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Journal articles on the topic 'Serpico'

Author: Grafiati

Published: 4 June 2021

Last updated: 28 July 2025

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1

Greenberg, Martin. "Serpico and the Future of the Blue Code of Silence." International Journal of Police Science 1, no. 1 (2022): 40–57. http://dx.doi.org/10.56331/487529/ipsa2.

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This essay reviews several of the moral messages found in the film Serpico (129 ,1973 min.) with emphasis upon understanding the meaning of the phrase “the blue wall of silence” as well as current efforts to limit its occurrences and harmful effects. The essay includes details about the life of Frank Serpico, picking up where the classic Hollywood film left off. Policing in the 1960s and the current nature and the future of policing reforms are considered. Serpico’s present-day opinions about police corruption and violence are also discussed. In addition, the newest private effort to use techn

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2

Serpico, Margaret, and Raymond White. "The botanical identity and transport of incense during the Egyptian New Kingdom." Antiquity 74, no. 286 (2000): 884–97. http://dx.doi.org/10.1017/s0003598x00060531.

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Resin preserved on New Kingdom vessels from Amarna in Middle Egypt provides evidence for incense burning and trade. Here Margaret Serpico & Raymond White describe a new interdisciplinary research project.

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3

Petit, Francis. "What Executives Can Learn From Frank Serpico." Journal of Business Case Studies (JBCS) 7, no. 5 (2011): 29–34. http://dx.doi.org/10.19030/jbcs.v7i5.5602.

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Wu, Qiang, Longsheng Xing, Min Du, et al. "A Genome-Wide Analysis of Serine Protease Inhibitors in Cydia pomonella Provides Insights into Their Evolution and Expression Pattern." International Journal of Molecular Sciences 24, no. 22 (2023): 16349. http://dx.doi.org/10.3390/ijms242216349.

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Serine protease inhibitors (serpins) appear to be ubiquitous in almost all living organisms, with a conserved structure and varying functions. Serpins can modulate immune responses by negatively regulating serine protease activities strictly and precisely. The codling moth, Cydia pomonella (L.), a major invasive pest in China, can cause serious economic losses. However, knowledge of serpin genes in this insect remain largely unknown. In this study, we performed a systematic analysis of the serpin genes in C. pomonella, obtaining 26 serpins from the C. pomonella genome. Subsequently, their sequ

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Invernizzi, Alessandro, Alessandro Torre, Salvatore Parrulli, et al. "Retinal findings in patients with COVID-19: Results from the SERPICO-19 study." EClinicalMedicine 27 (October 2020): 100550. http://dx.doi.org/10.1016/j.eclinm.2020.100550.

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Hayden, Linda Bailey. "Prof. Sebastiano B. Serpico: Modeling the Important Impact of Research on Education [Education]." IEEE Geoscience and Remote Sensing Magazine 8, no. 3 (2020): 100–101. http://dx.doi.org/10.1109/mgrs.2020.2998332.

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Garrido-Rodríguez, Pedro, Miguel Carmena-Bargueño, María Eugenia de la Morena-Barrio, et al. "Analysis of AlphaFold and molecular dynamics structure predictions of mutations in serpins." PLOS ONE 19, no. 7 (2024): e0304451. http://dx.doi.org/10.1371/journal.pone.0304451.

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Serine protease inhibitors (serpins) include thousands of structurally conserved proteins playing key roles in many organisms. Mutations affecting serpins may disturb their conformation, leading to inactive forms. Unfortunately, conformational consequences of serpin mutations are difficult to predict. In this study, we integrate experimental data of patients with mutations affecting one serpin with the predictions obtained by AlphaFold and molecular dynamics. Five SERPINC1 mutations causing antithrombin deficiency, the strongest congenital thrombophilia were selected from a cohort of 350 unrel

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8

Zhang, Ruonan, Zichun Zhong, Liyan He, et al. "Characterization of Serpin Family Genes in Three Rice Planthopper Species and Their Expression Profiles in Response to Metarhizium Infection." Agronomy 14, no. 11 (2024): 2630. http://dx.doi.org/10.3390/agronomy14112630.

