfide bond or vicinal selenylsulfide bond. This additional thiol-disulfide exchange step is in the form of the reduction and opening of the eight-membered ring motif. I have constructed a truncated version of the enzyme lacking the amino acid sequence possessing the ring motif so that I could isolate this ring-opening step from the rest of the catalytic cycle by using peptide disulfides/selenylsulfides as substrates. The results of this study using peptide substrates show that the ring opening step is the step of the catalytic cycle that is most effected by Sec to Cys substitution because the higher pKa of the Cys thiolate in comparison to the Sec selenolate means that the Cys residue must be protonated in this step.
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Heckler, Erin J. "Human quiescin-sulhydryl oxidase 1b role of CxxC motif cysteines in catalysis /." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file, 174 p, 2009. http://proquest.umi.com/pqdweb?did=1818417401&sid=5&Fmt=2&clientId=8331&RQT=309&VName=PQD.

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Cutrera, Jason Lewis. "Insights into the Structure and Function of PrgW and its Conserved Cysteines." Diss., Temple University Libraries, 2014. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/299645.

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Microbiology and Immunology
Ph.D.
Enterococcus faecalis is a Gram-positive bacterial species that is typically a member of the human gastrointestinal tract microbiota. However, E. faecalis is also a nosocomial pathogen, which is involved in urinary tract infections, soft tissue infections and endocarditis. In recent times, the occurrence of antibiotic resistance has complicated the treatment of these infections. One of the major differences between commensal and pathogenic strains of E. faecalis is that pathogens contain multiple mobile elements such as plasmids, transposons and integrative conjugative elements (ICE). These elements allow for the acquisition and transfer of virulence factors and resistance genes. Conjugative plasmids are a class of plasmids present in E. faecalis whose transfer to host cells is induced by a small pheromone peptide, cCF10 (LVTLVFV). This peptide is initially encoded as a 22-amino acid precursor (pre-cCF10) from the signal sequence of the chromosomal ccfA gene and is then proteolytically cleaved by signal peptidase II and Eep. Once pCF10 has been transferred a host E. faecalis cell, it is exceptionally stable. A replicon clone is maintained in greater than 85% of host cells over 100 generations in the absence of selection, suggesting the stability of pCF10 is intrinsic to the replicon. Three unique features of the replication initiation protein PrgW may contribute to this stability: (a) the interaction of PrgW with pre-cCF10, (b) disulfide bond formation at three conserved cysteines (C78, C275, and C307) in PrgW, and (c) processing of the nascent PrgW protein. Replication initiation proteins associated with theta replicons, such as pCF10, are often self-contained units. To initiate plasmid replication, the replication initiation protein (PrgW) binds to direct repeats (oriV) in its own coding sequence (prgW). In silico analysis of PrgW suggests the existence of three distinct domains within the protein. The first 122 amino acids are homologous to a conserved domain present in related replication initiation proteins, which includes a Helix-Turn-Helix (HTH) DNA binding domain. This suggests that this domain of PrgW has a DNA-binding function and binds to the oriV site in prgW. The following 61 amino acids are not similar to any known sequence, and are encoded by the DNA sequence containing the direct repeats in the oriV site. This domain may or may not have a distinct function. The remaining sequence forms a domain that contains cysteines C275 and C307, and is also similar to no known structure. It is hypothesized that this domain is related to the stability of pCF10. C307 appears to be critical, as previous experiments indicate that its mutation alone affects plasmid stability. Secondary structure analysis of this domain revealed the presence of multiple alpha-helices that contain distinct hydrophobic domains that possibly contribute to pre-cCF10 binding and PrgW tertiary structure. The positions of the conserved cysteines within these alpha-helices may stabilize a hydrophobic binding pocket that could potentially facilitate interaction with pre-cCF10. PrgW has a predicted molecular weight of 38.6 KDa and can be detected in Western blots as a band with an apparent approximate molecular weight (mw) of 36,000. Previous data from our lab indicates that, when overexpressed in E. faecalis, four bands of PrgW are present with observed molecular weights of 40,000, 36,000, 24,000 and 18,000. Time course experiments revealed that the 40,000 mw form is converted to a 36,000 mw form independent. The 40,000 mw form is unstable (with a complete turnover in 30 minutes) while the 36,000 mw form has a half-life of greater than 4 hours. The 24,000 mw band does not have a DNA binding motif and is likely a turnover product. When the three conserved cysteines (and only cysteines) in PrgW are replaced with alanine, the 40,000 mw form is still processed to the 36,000 mw form. However, the cysteine to alanine mutants accumulate the 36,000 mw form.
Temple University--Theses
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Hagedorn, Tara Dawn. "Reactive Sulfur: Redox Reactions of Cysteines and Methionines in the Cytoskeletal Protein Tubulin." W&M ScholarWorks, 2011. https://scholarworks.wm.edu/etd/1539626916.

