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Journal articles on the topic 'Protein S'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 March 2023

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1

Sorice, M., T. Griggi, A. Circella, L. Lenti, P. Arcieri, G. Domenico di Nucci, and G. Mariani. "Protein S antibodies in acquired protein S deficiencies [letter]." Blood 83, no. 8 (April 15, 1994): 2383–84. http://dx.doi.org/10.1182/blood.v83.8.2383b.2383b.

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2

Sorice, M., T. Griggi, A. Circella, L. Lenti, P. Arcieri, G. Domenico di Nucci, and G. Mariani. "Protein S antibodies in acquired protein S deficiencies [letter]." Blood 83, no. 8 (April 15, 1994): 2383–84. http://dx.doi.org/10.1182/blood.v83.8.2383b.bloodjournal8382383b.

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3

Sacchi, E., M. Pinotti, G. Marchetti, G. Merati, L. Tagliabue, P. M. Mannucci, and F. Bernardi. "Protein S mRNA in Patients with Protein S Deficiency." Thrombosis and Haemostasis 73, no. 05 (1995): 746–49. http://dx.doi.org/10.1055/s-0038-1653862.

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SummaryA protein S gene polymorphism, detectable by restriction analysis (BstXI) of amplified exonic sequences (exon 15), was studied in seven Italian families with protein S deficiency. In the 17 individuals heterozygous for the polymorphism the study was extended to platelet mRNA through reverse transcription, amplification and densitometric analysis. mRNA produced by the putative defective protein S genes was absent in three families and reduced to a different extent (as expressed by altered allelic ratios) in four families. The allelic ratios helped to distinguish total protein S deficiency (type I) from free protein S deficiency (type IIa) in families with equivocal phenotypes. This study indicates that the study of platelet mRNA, in association with phenotypic analysis based upon protein S assays in plasma, helps to classify patients with protein S deficiency.

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4

Kwaan, Hau. "Protein C and Protein S." Seminars in Thrombosis and Hemostasis 15, no. 03 (July 1989): 353–55. http://dx.doi.org/10.1055/s-2007-1002728.

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5

Esmon, Charles T. "Protein S and protein C." Trends in Cardiovascular Medicine 2, no. 6 (November 1992): 214–19. http://dx.doi.org/10.1016/1050-1738(92)90027-p.

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6

Rick, Margaret E. "Protein C and Protein S." JAMA 263, no. 5 (February 2, 1990): 701. http://dx.doi.org/10.1001/jama.1990.03440050095041.

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7

Nelson, R. M., and G. L. Long. "Binding of protein S to C4b-binding protein. Mutagenesis of protein S." Journal of Biological Chemistry 267, no. 12 (April 1992): 8140–45. http://dx.doi.org/10.1016/s0021-9258(18)42418-0.

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8

NAKAYAMA, Takayuki, and Tetsuhito KOJIMA. "Protein S Deficiency." Japanese Journal of Thrombosis and Hemostasis 12, no. 3 (2001): 235–39. http://dx.doi.org/10.2491/jjsth.12.235.

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9

Ratnaparkhi, Girish S., Satish Kumar Awasthi, P. Rani, P. Balaram, and R. Varadarajan. "Structural and thermodynamic consequences of introducing α-aminoisobutyric acid in the S peptide of ribonuclease S." Protein Engineering, Design and Selection 13, no. 10 (October 2000): 697–702. http://dx.doi.org/10.1093/protein/13.10.697.

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10

D'Angelo, A., and S. Vigano D'Angelo. "Protein S deficiency." Haematologica 93, no. 4 (April 1, 2008): 498–501. http://dx.doi.org/10.3324/haematol.12691.

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11

Borgel, Delphine, Sophie Gandrille, and Martine Aiach. "Protein S Deficiency." Thrombosis and Haemostasis 78, no. 01 (1997): 351–56. http://dx.doi.org/10.1055/s-0038-1657551.