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Rice planthoppers, including Nilaparvata lugens, Sogatella furcifera, and Laodelphax striatellus, are major agricultural pests. Serpins, which function as serine protease inhibitors, play a pivotal role in the immune systems of these insects, especially within the Toll signaling pathway and the prophenoloxidase (PPO) cascade. This study presents a comparative analysis of serpin genes among these species, highlighting their roles in immunity and development. Utilizing genomic and bioinformatics approaches, we identified 11, 11, and 14 serpin genes in N. lugens, S. furcifera, and L. striatellus,

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Nagahashi, Kotomi, Katsuhiro Takano, Katsue Suzuki-Inoue, et al. "Mutation in a highly conserved glycine residue in strand 5B of plasminogen activator inhibitor 1 causes polymerisation." Thrombosis and Haemostasis 117, no. 05 (2017): 860–69. http://dx.doi.org/10.1160/th16-07-0572.

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SummarySerpinopathy is characterised as abnormal accumulation of serine protease inhibitors (SERPINs) in cells and results in clinical symptoms owing to lack of SERPIN function or excessive accumulation of abnormal SERPIN. We recently identified a patient with functional deficiency of plasminogen activator inhibitor-1 (PAI-1), a member of the SERPIN superfamily. The patient exhibited life-threatening bleeding tendencies, which have also been observed in patients with a complete deficiency in PAI-1. Sequence analysis revealed a homozygous singlenucleotide substitution from guanine to cytosine a

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Marinho, Paula M., Allexya A. A. Marcos, Ana Marisa P. Castello Branco, et al. "Results from the SERPICO-19 study – the role of retinal evaluation and in vivo vascular assessment in COVID-19." EClinicalMedicine 29-30 (December 2020): 100655. http://dx.doi.org/10.1016/j.eclinm.2020.100655.

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Manandhar, Sandeep, Patrick Bouthemy, Erik Welf, Gaudenz Danuser, Philippe Roudot, and Charles Kervrann. "3D flow field estimation and assessment for live cell fluorescence microscopy." Bioinformatics 36, no. 5 (2019): 1317–25. http://dx.doi.org/10.1093/bioinformatics/btz780.

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Abstract Motivation The revolution in light sheet microscopy enables the concurrent observation of thousands of dynamic processes, from single molecules to cellular organelles, with high spatiotemporal resolution. However, challenges in the interpretation of multidimensional data requires the fully automatic measurement of those motions to link local processes to cellular functions. This includes the design and the implementation of image processing pipelines able to deal with diverse motion types, and 3D visualization tools adapted to the human visual system. Results Here, we describe a new m

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Salang, Rosnanee, Wansika Phadungsil, Amornrat Geadkaew-Krenc, and Rudi Grams. "Investigation of a Serine Protease Inhibitor Active in the Infectious Stage of the Human Liver Fluke Opisthorchis viverrini." Pathogens 13, no. 8 (2024): 678. http://dx.doi.org/10.3390/pathogens13080678.

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Serine protease inhibitors (serpins) participate in the regulation of inflammation, blood coagulation, and complement activation in humans. This research aimed to identify and characterize such inhibitors of the human liver fluke Opisthorchis viverrini. Parasite proteins that might contribute to the modulation of host physiology are of particular interest, especially as chronic opisthorchiasis increases the risk of developing biliary cancer. BLAST was used to find hypothetical serpins predicted from the parasite genome data. RNA extraction and reverse transcriptase PCR were used to isolate a s

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Dong, Chongmei, Ting-Chun Huang, and Thomas H. Roberts. "Genes Encoding Structurally Conserved Serpins in the Wheat Genome: Identification and Expression Profiles during Plant Development and Abiotic and Biotic Stress." International Journal of Molecular Sciences 24, no. 3 (2023): 2707. http://dx.doi.org/10.3390/ijms24032707.

