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Journal articles on the topic 'Protein S'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Sorice, M., T. Griggi, A. Circella, et al. "Protein S antibodies in acquired protein S deficiencies [letter]." Blood 83, no. 8 (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, et al. "Protein S antibodies in acquired protein S deficiencies [letter]." Blood 83, no. 8 (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, et al. "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 deficienc

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4

Kwaan, Hau. "Protein C and Protein S." Seminars in Thrombosis and Hemostasis 15, no. 03 (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 (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 (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 (1992): 8140–45. http://dx.doi.org/10.1016/s0021-9258(18)42418-0.

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8

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 dec

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9

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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10

Zhang, Mingzi M., and Howard C. Hang. "Protein S-palmitoylation in cellular differentiation." Biochemical Society Transactions 45, no. 1 (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 t

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11

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

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12

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

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13

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

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14

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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15

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

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16

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 (2005): 778–85. http://dx.doi.org/10.1309/bg1gr3anar9905f4.

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17

Chamberlain, Luke H., and Michael J. Shipston. "The Physiology of Protein S-acylation." Physiological Reviews 95, no. 2 (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

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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 (1989): 999–1042. http://dx.doi.org/10.1016/s0950-3536(89)80055-1.

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19

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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20

Zhang, Jing, Yongxiang Wang, Shuwen Fu, et al. "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 (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 transfecte

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21

Breitwieser, Andreas, Philipp Siedlaczek, Helga Lichtenegger, Uwe B. Sleytr, and Dietmar Pum. "S-Layer Protein Coated Carbon Nanotubes." Coatings 9, no. 8 (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 or

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22

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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23

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 (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 antige

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24

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 (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 sho

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25

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

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26

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 (1987): 109–14. http://dx.doi.org/10.1016/0049-3848(87)90262-3.

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27

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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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 (2007): pdb.top11. http://dx.doi.org/10.1101/pdb.top11.

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29

Kordyukova, Larisa V., Marina V. Serebryakova, Vladislav V. Khrustalev, and Michael Veit. "Differential S-acylation of Enveloped Viruses." Protein & Peptide Letters 26, no. 8 (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

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30

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 (1996): 13386–92. http://dx.doi.org/10.1021/bi960856+.

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31

Zhang, Yan, Elise R. Lyver, Eiko Nakamaru-Ogiso, et al. "Dre2, a Conserved Eukaryotic Fe/S Cluster Protein, Functions in Cytosolic Fe/S Protein Biogenesis." Molecular and Cellular Biology 28, no. 18 (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

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32

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 indivi

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33

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 (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 contribut

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34

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 (1985): 199–201. http://dx.doi.org/10.1007/bf00269288.

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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 (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 (1987): 25–36. http://dx.doi.org/10.1016/0009-8981(87)90380-9.

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37

Hopmeier, P. "Mangelzustände an Antithrombin III, Protein C und Protein S." Hämostaseologie 13, no. 04 (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

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38

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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39

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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40

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

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41

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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42

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

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43

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 (1992): 484???489. http://dx.doi.org/10.1097/00126334-199205000-00009.

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44

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 (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 exp

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45

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 (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

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46

Nguyen-Mau, Sao-Mai, So-Young Oh, Daphne I. Schneewind, Dominique Missiakas, and Olaf Schneewind. "Bacillus anthracis SlaQ Promotes S-Layer Protein Assembly." Journal of Bacteriology 197, no. 19 (2015): 3216–27. http://dx.doi.org/10.1128/jb.00492-15.

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ABSTRACTBacillus anthracisvegetative forms assemble an S-layer comprised of two S-layer proteins, Sap and EA1. A hallmark of S-layer proteins are their C-terminal crystallization domains, which assemble into a crystalline lattice once these polypeptides are deposited on the bacterial surface via association between their N-terminal S-layer homology domains and the secondary cell wall polysaccharide. Here we show thatslaQ, encoding a small cytoplasmic protein conserved among pathogenic bacilli elaborating S-layers, is required for the efficient secretion and assembly of Sap and EA1. S-layer pro

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47

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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48

Malm, J., X. H. He, A. Bjartell, L. Shen, P. A. Abrahamsson, and B. Dahlbäck. "Vitamin K-dependent protein S in Leydig cells of human testis." Biochemical Journal 302, no. 3 (1994): 845–50. http://dx.doi.org/10.1042/bj3020845.

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Protein S is an anticoagulant plasma protein, functioning as a cofactor to activated protein C in the regulation of blood coagulation. In addition, protein S forms a complex with the complement regulatory protein, C4b-binding protein. Protein S is unique among the vitamin K-dependent proteins in being structurally similar to androgen binding proteins. Protein S immunoreactivity was demonstrated in Leydig cells of human testis. In Northern blotting experiments, the presence of protein S mRNA in human testis tissue could be shown. In situ hybridization experiments localized protein S mRNA to the

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49

Chang, Glenn T. G., Bart H. A. Maas, Hans K. Ploos van Amstel, Pieter H. Reitsma, Rogier M. Bertina, and Bonno N. Bouma. "Studies of the Interaction between Human Protein S and Human C4b-Binding Protein Using Deletion Variants of Recombinant Human Protein S." Thrombosis and Haemostasis 71, no. 04 (1994): 461–67. http://dx.doi.org/10.1055/s-0038-1642461.

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SummaryHuman protein S interacts noncovalently with human C4b-binding protein (C4BP). We have studied this interaction using deletion variants of recombinant human protein S. Two deletion variants were constructed by restriction enzyme digestion and in vitro site-specific mutagenesis of the human protein S cDNA. The variants were stably expressed in Cl27 cells. Recombinant proteins were purified using Fast Flow Q anion-exchange chromatography. The activated protein C (APC) cofactor activity, C4BP binding properties and reactivity to different monoclonal antibodies against human protein S were

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50

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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