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12

Meissner, W., H. Fritz, Th Deufel, B. Dohrn, A. Meier-Hellmann, and K. Reinhart. "S-100 PROTEIN." Critical Care Medicine 26, Supplement (January 1998): 83A. http://dx.doi.org/10.1097/00003246-199801001-00213.

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13

Van Cott, Elizabeth M., Marlies Ledford-Kraemer, Piet Meijer, William L. Nichols, Stephen M. Johnson, and Ellinor I. B. Peerschke. "Protein S Assays." American Journal of Clinical Pathology 123, no. 5 (May 2005): 778–85. http://dx.doi.org/10.1309/bg1gr3anar9905f4.

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14

Ruoppolo, Margherita, and Robert B. Freedman. "Protein-S-S-Glutathione Mixed Disulfides as Models of Unfolded Proteins." Biochemistry 33, no. 24 (June 21, 1994): 7654–62. http://dx.doi.org/10.1021/bi00190a020.

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15

Bertina, R. M., A. van Wijngaarden, J. Reinalda-Poot, S. R. Poort, and V. J. J. Bom. "Determination of Plasma Protein S - The Protein Cofactor of Activated Protein C." Thrombosis and Haemostasis 53, no. 02 (1985): 268–72. http://dx.doi.org/10.1055/s-0038-1661291.

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SummaryProtein S, an important cofactor of activated protein C, and C4b-binding protein were purified from human plasma. Specific antibodies against the purified proteins were raised in rabbits and used for the development of immunologic assays for these proteins in plasma: an immunoradiometric assay for protein S (which measures both free protein S and protein S complexed with C4b-binding protein) and an electroimmunoassay for C4b- binding protein. Ranges for the concentrations of these proteins were established in healthy volunteers and patients using oral anticoagulant therapy. A slight decrease in protein S antigen was observed in patients with liver disease (0.78 ± 0.25 U/ml); no significant decrease in protein S was observed in patients with DIC (0.95 ± 0.25 U/ml).Criteria were developed for the laboratory diagnosis of an isolated protein S deficiency

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16

MIYATA, Toshiyuki, Jun MIZUGUCHI, Atsuo SUZUKI, and Tetsuhito KOJIMA. "Basics of protein C and protein S." Japanese Journal of Thrombosis and Hemostasis 25, no. 1 (2014): 40–47. http://dx.doi.org/10.2491/jjsth.25.40.

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17

Zhang, Mingzi M., and Howard C. Hang. "Protein S-palmitoylation in cellular differentiation." Biochemical Society Transactions 45, no. 1 (February 8, 2017): 275–85. http://dx.doi.org/10.1042/bst20160236.

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Reversible protein S-palmitoylation confers spatiotemporal control of protein function by modulating protein stability, trafficking and activity, as well as protein–protein and membrane–protein associations. Enabled by technological advances, global studies revealed S-palmitoylation to be an important and pervasive posttranslational modification in eukaryotes with the potential to coordinate diverse biological processes as cells transition from one state to another. Here, we review the strategies and tools to analyze in vivo protein palmitoylation and interrogate the functions of the enzymes that put on and take off palmitate from proteins. We also highlight palmitoyl proteins and palmitoylation-related enzymes that are associated with cellular differentiation and/or tissue development in yeasts, protozoa, mammals, plants and other model eukaryotes.

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18

Dolan, G., J. Ball, and F. E. Preston. "10 Protein C and protein S." Baillière's Clinical Haematology 2, no. 4 (October 1989): 999–1042. http://dx.doi.org/10.1016/s0950-3536(89)80055-1.

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19

Chamberlain, Luke H., and Michael J. Shipston. "The Physiology of Protein S-acylation." Physiological Reviews 95, no. 2 (April 2015): 341–76. http://dx.doi.org/10.1152/physrev.00032.2014.