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Serpins constitute a family of proteins with a very wide distribution in nature. Serpins have a well-conserved tertiary structure enabling irreversible protease inhibition or other specific biochemical functions. We examined the 189 putative wheat serpin genes previously identified by Benbow et al. (2019) via analysis of gene annotations (RefSeq v1.0) and combined our previous examinations of wheat ESTs and the 454 genome assembly. We found that 81 of the 189 putative serpin genes, plus two manually annotated genes, encode full-length, structurally conserved serpins. Expression of these serpin

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de la Morena-Barrio, María, Edna Sandoval, Pilar Llamas, et al. "High levels of latent antithrombin in plasma from patients with antithrombin deficiency." Thrombosis and Haemostasis 117, no. 05 (2017): 880–88. http://dx.doi.org/10.1160/th16-11-0866.

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SummaryAntithrombin is an anticoagulant serpin that efficiently inhibits multiple procoagulant proteases. The cost for the structural flexibility required for this function is the vulnerability to mutations that impact its folding pathway. Most conformational mutations identified in serpins cause polymerisation. Only three mutations in SERPINC1 affecting two residues have been found to favour transformation to the latent conformation of antithrombin, another hyperstable non-anticoagulant form with strong antiangiogenic activity that constitutes 3 % of plasma antithrombin in healthy subjects. T

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Jairajpuri, Mohamad Aman, and Shoyab Ansari. "Using serpins cysteine protease cross-specificity to possibly trap SARS-CoV-2 Mpro with reactive center loop chimera." Clinical Science 134, no. 17 (2020): 2235–41. http://dx.doi.org/10.1042/cs20200767.

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Abstract Human serine protease inhibitors (serpins) are the main inhibitors of serine proteases, but some of them also have the capability to effectively inhibit cysteine proteases. Severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2) main protease (Mpro) is a chymotrypsin-type cysteine protease that is needed to produce functional proteins essential for virus replication and transcription. Serpin traps its target proteases by presenting a reactive center loop (RCL) as protease-specific cleavage site, resulting in protease inactivation. Mpro target sites with its active site serine and

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Dolmer, Klavs, та Peter G. W. Gettins. "How the Serpin α1-Proteinase Inhibitor Folds". Journal of Biological Chemistry 287, № 15 (2012): 12425–32. http://dx.doi.org/10.1074/jbc.m111.315465.

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Serpins are remarkable and unique proteins in being able to spontaneously fold into a metastable conformation without the aid of a chaperone or prodomain. This metastable conformation is essential for inhibition of proteinases, so that massive serpin conformational change, driven by the favorable energetics of relaxation of the metastable conformation to the more stable one, can kinetically trap the proteinase-serpin acylenzyme intermediate. Failure to direct folding to the metastable conformation would lead to inactive, latent serpin. How serpins fold into such a metastable state is unknown.

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Quezada, Landys A. Lopez, and James H. McKerrow. "Schistosome serine protease inhibitors: parasite defense or homeostasis?" Anais da Academia Brasileira de Ciências 83, no. 2 (2011): 663–72. http://dx.doi.org/10.1590/s0001-37652011000200025.

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Serpins are a structurally conserved family of macromolecular inhibitors found in numerous biological systems. The completion and annotation of the genomes of Schistosoma mansoni and Schistosoma japonicum has enabled the identification by phylogenetic analysis of two major serpin clades. S. mansoni shows a greater multiplicity of serpin genes, perhaps reflecting adaptation to infection of a human host. Putative targets of schistosome serpins can be predicted from the sequence of the reactive center loop (RCL). Schistosome serpins may play important roles in both post-translational regulation o

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Rehman, Shazia, Bodil Jørgensen, Ejaz Aziz, Riffat Batool, Samar Naseer, and Søren K. Rasmussen. "Genome Wide Identification and Comparative Analysis of the Serpin Gene Family in Brachypodium and Barley." Plants 9, no. 11 (2020): 1439. http://dx.doi.org/10.3390/plants9111439.