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Lin, Liwen. "Comprehensive identification of nitroxyl-reactive cysteines in human platelet proteins by quantitative mass spectrometry." Thesis, University of British Columbia, 2011. http://hdl.handle.net/2429/37089.

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HNO, a small compound which can be produced upon hydrolysis of Angeli’s Salt, is known to be able to inhibit platelet aggregation. An important step to elucidate the mechanism of the antiaggregatory effect of HNO and define the drug’s targets is the identification of HNO-reactive proteins in platelets. The sulfhydryl group is considered the major target of HNO. It can be modified into either sulfinamide or disulfide. The sulfinamide modification is directly detectable by mass spectrometry; however, cysteines converted into disulfide groups by HNO cannot be monitored this way, because the origin of the other cysteine it reacts with is unknown. The goal of this thesis was to identify HNO-reactive cysteines in human platelet proteins regardless of the eventual modification states and discover cysteines which might play key roles in platelet inhibition by HNO. In the first series of studies, a differential alkylation method was developed, evaluated on a protein model and applied on human platelets to identify HNO-reactive cysteines. The results show that 32 HNO-reactive cysteines from 18 proteins were identified. Moreover, utilizing the detectable mass shift derived from sulfinamide, the modification states (i.e., sulfinamide or disulfide) of the 32 HNO-reactive cysteines were further investigated. In the second series of studies, isotope-coded affinity tag enrichment was combined with the differential alkylation method to increase the number of HNO-reactive cysteines discovered. The results show that 159 HNO-reactive cysteines from 78 proteins were identified. Studies have shown that platelet inhibition by HNO was time-dependent; the effect was not evident after 60 minutes of incubation with HNO. Therefore, a time-dependent study was performed to identify cysteines whose HNO-induced modifications were reversed after 60 minutes of incubation. The results show that the modifications of 83 cysteines out of the 159 HNO-reactive cysteines were reversible. Based on the reactivity toward HNO, the reversibility of HNO-induced modifications and the biological functions, talin, filamin, α-actinin and integrin αIIbβ3 are proposed as potential drug targets that may play key roles in platelet inhibition by HNO.
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Guo, Xiaodan. "The role of C-terminal cysteines in regulating human proteinase-activated receptor-1 function." Thesis, University of Hull, 2010. http://hydra.hull.ac.uk/resources/hull:4483.

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Proteinase-activated receptors (PARs) are a novel group of G-protein coupled receptors (GPCRs). The most striking evidence to distinguish them from other GPCRs is that they carry their own tethered ligand within extracellular N-terminus. To activate the receptors, the tethered ligand is exposed by proteolytic cleavage which subsequently binds to the extracellular loop 2 to trigger receptor function. Four members have been identified so far in this group—PAR1, PAR2, PAR3 and PAR4. Palmitoylation is the reversible covalent attachment of fatty acids to the cysteine residues of some GPCRs via a thioester linkage; resulting in a fourth intracellular loop. Although recent evidence has suggested that palmitoylation can have a profound effect on GPCR function such as cell surface expression and receptor signalling, the role of palmitoylation in regulating PAR function is currently unknown. This study focused on the role of putative palmitoylation region of hPAR1--C-terminal cysteines (C387and C388) in regulating receptor function. Wild type hPAR1 (wt-hPAR1) and hPAR1 mutants (hPAR1C387A, hPAR1C388A and hPAR1C387AC388A) were constructed and permanently expressed in Kirsten virus sarcoma transformed rat kidney epithelial cells (KNRK). hPAR1C387A and hPAR1C388A displayed similar cell surface expression (~80%) to that of wt-hPAR1, but hPAR1C387AC388A displayed only ~40% cell surface expression. hPAR1C387A, hPAR1C388A and wt-hPAR1 displayed similar sensitivity in calcium signalling towards selective PAR1 agonists—thrombin and TFLLR-NH2. Surprisingly, hPAR1C387AC388A failed to generate a calcium signal to either PAR1 agonists. The reduced cell surface expression of hPAR1C387A388A was not responsible for the lack of calcium signal since a wt-hPAR1 cell line with similar cell surface expression to hPAR1C387AC388A displayed robust responses to both thrombin and TFLLR-NH2. hPAR1C387AC388A was also unable to trigger ERK1/2 phosphorylation in response to either PAR1 agonists. In agonist triggered internalisation experiments all mutant receptors internalised in response to thrombin and TFLLR, except for wt-hPAR1 which only internalised in response to thrombin. Therefore, we conclude that putative palmitoylation sites within hPAR1 regulate receptor expression, agonist triggered internalisation and are critical for hPAR1 coupling to calcium and ERK1/2.
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Books on the topic "Cysteines"