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Protein S-acylation, the only fully reversible posttranslational lipid modification of proteins, is emerging as a ubiquitous mechanism to control the properties and function of a diverse array of proteins and consequently physiological processes. S-acylation results from the enzymatic addition of long-chain lipids, most typically palmitate, onto intracellular cysteine residues of soluble and transmembrane proteins via a labile thioester linkage. Addition of lipid results in increases in protein hydrophobicity that can impact on protein structure, assembly, maturation, trafficking, and function. The recent explosion in global S-acylation (palmitoyl) proteomic profiling as a result of improved biochemical tools to assay S-acylation, in conjunction with the recent identification of enzymes that control protein S-acylation and de-acylation, has opened a new vista into the physiological function of S-acylation. This review introduces key features of S-acylation and tools to interrogate this process, and highlights the eclectic array of proteins regulated including membrane receptors, ion channels and transporters, enzymes and kinases, signaling adapters and chaperones, cell adhesion, and structural proteins. We highlight recent findings correlating disruption of S-acylation to pathophysiology and disease and discuss some of the major challenges and opportunities in this rapidly expanding field.

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20

Huoponen, Outi, Jukka Partanen, Vesa Rasi, Tom Krusius, and Tuuli Heinikari. "Protein S gene polymorphisms Pro626 and nt2698 – no correlation to free protein S levels or protein S activities." Thrombosis and Haemostasis 94, no. 12 (2005): 1340–41. http://dx.doi.org/10.1160/th05-06-1340.

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21

Hillarp, Andreas, Björn Dahlbäck, and Kristina Persson. "Analytical Considerations for Free Protein S Assays in Protein S Deficiency." Thrombosis and Haemostasis 86, no. 11 (2001): 1144–47. http://dx.doi.org/10.1055/s-0037-1616042.

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SummaryProtein S is an anticoagulant protein that circulates in plasma in complex with C4b-binding protein (C4BP) or in free form. Deficiency of protein S increases the risk of venous thrombosis. Measurement of free protein S, as compared to total levels, has been shown to be superior for prediction of protein S deficiency. We studied the effects of different handling protocols for an immuno- and a ligand (C4BP)-based assay for free protein S. When the assay was performed at 37° C, the levels of free protein S in plasma from protein S deficient patients were approximately twice those obtained at room temperature. The reason for this phenomenon was that plasmas from protein S deficient patients exhibited a time-, temperature-, and dilution-dependent increase in free protein S, which was more pronounced than corresponding dilution of the normal plasma that was used to create the standard curve. These findings demonstrate the importance of assay procedure and sample handling in assays for free protein S.

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22

Huisveld, I. A., J. E. H. Hospers, J. C. M. Meijers, A. E. Starkenburg, W. B. M. Erich, and B. N. Bouma. "Oral contraceptives reduce total protein S, but not free protein S." Thrombosis Research 45, no. 1 (January 1987): 109–14. http://dx.doi.org/10.1016/0049-3848(87)90262-3.

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23

Rodger, Marc A., Marc Carrier, Muriel Gervais, and Gail Rock. "Normal Functional Protein S Activity Does Not Exclude Protein S Deficiency." Pathophysiology of Haemostasis and Thrombosis 33, no. 4 (2003): 202–5. http://dx.doi.org/10.1159/000081509.

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24

Breitwieser, Andreas, Philipp Siedlaczek, Helga Lichtenegger, Uwe B. Sleytr, and Dietmar Pum. "S-Layer Protein Coated Carbon Nanotubes." Coatings 9, no. 8 (August 2, 2019): 492. http://dx.doi.org/10.3390/coatings9080492.