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Serpins (serine protease inhibitors) constitute one of the largest and most widely distributed superfamilies of protease inhibitors and have been identified in nearly all organisms. To gain significant insights, a comprehensive in silico analysis of the serpin gene family was carried out in the model plant for temperate grasses Brachypodium distachyon and barley Hordeum vulgare using bioinformatic tools at the genome level for the first time. We identified a total of 27 BdSRPs and 25 HvSRP genes in Brachypodium and barley, respectively, showing an unexpectedly high gene number in these model p

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Ran, Maoshuang, Yulian Shi, Boning Li, et al. "Genome-Wide Characterization and Comparative Genomic Analysis of the Serpin Gene Family in Microsporidian Nosema bombycis." International Journal of Molecular Sciences 24, no. 1 (2022): 550. http://dx.doi.org/10.3390/ijms24010550.

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Microsporidia are ubiquitous in the environment, infecting almost all invertebrates, vertebrates, and some protists. The microsporidian Nosema bombycis causes silkworms pébrine disease and leads to huge economic losses. Parasite secreted proteins play vital roles in pathogen–host interactions. Serine protease inhibitors (serpins), belonging to the largest and most broadly distributed protease inhibitor superfamily, are also found in Microsporidia. In this study, we characterized 19 serpins (NbSPNs) in N. bombycis; eight of them were predicted with signal peptides. All NbSPN proteins contain a

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Al-Khatib, Sohaib, Mohammad Nitham Almajali, Ayah Al-Bzour, Joud Al-Ramadneh, Laila Sa'd, and Noor Othman. "Abstract 5594: Exploring genetic determinants: A comprehensive analysis of SERPINB family variants and prognosis in Jordanian glioblastoma multiforme patients." Cancer Research 84, no. 6_Supplement (2024): 5594. http://dx.doi.org/10.1158/1538-7445.am2024-5594.

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Abstract Background: Glioblastoma multiforme (GBM) is a major concern with high fatality rate. In Jordan, the incidence of GBM has notably increased, emphasizing the urgency for population-specific research. Serpins are serine proteinase inhibitors, with several Serpins being overexpressed in cancer cells however the exact mechanism by which they affect GBM progression remains unclear. Thus, we aim to analyze the single-nucleotide polymorphism (SNP) of SERPINB11 and its association with GBM survival. Methods: A cohort of 63 GBM patients recruited from King Abdullah University Hospital (KAUH) i

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Eszterbauer, Edit, Dóra Sipos, Győző L. Kaján, et al. "Genetic Diversity of Serine Protease Inhibitors in Myxozoan (Cnidaria, Myxozoa) Fish Parasites." Microorganisms 8, no. 10 (2020): 1502. http://dx.doi.org/10.3390/microorganisms8101502.

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We studied the genetic variability of serine protease inhibitors (serpins) of Myxozoa, microscopic endoparasites of fish. Myxozoans affect the health of both farmed and wild fish populations, causing diseases and mortalities. Despite their global impact, no effective protection exists against these parasites. Serpins were reported as important factors for host invasion and immune evasion, and as promising targets for the development of antiparasitic therapies. For the first time, we identified and aligned serpin sequences from high throughput sequencing datasets of ten myxozoan species, and an

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MAINKAR, PAWAN S., MANOJ M. L, DEEPANSHU JAYASWAL, YAMINI AGARWAL, RAKESH K. PRAJAPAT, and REKHA KANSAL. "Identification and in-silico characterization of Serpin genes in legumes genomes." Indian Journal of Agricultural Sciences 90, no. 9 (2020): 1763–68. http://dx.doi.org/10.56093/ijas.v90i9.106624.

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Serine protease inhibitors (serpins) are a unique family of protease inhibitor containing mobile reactive center loop. The availability of genome sequences of pigeonpea, soybean, commanbean, cowpea, mungbean and adzuki bean provided an opportunity to search for the serpin genes. A total of seven serpin genes were identified in the above legume genomes. Phylogenetic analysis of legume serpins, devided them into two major clades (Clade-I:VanSerpin, VraSerpin, VunSerpin, PvuSerpin and clade-II: GmaSerpin1, GmaSerpin2 and CcaSerpin) based on conserved reactive center (P2-P1’), domains and exon-int

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Tyagi, Suresh C. "Role of oxidative mixed-disulfide formation in elastase–serine proteinase inhibitor (serpin) complex." Biochemistry and Cell Biology 74, no. 3 (1996): 391–401. http://dx.doi.org/10.1139/o96-042.