1

Kirschke, Heidrun. Lysosomal cysteine proteases. 2nd ed. Oxford: Oxford University Press, 1997.

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Turk, Vito, ed. Cysteine Proteinases and their Inhibitors. Berlin, Boston: De Gruyter, 1986. http://dx.doi.org/10.1515/9783110846836.

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Robinson, Mark W., and John P. Dalton, eds. Cysteine Proteases of Pathogenic Organisms. Boston, MA: Springer US, 2011. http://dx.doi.org/10.1007/978-1-4419-8414-2.

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Cysteine proteases of pathogenic organisms. New York: Springer Science+Business Media, 2011.

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Kirschke, Heidrun. Proteinases 1: lysosomal cysteine proteinases. London: Academic Press, 1995.

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Nycander, Maria. Interaction of cystatins with cysteine proteinases. Uppsala: Sveriges Lantbruksuniversitet, 1998.

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Pritchard, Jane Elisabeth. Genetic characterization of cysteine sulphinic acid decarboxylase. Birmingham: University of Birmingham, 1999.

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Barry, Christopher Harper. Characterisation of a recombinant human cysteine dioxygenase. Birmingham: University of Birmingham, 2003.

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Pomroy, Neil Christopher. Solubilization of hydrophobic peptides by reversible cysteine PEGylation. Ottawa: National Library of Canada, 1999.

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Parsons, Richard Bramwell. Cysteine metabolism in the brain, liver and kidney. Birmingham: University of Birmingham, 1998.

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Book chapters on the topic "Cysteines"

1

Cooper, Arthur J. L. "Mechanisms of CysteineS-conjugate β-Lyases." In Advances in Enzymology - and Related Areas of Molecular Biology, 199–238. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470123188.ch6.

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Baudin-Creuza, Véronique, Chien Ho, and Michael C. Marden. "Hb Octamers by Introduction of Surface Cysteines." In Chemistry and Biochemistry of Oxygen Therapeutics, 371–80. Chichester, UK: John Wiley & Sons, Ltd, 2011. http://dx.doi.org/10.1002/9781119975427.ch26.

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Hansen, Simon Boje, and Kasper Røjkjær Andersen. "Introducing Cysteines into Nanobodies for Site-Specific Labeling." In Methods in Molecular Biology, 327–43. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2075-5_16.

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Du, Aiguo, Hui Liu, Hai Deng, and Yi Pan. "Progress in Prediction of Oxidation States of Cysteines via Computational Approaches." In Algorithmic and Artificial Intelligence Methods for Protein Bioinformatics, 217–30. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118567869.ch11.

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Bonetto, Valentina, and Pietro Ghezzi. "Thiol-Disulfide Oxidoreduction of Protein Cysteines: Old Methods Revisited for Proteomics." In Redox Proteomics, 101–22. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/0471973122.ch4.

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van Beeumen, Jozef. "Identification of the Heme-Binding Cysteines in Cytochromes c Without Radioactive Labeling." In Advanced Methods in Protein Microsequence Analysis, 256–64. Berlin, Heidelberg: Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-71534-1_21.

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Massey, V., S. M. Miller, D. P. Ballou, C. H. Williams, M. Moore, M. Distefano, and C. T. Walsh. "The penultimate cysteines in mercuric reductase aid in the reduction of mercury." In Flavins and Flavoproteins 1987, edited by D. E. Edmondson and D. B. McCormick, 41–44. Berlin, Boston: De Gruyter, 1987. http://dx.doi.org/10.1515/9783110884715-008.

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Bishop, Anthony C., and Anna Serbina. "Targeting Nonconserved and Pathogenic Cysteines of Protein Tyrosine Phosphatases with Small Molecules." In Methods in Molecular Biology, 271–83. New York, NY: Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-3569-8_17.

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Dickgiesser, Stephan, Roland Kellner, Harald Kolmar, and Nicolas Rasche. "Site-Specific Conjugation of Thiol-Reactive Cytotoxic Agents to Nonnative Cysteines of Engineered Monoclonal Antibodies." In Methods in Molecular Biology, 1–14. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9654-4_1.