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Carbon nanotubes (CNTs) have already been considered for medical applications due to their small diameter and ability to penetrate cells and tissues. However, since CNTs are chemically inert and non-dispersible in water, they have to be chemically functionalized or coated with biomolecules to carry payloads or interact with the environment. Proteins, although often only randomly bound to the CNT surface, are preferred because they provide a better biocompatibility and present functional groups for binding additional molecules. A new approach to functionalize CNTs with a closed and precisely ordered protein layer is offered by bacterial surface layer (S-layer) proteins, which have already attracted much attention in the functionalization of surfaces. We could demonstrate that bacterial S-layer proteins (SbpA of Lysinibacillus sphaericus CCM 2177 and the recombinant fusion protein rSbpA31-1068GG comprising the S-layer protein and two copies of the IgG binding region of Protein G) can be used to disperse and functionalize oxidized multi walled CNTs. Following a simple protocol, a complete surface coverage with a long-range crystalline S-layer lattice can be obtained. When rSbpA31-1068GG was used for coating, the introduced functionality could be confirmed by binding gold labeled antibodies via the IgG binding domain of the fusion protein. Since a great variety of functional S-layer fusion proteins has already been described, our new technology has the potential for a broad spectrum of functionalized CNTs.

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25

Graziano, Giuseppe, Francesca Catanzano, Concetta Giancola, and Guido Barone. "DSC Study of the Thermal Stability of S-Protein and S-Peptide/S-Protein Complexes†." Biochemistry 35, no. 41 (January 1996): 13386–92. http://dx.doi.org/10.1021/bi960856+.

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26

Schwarz, HP, W. Muntean, H. Watzke, B. Richter, and JH Griffin. "Low total protein S antigen but high protein S activity due to decreased C4b-binding protein in neonates." Blood 71, no. 3 (March 1, 1988): 562–65. http://dx.doi.org/10.1182/blood.v71.3.562.562.

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Abstract Protein S, a vitamin K-dependent cofactor for activated protein C, exists in normal adult plasma in a free anticoagulantly active form and in an inactive form complexed to C4b-binding protein. Immunologic and functional levels of protein S and C4b-binding protein in plasma were determined for 20 newborn infants and compared with adult normal pooled plasma. Total protein S antigen levels averaged 23%, similar to other vitamin K-dependent plasma proteins. However, the protein S anticoagulant activity was 74% of that of adult normal plasma. This apparent discrepancy of activity to antigen was shown to be due to low or undetectable levels of C4b-binding protein, which results in the presence of most if not all of protein S in its free and active form. The relatively high level of anticoagulantly active protein S in infants may enhance the potential of the protein C pathway, thereby minimizing risks of venous thrombosis in this group.

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27

Schwarz, HP, W. Muntean, H. Watzke, B. Richter, and JH Griffin. "Low total protein S antigen but high protein S activity due to decreased C4b-binding protein in neonates." Blood 71, no. 3 (March 1, 1988): 562–65. http://dx.doi.org/10.1182/blood.v71.3.562.bloodjournal713562.

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Protein S, a vitamin K-dependent cofactor for activated protein C, exists in normal adult plasma in a free anticoagulantly active form and in an inactive form complexed to C4b-binding protein. Immunologic and functional levels of protein S and C4b-binding protein in plasma were determined for 20 newborn infants and compared with adult normal pooled plasma. Total protein S antigen levels averaged 23%, similar to other vitamin K-dependent plasma proteins. However, the protein S anticoagulant activity was 74% of that of adult normal plasma. This apparent discrepancy of activity to antigen was shown to be due to low or undetectable levels of C4b-binding protein, which results in the presence of most if not all of protein S in its free and active form. The relatively high level of anticoagulantly active protein S in infants may enhance the potential of the protein C pathway, thereby minimizing risks of venous thrombosis in this group.

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28

Einarson, M. B., E. N. Pugacheva, and J. R. Orlinick. "Identification of Protein-Protein Interactions with Glutathione-S-Transferase (GST) Fusion Proteins." Cold Spring Harbor Protocols 2007, no. 8 (August 1, 2007): pdb.top11. http://dx.doi.org/10.1101/pdb.top11.

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29

KAMIYA, Tadashi. "Protein S and thromboembolism." Blood & Vessel 17, no. 2 (1986): 89–98. http://dx.doi.org/10.2491/jjsth1970.17.89.