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To understand the role of thiol and oxidative mixed-disulfide exchange reaction in serpins, we analyzed the conformation of native and mixed-disulfide forms of α1-proteinase inhibitor (α1PI), α1-antichymotrypsin (α1-ACT), α2-antiplasmin (α2-AP), angiotensinogen, and ovalbumin. The conformation of native and oxidized mixed-disulfide serpins was measured by transverse urea gradient (TUG) gels. The results suggest that the acute phase proteins α1-PI and α1-ACT undergo conformational changes following oxidative mixed-disulfide formation and that α2-AP and angiotensinogen do not. The kinetics of di

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Wilkinson, David J. "Serpins in cartilage and osteoarthritis: what do we know?" Biochemical Society Transactions 49, no. 2 (2021): 1013–26. http://dx.doi.org/10.1042/bst20201231.

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Serpins (serine proteinase inhibitors) are an ancient superfamily of structurally similar proteins, the majority of which use an elegant suicide inhibition mechanism to target serine proteinases. Despite likely evolving from a single common ancestor, the 36 human serpins have established roles regulating diverse biological processes, such as blood coagulation, embryonic development and extracellular matrix (ECM) turnover. Genetic mutations in serpin genes underpin a host of monogenic disorders — collectively termed the ‘serpinopathies’ — but serpin dysregulation has also been shown to drive pa

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Moon, Kristin B., Peter C. Turner, and Richard W. Moyer. "SPI-1-Dependent Host Range of Rabbitpox Virus and Complex Formation with Cathepsin G Is Associated with Serpin Motifs." Journal of Virology 73, no. 11 (1999): 8999–9010. http://dx.doi.org/10.1128/jvi.73.11.8999-9010.1999.

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ABSTRACT Serpins are a superfamily of serine proteinase inhibitors which function to regulate a number of key biological processes including fibrinolysis, inflammation, and cell migration. Poxviruses are the only viruses known to encode functional serpins. While some poxvirus serpins regulate inflammation (myxoma virus SERP1 and cowpox virus [CPV] crmA/SPI-2) or apoptosis (myxoma virus SERP2 and CPV crmA/SPI-2), the function of other poxvirus serpins remains unknown. The rabbitpox virus (RPV) SPI-1 protein is 47% identical to crmA and shares all of the serpin structural motifs. However, no ser

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Eszterbauer, Edit, Dóra Szegő, Krisztina Ursu, Dóra Sipos, and Ákos Gellért. "Serine protease inhibitors of the whirling disease parasite Myxobolus cerebralis (Cnidaria, Myxozoa): Expression profiling and functional predictions." PLOS ONE 16, no. 3 (2021): e0249266. http://dx.doi.org/10.1371/journal.pone.0249266.

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Here, we studied the expression pattern and putative function of four, previously identified serine protease inhibitors (serpins) of Myxobolus cerebralis, a pathogenic myxozoan species (Cnidaria: Myxozoa) causing whirling disease of salmonid fishes. The relative expression profiles of serpins were determined at different developmental stages both in fish and in annelid hosts using serpin-specific qPCR assays. The expression of serpin Mc-S1 was similar throughout the life cycle, whereas a significant decrease was detected in the relative expression of Mc-S3 and Mc-S5 during the development in f

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Hejgaard, Jørn, William A. Laing, Salla Marttila, Andrew P. Gleave, and Thomas H. Roberts. "Serpins in fruit and vegetative tissues of apple (Malus domestica): expression of four serpins with distinct reactive centres and characterisation of a major inhibitory seed form, MdZ1b." Functional Plant Biology 32, no. 6 (2005): 517. http://dx.doi.org/10.1071/fp04220.