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Mukherjee, Somnath, Maria Matveenko, and Christian F. W. Becker. "Highly Precise Protein Semisynthesis through Ligation–Desulfurization Chemistry in Combination with Phenacyl Protection of Native Cysteines." In Expressed Protein Ligation, 343–58. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0434-2_17.

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Conference papers on the topic "Cysteines"

1

Kosmachevskaya, Olga Vladimirovna, Elvira Ilgizovna Nasybullina, Natalya Nikolaevna Novikova, Konstantin Borisovich Shumaev, and Alexey Fedorovich Topunov. "HEMOGLOBIN THIOLS: BIOLOGICAL SIGNIFICANCE AND REGULATION." In International conference New technologies in medicine, biology, pharmacology and ecology (NT +M&Ec ' 2020). Institute of information technology, 2020. http://dx.doi.org/10.47501/978-5-6044060-0-7.20.

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Human hemoglobin has two reactive cysteines (Cys-93β) located on the surface of the molecule. Inclusion of these thiols in the composition of dinitrosyl iron complexe is one way of regulating their reactivity. The thiols bound into complexes exhibit enhanced reactivity with electrophiles and are protected from oxidation by tert-butyl hydroperoxide.
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Roussel, Christophe, Loic Dayon, Tatiana C. Rohner, Niels Lion, and Hubert Girault. "On-line electrochemical tagging of free cysteines during nanospray ionisation for mass spectrometry analysis." In Photonics Europe, edited by Michel D. Faupel and Patrick Meyrueis. SPIE, 2004. http://dx.doi.org/10.1117/12.554259.

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Beeler, D., L. Fritze, G. Soff, R. Jackman, and R. Rosenberg. "HUMAN THROMBOMODULIN cDNA:SEQUENCE AND TRANSLATED STRUCTURE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643967.

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A 750 bp bovine Thrombomodulin (TM) cDNA fragment was used as an hybridization probe to screen an oligo-dT primed Lambda gtll. cDNA library prepared from human umbilical vein endothelial cell mRNA. A 2.4 kb positive human clone was isolated which showed an 80% nucleotide sequence homology with bovine TM cDNA. This clone and a 550 bp fragment from its 5' end were used to further screen the oligo-dT primed library as well as randomly primed library prepared from the same mRNA. The cDNA clones obtained allow us to describe the overall structure of human TM and reveal that it is extremely similar to the structure of bovine TM, especially as the bovine TM is organized like the receptor for low density lipoprotein (LDL R). Both TM and LDL R exhibit short cytoplasmic C-terminal tails which are either neutral or negatively charged. Other coated pit receptors such as the insulin receptor or the epidermal growth factor (EGF) receptor have very large cytoplasmic regions with a complex tyrosine kinase segment as well as multiple sites for phosphorylation. Both TM and LDL R possess a transmembrane region and an immediately adjacent extracellular serine/threonine rich region which in LDL R has been shown to bear 0-1inked sugars. Both TM and LDL R contain a more distal area of cysteine rich repeats, first noted in the EGF precursor and termed EGF type B. However, the TM EGF type B repeats appear to have been duplicated in TM resulting in their being 6 of them rather than the 3 found in LDL R. The N-terminal half of LDL R is thought to contain the ligand binding region of the receptor and is constructed from multiple cysteine rich repeats similar to those of Complement factor C9. The structure of this region of TM is quite different from that of LDL R, possessing few cysteines. We suspect that protein C and/or thrombin may bind to this unique domain of TM.
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Peyronel, Fernanda, David Pink, Gurpreet Matharoo, Iris Joye, Shajahan Razul, and Wei Cao. "Spontaneous aggregation of glutathione in aqueous solutions and the use of Ellman's procedure to detect thiol moieties." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/cyco6389.