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30

NOMURA, MASAKAZU, and HIDEYUKI YAMADA. "Sericin/Protein Powder S." Sen'i Gakkaishi 48, no. 6 (1992): P305—P306. http://dx.doi.org/10.2115/fiber.48.6_p305.

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31

Hafizi, Sassan, and Björn Dahlbäck. "Gas6 and protein S." FEBS Journal 273, no. 23 (October 25, 2006): 5231–44. http://dx.doi.org/10.1111/j.1742-4658.2006.05529.x.

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32

Bertina, R. M. "Hereditary Protein S Deficiency." Pathophysiology of Haemostasis and Thrombosis 15, no. 4 (1985): 241–46. http://dx.doi.org/10.1159/000215155.

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33

Kennedy, C. R. "Acquired protein S deficiency." Archives of Disease in Childhood 69, no. 2 (August 1, 1993): 265. http://dx.doi.org/10.1136/adc.69.2.265.

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34

Bissuel, Fran??ois, Micheline Berruyer, Xavier Causse, Marc Dechavanne, and Christian Trepo. "Acquired Protein S Deficiency." JAIDS Journal of Acquired Immune Deficiency Syndromes 5, no. 5 (May 1992): 484???489. http://dx.doi.org/10.1097/00126334-199205000-00009.

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35

Lush, C. J., L. Armstrong, and V. E. Mitchell. "Free Protein S and C4b Binding Protein." American Journal of Clinical Pathology 96, no. 3 (September 1, 1991): 434–38. http://dx.doi.org/10.1093/ajcp/96.3.434.

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36

Kessler, Craig M., and Dudley K. Strickland. "Protein C and protein S clinical perspectives." Clinica Chimica Acta 170, no. 1 (November 1987): 25–36. http://dx.doi.org/10.1016/0009-8981(87)90380-9.

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37

Teulieres, Chantal, Gilbert Alibert, and Raoul Ranjeva. "Reversible phosphorylation of tonoplast proteins involves tonoplast-bound calcium-calmodulin-dependent protein kinase(s) and protein phosphatase(s)." Plant Cell Reports 4, no. 4 (August 1985): 199–201. http://dx.doi.org/10.1007/bf00269288.

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38

Simmonds, RE, H. Ireland, G. Kunz, and DA Lane. "Identification of 19 protein S gene mutations in patients with phenotypic protein S deficiency and thrombosis. Protein S Study Group." Blood 88, no. 11 (December 1, 1996): 4195–204. http://dx.doi.org/10.1182/blood.v88.11.4195.4195.

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Abstract Protein S is a protein C-dependent and independent inhibitor of the coagulation cascade. Deficiency of protein S is an established risk factor for venous thromboembolism. We have used a strategy of specific amplification of the coding regions and intron/exon boundaries of the active protein S gene (PROS1) and direct single-strand solid phase sequencing, to seek mutations in 35 individuals with phenotypic protein S deficiency. Nineteen point mutations (16 novel) in 19 probands (or relatives of probands) with venous thromboembolism are reported here. Fifteen of the 19 mutations were expected to be causal and included 10 missense mutations (Lys9Glu, Glu26Ala, Gly54Glu, Cys145Tyr, Cys200Ser, Ser283Pro, Gly340Asp, Cys408Ser, Ser460Pro, and Cys625Arg). Three of the 15 mutations resulted in premature stop codons (delete T 635 producing a stop codon at position 126, Lys368stop and Tyr595stop) and two were at intron/exon boundaries (+1 G to A in intron d and +3 A to C in intron j). Of the remaining four mutations, three were within intronic sequence and one was a silent mutation within the coding region and did not alter amino acid composition. In two of the 10 missense mutations, reduced plasma protein S activity compared with antigen level suggested the presence of variant (type II) protein S.

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39

Simmonds, RE, H. Ireland, G. Kunz, and DA Lane. "Identification of 19 protein S gene mutations in patients with phenotypic protein S deficiency and thrombosis. Protein S Study Group." Blood 88, no. 11 (December 1, 1996): 4195–204. http://dx.doi.org/10.1182/blood.v88.11.4195.bloodjournal88114195.