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Most serpins irreversibly inhibit serine proteinases of the chymotrypsin family using a suicide-substrate-based mechanism. Serpins are present in all domains of life, but physiological functions in the plant kingdom are yet to be elucidated. Inhibitory properties of many abundant cereal grain serpins are well characterised, but serpins have not been identified in eudicot seeds. In apple (Malus domestica Borkh.), the origin of 88 serpin expressed sequence tags (ESTs) identified among 160 000 ESTs from 30 cultivar-, tissue- and time-specific libraries showed that serpin genes are expressed in a

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Bao, Jialing, Guoqing Pan, Mortimer Poncz, Junhong Wei, Maoshuang Ran, and Zeyang Zhou. "Serpin functions in host-pathogen interactions." PeerJ 6 (April 5, 2018): e4557. http://dx.doi.org/10.7717/peerj.4557.

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Serpins are a broadly distributed superfamily of protease inhibitors that are present in all kingdoms of life. The acronym, serpin, is derived from their function as potentserineproteasesinhibitors. Early studies of serpins focused on their functions in haemostasis since modulating serine proteases activities are essential for coagulation. Additional research has revealed that serpins function in infection and inflammation, by modulating serine and cysteine proteases activities. The aim of this review is to summarize the accumulating findings and current understanding of the functions of serpi

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Spence, Matthew A., Matthew D. Mortimer, Ashley M. Buckle, Bui Quang Minh, and Colin J. Jackson. "A Comprehensive Phylogenetic Analysis of the Serpin Superfamily." Molecular Biology and Evolution 38, no. 7 (2021): 2915–29. http://dx.doi.org/10.1093/molbev/msab081.

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Abstract Serine protease inhibitors (serpins) are found in all kingdoms of life and play essential roles in multiple physiological processes. Owing to the diversity of the superfamily, phylogenetic analysis is challenging and prokaryotic serpins have been speculated to have been acquired from Metazoa through horizontal gene transfer due to their unexpectedly high homology. Here, we have leveraged a structural alignment of diverse serpins to generate a comprehensive 6,000-sequence phylogeny that encompasses serpins from all kingdoms of life. We show that in addition to a central “hub” of highly

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Khan, Mohammad Sazzad, Poonam Singh, Asim Azhar, et al. "Serpin Inhibition Mechanism: A Delicate Balance between Native Metastable State and Polymerization." Journal of Amino Acids 2011 (May 24, 2011): 1–10. http://dx.doi.org/10.4061/2011/606797.

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The serpins (serine proteinase inhibitors) are structurally similar but functionally diverse proteins that fold into a conserved structure and employ a unique suicide substrate-like inhibitory mechanism. Serpins play absolutely critical role in the control of proteases involved in the inflammatory, complement, coagulation and fibrinolytic pathways and are associated with many conformational diseases. Serpin's native state is a metastable state which transforms to a more stable state during its inhibitory mechanism. Serpin in the native form is in the stressed (S) conformation that undergoes a

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Ge, Zhao-Yu, Pin-Jun Wan, Xiong-Feng Cheng, Yang Zhang, Guo-Qing Li, and Zhao-Jun Han. "Cloning and characterization of serpin-like genes from the striped rice stem borer, Chilo suppressalis." Genome 56, no. 6 (2013): 359–66. http://dx.doi.org/10.1139/gen-2013-0051.

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Serpins, also called serine proteinase inhibitors, are widely distributed in eukaryotes. In insects, serpins play important roles in regulating immune responses, gut physiology, and other processes. Here, we report the cloning and characterization of 12 serpin-like cDNAs from the striped rice stem borer (Chilo suppressalis), a major rice pest. The putative proteins share significant sequence similarity with known insect serpins, especially those from lepidopterons. Analysis of functional domains revealed that nine of the cloned serpins are putative trypsin- or chymotrypsin-like inhibitors; two

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Liu, Huawei, Jiahui Xu, Luoling Wang, et al. "Serpin-1a and serpin-6 regulate the Toll pathway immune homeostasis by synergistically inhibiting the Spätzle-processing enzyme CLIP2 in silkworm, Bombyx mori." PLOS Pathogens 19, no. 10 (2023): e1011740. http://dx.doi.org/10.1371/journal.ppat.1011740.