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Ellman's procedure for detecting thiol moieties has been used to quantify the formation of disulfide bonds. The philosophy here is that DTNB used by Ellman will detect the development of oxidation as a function of time as per temporal decrease of the SH moieties. Recently (Lauwers et al 2016, Cao et al 2021) this technique was used to quantify the oxidation of cysteine and glutathione as function of time. It was reported that, at pH = 6.5, for all cases of cysteine and one case of glutathione studied, the number of thiols became zero in a finite time, tc. Using Smoluchowski equations (a) we pointed out that in milliQ water with cysteine molecules searching randomly to form disulfide bonds, we should find that tc → ∞, and (b) we proposed that cysteine molecules, carrying zero net charge at pH = 6.5, aggregated so that SH groups were ‘hidden’ in the interior thus preventing the detection of thiols by DTNB thus erroneously reporting the number of thiols to be zero after a finite time. This is analogous to the necessity to disrupt the structure of a protein before using Ellman's procedure. We have used atomic scale molecular dynamics to simulate both cysteine and glutathione in milliQ water. The results showed that, instead of being randomly distributed, cysteine does indeed form aggregates as the Smoluchowski equations indicated. We shall present results for glutathione to (i) establish whether this molecule, which is charged at pH = 6.5, forms aggregates, (ii) if aggregates are formed, whether DTNB will be unable to access thiols hidden inside them.
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Chepikova, O. E., A. I. Petushkova, I. V. Rodionov, N. V. Gorokhovets, A. A. Zamyatnin Jr, and L. V. Savvateeva. "KINETIC PARAMETERS DETERMINATION OF THE INTERACTIONS BETWEEN CYSTEINE CATHEPSINS AND PEPTIDE INHIBITORS." In X Международная конференция молодых ученых: биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-391.

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Excess of cysteine cathepsins activity in tumor microenvironment is caused by violation of their regulation mechanisms. Proteolytic enzymes can hydrolyze endogenous cathepsin inhibitors cystatins. In this study, the interactions between exogenous covalent or non-covalent peptide inhibitors with antitumor activity and recombinant human cysteine cathepsins S and L were studied.
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Longinos, Sotirios, Dionisia Dimitra Longinou, Mirlan Tuleugaliyev, and Mahmut Parlaktuna. "Examination of Cysteine, Glutamine and Isoleucine as Methane-Propane Gas Hydrate Kinetic Inhibitors." In SPE Annual Caspian Technical Conference. SPE, 2022. http://dx.doi.org/10.2118/212055-ms.

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Abstract Gas hydrates are recognized as a significant concern to the oil and gas flow assurance, as it generates pipelines blockages. In this research three alterative amino acids such as: glutamine, cysteine and isoleucine investigated if they work as kinetic inhibitors on methane-propane gas hydrate creation. The outcomes indicated that cysteine worked as inhibitor while isoleucine and glutamine worked as promoters (glutamine>isoleucine) for both hydrate formation and induction time. Experiments with glutamine and isoleucine have the highest value of hydrate productivity while the lowest value of hydrate productivity belongs to experiments with cysteine. From hydrodynamic behavior, radial flow experiments indicated better gas liquid contact compared to mixed flow experiments.
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Hassan, H. J., L. Cianetti, P. M. Mannucci, V. Vicente, R. Cortese, and C. Peschle. "HEREDITARY THROMBOPHILIA CAUSED BY MISSENSE MUTATION IN PROTEIN C GENE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642944.

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The structure of the gene for protein C was analyzed in 13 protein C deficient unrelated patients (11 heterozygous, 2 homozygous), who showed an equivalent reduction of this serine protease at both enzymatic and antigen level. No deletion(s) or rearrangement(s) was demonstrated by Southern blot after hybridization to a cDNA probe. One patient showed a variant restriction pattern after Bam HI digestion, characterized by an abnormal 9.6 kb band in addition to the 8.3 and 1.3 normal ones. Extensive family studies, including 7 heterozygotes with the same clinical phenotype, showed the same abnormal pattern in all and only these heterozygotes. Protein C gene from the propositus was cloned in EMBL3 lambda vector. A 411 bp PstI - SacI fragment from exon 9 encompassing the mutation in the Bam HI site was subcloned in M13mpl8. Its sequence showed a single transversion in the Bam HI palyndrome (GGATCC -> GCATCC) : this causes a substitution of the 402 thryptophan residue with a cystein. The 402 thryptophan residue is constantly conserved in a biochemical domain present in all eukaryotic serine proteases: substitution of the large thryptophan aromatic ring with the small cysteine hydrophilic side-chain conceivably leads to destabilization of the tertiary structure of protein C in these heterozygotes. Thus, the point mutation reported here is sufficient to explain the protein C deficiency in these subjects, and is apparently responsible for their clinical phenotype.
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Kino, Katsuhito, Masayuki Morikawa, Takeshi Senda, Masayo Suzuki, Takanobu Kobayashi, and Hiroshi Miyazawa. "Formation of a flavin-linked cysteine." In The 17th International Electronic Conference on Synthetic Organic Chemistry. Basel, Switzerland: MDPI, 2013. http://dx.doi.org/10.3390/ecsoc-17-b002.