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Protein S is a protein C-dependent and independent inhibitor of the coagulation cascade. Deficiency of protein S is an established risk factor for venous thromboembolism. We have used a strategy of specific amplification of the coding regions and intron/exon boundaries of the active protein S gene (PROS1) and direct single-strand solid phase sequencing, to seek mutations in 35 individuals with phenotypic protein S deficiency. Nineteen point mutations (16 novel) in 19 probands (or relatives of probands) with venous thromboembolism are reported here. Fifteen of the 19 mutations were expected to be causal and included 10 missense mutations (Lys9Glu, Glu26Ala, Gly54Glu, Cys145Tyr, Cys200Ser, Ser283Pro, Gly340Asp, Cys408Ser, Ser460Pro, and Cys625Arg). Three of the 15 mutations resulted in premature stop codons (delete T 635 producing a stop codon at position 126, Lys368stop and Tyr595stop) and two were at intron/exon boundaries (+1 G to A in intron d and +3 A to C in intron j). Of the remaining four mutations, three were within intronic sequence and one was a silent mutation within the coding region and did not alter amino acid composition. In two of the 10 missense mutations, reduced plasma protein S activity compared with antigen level suggested the presence of variant (type II) protein S.

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40

Zhang, Yan, Elise R. Lyver, Eiko Nakamaru-Ogiso, Heeyong Yoon, Boominathan Amutha, Dong-Woo Lee, Erfei Bi, et al. "Dre2, a Conserved Eukaryotic Fe/S Cluster Protein, Functions in Cytosolic Fe/S Protein Biogenesis." Molecular and Cellular Biology 28, no. 18 (July 14, 2008): 5569–82. http://dx.doi.org/10.1128/mcb.00642-08.

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ABSTRACT In a forward genetic screen for interaction with mitochondrial iron carrier proteins in Saccharomyces cerevisiae, a hypomorphic mutation of the essential DRE2 gene was found to confer lethality when combined with Δmrs3 and Δmrs4. The dre2 mutant or Dre2-depleted cells were deficient in cytosolic Fe/S cluster protein activities while maintaining mitochondrial Fe/S clusters. The Dre2 amino acid sequence was evolutionarily conserved, and cysteine motifs (CX2CXC and twin CX2C) in human and yeast proteins were perfectly aligned. The human Dre2 homolog (implicated in blocking apoptosis and called CIAPIN1 or anamorsin) was able to complement the nonviability of a Δdre2 deletion strain. The Dre2 protein with triple hemagglutinin tag was located in the cytoplasm and in the mitochondrial intermembrane space. Yeast Dre2 overexpressed and purified from bacteria was brown and exhibited signature absorption and electron paramagnetic resonance spectra, indicating the presence of both [2Fe-2S] and [4Fe-4S] clusters. Thus, Dre2 is an essential conserved Fe/S cluster protein implicated in extramitochondrial Fe/S cluster assembly, similar to other components of the so-called CIA (cytoplasmic Fe/S cluster assembly) pathway although partially localized to the mitochondrial intermembrane space.

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41

Hopmeier, P. "Mangelzustände an Antithrombin III, Protein C und Protein S." Hämostaseologie 13, no. 04 (July 1993): 152–56. http://dx.doi.org/10.1055/s-0038-1655229.

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ZusammenfassungMangelzustände an Antithrombin III, Protein C und Protein S sind vielfach mit einem erhöhten Thromboembolierisiko verbunden. Klinische Manifestationen sind beim Antithrombin-Ill-Mangel vorwiegend tiefe Venenthrombosen, während beim Protein-Cund Protein-S-Mangel auch arterielle Verschlüsse vereinzelt Vorkommen. Die Diagnose dieser Mangelzustände ist durch Routinetests heute einfach und zuverlässig möglich. Hingegen ist ein positiver Befund bei Personen mit unauffälliger Anamnese schwierig zu interpretieren. Besonders beim Protein-C-/Protein-S-System dürften ein oder mehrere noch nicht näher definierte Kofaktoren Bedeutung haben, und auch die Rolle des C4b-binding proteins ist nicht in allen Aspekten geklärt.Ob bei Mangelpatienten die Erfassung des individuellen Thromboembolierisikos mit Hilfe von Aktivierungsmarkern zuverlässig möglich sein wird, ist zur Zeit ungewiß.

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42

Carr, Jr., Marcus E., and Sheryl L. Zekert. "Protein S and C4b-Binding Protein Levels in Patients with Stroke: Implications for Protein S Regulation." Pathophysiology of Haemostasis and Thrombosis 23, no. 3 (1993): 159–67. http://dx.doi.org/10.1159/000216869.

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43

Zhang, Jing, Yongxiang Wang, Shuwen Fu, Quan Yuan, Qianru Wang, Ningshao Xia, Yumei Wen, Jisu Li, and Shuping Tong. "Role of Small Envelope Protein in Sustaining the Intracellular and Extracellular Levels of Hepatitis B Virus Large and Middle Envelope Proteins." Viruses 13, no. 4 (April 2, 2021): 613. http://dx.doi.org/10.3390/v13040613.

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Hepatitis B virus (HBV) expresses co-terminal large (L), middle (M), and small (S) envelope proteins. S protein drives virion and subviral particle secretion, whereas L protein inhibits subviral particle secretion but coordinates virion morphogenesis. We previously found that preventing S protein expression from a subgenomic construct eliminated M protein. The present study further examined impact of S protein on L and M proteins. Mutations were introduced to subgenomic construct of genotype A or 1.1 mer replication construct of genotype A or D, and viral proteins were analyzed from transfected Huh7 cells. Mutating S gene ATG to prevent expression of full-length S protein eliminated M protein, reduced intracellular level of L protein despite its blocked secretion, and generated a truncated S protein through translation initiation from a downstream ATG. Truncated S protein was secretion deficient and could inhibit secretion of L, M, S proteins from wild-type constructs. Providing full-length S protein in trans rescued L protein secretion and increased its intracellular level from mutants of lost S gene ATG. Lost core protein expression reduced all the three envelope proteins. In conclusion, full-length S protein could sustain intracellular and extracellular L and M proteins, while truncated S protein could block subviral particle secretion.

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44

James, D. Andrew, Darcy C. Burns, and G. Andrew Woolley. "Kinetic characterization of ribonuclease S mutants containing photoisomerizable phenylazophenylalanine residues." Protein Engineering, Design and Selection 14, no. 12 (December 2001): 983–91. http://dx.doi.org/10.1093/protein/14.12.983.

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45

Castaman, G., E. Biguzzi, C. Razzari, A. Tosetto, G. Fontana, D. Asti, V. Brancaccio, D. Castori, D. A. Lane, and E. M. Faioni. "Association of protein S p.Pro667Pro dimorphism with plasma protein S levels in normal individuals and patients with inherited protein S deficiency." Thrombosis Research 120, no. 3 (January 2007): 421–26. http://dx.doi.org/10.1016/j.thromres.2006.10.014.

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46

Brugge, Jeroen, Guido Tans, Jan Rosing, and Elisabetta Castoldi. "Protein S levels modulate the activated protein C resistance phenotype induced by elevated prothrombin levels." Thrombosis and Haemostasis 95, no. 02 (2006): 236–42. http://dx.doi.org/10.1160/th05-08-0582.