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Maya, K., Lalita Rane, Tousief Irshad Ahmed, Mohammad Javed Ansari, Chandra Kumar Dixit, and Rahul Kanaoujiya. "L-Cysteine Passivated Carbon Quantum Dots as Biosensor for early Stage Detection of Prostate Cancer." In International Conference on Recent Advancements in Biomedical Engineering. Switzerland: Trans Tech Publications Ltd, 2022. http://dx.doi.org/10.4028/p-x65kwp.

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Green synthesized surface passivated carbon dots for detection of Citrate as biomarker for prostate cancer. The carbon sources of CQDs are passivated with L-cysteine via a one-pot hydrothermal route. The quenching in emission intensity of the synthesized carbon dots (CQDs) is observed for Citrate samples. The hydroxyl and carboxylic functional groups of Citrate showed a binding affinity with amino and free carboxyl cysteine passivated over the surface of carbon dots. The CQDs showed a high sensitivity for detection of Citrate in a continuous range of 1.0 μM–500 μM. The CQDs showed good level of selectivity, repeatability, and stability for the detection of Citrate. We successfully detected the Citrate content for prostate cancer cells using an L-cysteine passivated carbon quantum dots various incubation durations. As a result, quenching in fluorescence intensity CQDs are noted to analyze extent of cancer cells in biological samples.
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Zhao, Lingzhi, Liu Zhao, Yanqing Miao, and Chunye Liu. "Colorimetric Sensing of Cysteine in serum by the competitive adsorption toward AuNPs between Cysteine and ATP." In 3rd International Conference on Material, Mechanical and Manufacturing Engineering (IC3ME 2015). Paris, France: Atlantis Press, 2015. http://dx.doi.org/10.2991/ic3me-15.2015.27.

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Reports on the topic "Cysteines"

1

Dill, Kilian, Richard J. O'Connor, and Evelyn L. McGown. Reaction of Cysteine(s) with Phenyldichloroarsine. Fort Belvoir, VA: Defense Technical Information Center, January 1990. http://dx.doi.org/10.21236/ada223117.

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Kim, Chongwoo A. Potential Cysteine Redox Regulation of the Polycomb Group. Fort Belvoir, VA: Defense Technical Information Center, August 2005. http://dx.doi.org/10.21236/ada521853.

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Spek, J. W. Standardized ileal digestible methionine and cysteine requirement for broilers. Wageningen: Wageningen Livestock Research, 2018. http://dx.doi.org/10.18174/455513.

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Spek, J. W. Standardized ileal digestible methionine and cysteine requirement for laying hens. Wageningen: Wageningen Livestock Research, 2018. http://dx.doi.org/10.18174/455520.

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Sanders, Tanya C. A New Class of Serine and Cysteine Protease Inhibitor with Chemotherapeutic Potential. Fort Belvoir, VA: Defense Technical Information Center, June 1999. http://dx.doi.org/10.21236/ada370850.

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Sanders, Tanya C. A New Class of Serine and Cysteine Protease Inhibitor with Chemotherapeutic Potential. Fort Belvoir, VA: Defense Technical Information Center, July 1998. http://dx.doi.org/10.21236/ada353868.

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Muza, S. R., D. Kaminsky, C. S. Fulco, L. E. Banderet, and A. Cymerman. Cysteinyl Leukotriene Blockade Does Not Prevent Acute Mountain Sickness. Fort Belvoir, VA: Defense Technical Information Center, May 2004. http://dx.doi.org/10.21236/ada423394.

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Anders, M. W. Biosynthesis, Physiological Disposition, and Biochemical Effects of Nephrotoxic Glutathione and Cysteine S-Conjugates. Fort Belvoir, VA: Defense Technical Information Center, April 1990. http://dx.doi.org/10.21236/ada221522.

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Chung, Fang-Yu, and Yu-Fon Chen. Chemical modified natural nanogels crosslinked with S Benzyl L cysteine exhibit potent antibacterial activity. Peeref, March 2023. http://dx.doi.org/10.54985/peeref.2303p2513551.

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Peters, R. W., J. M. Wu, N. Meshkov, M. C. Thurnauer, and A. G. Ostafin. Use of cysteine-modified TiO{sub 2} photocatalyst for treatment of combined organic/inorganic wastewaters. Office of Scientific and Technical Information (OSTI), March 1995. http://dx.doi.org/10.2172/28267.

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