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SummaryElevated plasma prothrombin levels, due to the prothrombin 20210 G/A mutation or to acquired causes, area risk factor for venous thrombosis,partly because of prothrombin-mediated inhibition of the protein C anticoagulant pathway and consequent activated proteinC (APC) resistance. We determined the effect of plasma prothrombin concentration on the APC resistance phenotype and evaluated the role of protein S levels asa modulating variable. The effect of prothrombin and protein S levels on APC resistance was investigated in reconstituted plasma systems and in a population of healthy individuals using both the aPTT-based and the thrombin generation-based APC resistance tests. In reconstituted plasma, APC resistance increased at increasing prothrombin concentration in both assays. Enhanced APC resistance was caused by the effect of prothrombin on the clotting time in the absence of APC in the aPTT-based test, and on thrombin formation in the presence of APC in the thrombin generation-based test. In plasma from healthy individuals prothrombin levels were highly correlated to protein S levels. Since prothrombin and proteinS had opposite effects on the APC resistance phenotype, the prothrombin/protein S ratio was a better predictor of APC resistance than the levels of either protein alone. Prothrombin titrations in plasmas containing different amounts of proteinS confirmed that proteinS levels modulate the ability of prothrombin to induce APC resistance. These findings suggest that carriers of the prothrombin 20210 G/A mutation, who have a high prothrombin/protein S ratio, may experience a higher thrombosis risk than non-carriers with comparable prothrombin levels.

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Smith, Donald B., Lloyd C. Berger, and Alan G. Wildeman. "Modified glutathione S-transferase fusion proteins for simplified analysis of protein - protein interactions." Nucleic Acids Research 21, no. 2 (1993): 359–60. http://dx.doi.org/10.1093/nar/21.2.359.

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Kordyukova, Larisa V., Marina V. Serebryakova, Vladislav V. Khrustalev, and Michael Veit. "Differential S-acylation of Enveloped Viruses." Protein & Peptide Letters 26, no. 8 (September 11, 2019): 588–600. http://dx.doi.org/10.2174/0929866526666190603082521.

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Post-translational modifications often regulate protein functioning. Covalent attachment of long chain fatty acids to cysteine residues via a thioester linkage (known as protein palmitoylation or S-acylation) affects protein trafficking, protein-protein and protein-membrane interactions. This post-translational modification is coupled to membrane fusion or virus assembly and may affect viral replication in vitro and thus also virus pathogenesis in vivo. In this review we outline modern methods to study S-acylation of viral proteins and to characterize palmitoylproteomes of virus infected cells. The palmitoylation site predictor CSS-palm is critically tested against the Class I enveloped virus proteins. We further focus on identifying the S-acylation sites directly within acyl-peptides and the specific fatty acid (e.g, palmitate, stearate) bound to them using MALDI-TOF MS-based approaches. The fatty acid heterogeneity/ selectivity issue attracts now more attention since the recently published 3D-structures of two DHHC-acyl-transferases gave a hint how this might be achieved.

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Ju, Yun-Jin, Hye-Won Lee, Ji-Woong Choi, and Min-Sik Choi. "The Role of Protein S-Nitrosylation in Protein Misfolding-Associated Diseases." Life 11, no. 7 (July 17, 2021): 705. http://dx.doi.org/10.3390/life11070705.

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Abnormal and excessive nitrosative stress contributes to neurodegenerative disease associated with the production of pathological levels of misfolded proteins. The accumulated findings strongly suggest that excessive NO production can induce and deepen these pathological processes, particularly by the S-nitrosylation of target proteins. Therefore, the relationship between S-nitrosylated proteins and the accumulation of misfolded proteins was reviewed. We particularly focused on the S-nitrosylation of E3-ubiquitin-protein ligase, parkin, and endoplasmic reticulum chaperone, PDI, which contribute to the accumulation of misfolded proteins. In addition to the target proteins being S-nitrosylated, NOS, which produces NO, and GSNOR, which inhibits S-nitrosylation, were also suggested as potential therapeutic targets for protein misfolding-associated diseases.

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Razzari, Cristina, Rachel Simmonds, and Suely Rezende. "In vitro high level protein S expression after modification of protein S cDNA." Thrombosis and Haemostasis 90, no. 12 (2003): 1214–15. http://dx.doi.org/10.1055/s-0037-1613426.

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