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The Toll receptor signaling pathway is an important innate immune response of insects to pathogen infection; its extracellular signal transduction involves serine protease cascade activation. However, excessive or constitutive activation of the Toll pathway can be detrimental. Hence, the balance between activation and inhibition of the extracellular protease cascade must be tightly regulated to achieve favorable outcomes. Previous studies have shown that serpins—serine protease inhibitors—negatively regulate insect innate immunity by inhibiting extracellular protease cascade signaling. Althoug

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Gettins, Peter G. W., and Steven T. Olson. "Inhibitory serpins. New insights into their folding, polymerization, regulation and clearance." Biochemical Journal 473, no. 15 (2016): 2273–93. http://dx.doi.org/10.1042/bcj20160014.

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Serpins are a widely distributed family of high molecular mass protein proteinase inhibitors that can inhibit both serine and cysteine proteinases by a remarkable mechanism-based kinetic trapping of an acyl or thioacyl enzyme intermediate that involves massive conformational transformation. The trapping is based on distortion of the proteinase in the complex, with energy derived from the unique metastability of the active serpin. Serpins are the favoured inhibitors for regulation of proteinases in complex proteolytic cascades, such as are involved in blood coagulation, fibrinolysis and complem

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Lee, Christine N., Brooke Ashlyn Hall, Leah Sanford, and Adebayo J. Molehin. "Molecular Characterization and Functional Analysis of a Schistosoma mansoni Serine Protease Inhibitor, Smserpin-p46." Microorganisms 12, no. 6 (2024): 1164. http://dx.doi.org/10.3390/microorganisms12061164.

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Serine protease inhibitors are a superfamily of proteins that regulate various physiological processes including fibrinolysis, inflammation and immune responses. In parasite systems, serpins are believed to play important roles in parasite colonization, inhibition of host immune serine proteases and penetration of defensive barriers. However, serpins are less well characterized in schistosomes. In this study, a Schistosoma mansoni serpin (Smserpin-p46) containing a 1360 base pair open reading frame, was cloned, expressed and functionally characterized. Bioinformatics analysis revealed that Sms

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Al-Khatib, Sohaib M., Ayah N. Al-Bzour, Mohammad N. Al-Majali, et al. "Exploring Genetic Determinants: A Comprehensive Analysis of Serpin B Family SNPs and Prognosis in Glioblastoma Multiforme Patients." Cancers 16, no. 6 (2024): 1112. http://dx.doi.org/10.3390/cancers16061112.

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Serpins are serine proteinase inhibitors, with several serpins being overexpressed in cancer cells. Thus, we aim to analyze the single-nucleotide polymorphism (SNP) of Serpinb11 and its association with GBM survival. A cohort of 63 GBM patients recruited from King Abdullah University Hospital in Jordan underwent polymorphism analysis and overall survival (OS) assessments. The Cancer Genome Atlas (GBM) cohort was useful for validation. We constructed a risk score using the principal component analysis for the following Serpin genes: Serpinb3, Serpinb5, Serpinb6, Serpinb11, and Serpinb12, and pa

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BJÖRK, Ingemar, Kerstin NORDLING, Elke RAUB-SEGALL, Ulf HELLMAN, and Steven T. OLSON. "Inactivation of papain by antithrombin due to autolytic digestion: a model of serpin inactivation of cysteine proteinases." Biochemical Journal 335, no. 3 (1998): 701–9. http://dx.doi.org/10.1042/bj3350701.

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Cross-class inhibition of cysteine proteinases by serpins differs from serpin inhibition of serine proteinases primarily in that no stable serpin–cysteine proteinase complex can be demonstrated. This difference in reaction mechanism was elucidated by studies of the inactivation of the cysteine proteinases, papain and cathepsin L, by the serpin antithrombin. The two proteinases were inactivated with second-order rate constants of (1.6±0.1)×103 and (8.6±0.4)×102 M-1·s-1 respectively. An antithrombin to papain inactivation stoichiometry of ∼ 3 indicated extensive cleavage of the inhibitor concurr

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Balashova, M. V., L. V. Lyutova, Yu A. Rudenskaya, et al. "Anticoagulative and anticomplementary activity of endogenous inhibitor preparation from hepatopancreas of red king crab (paralithosed camtschaticus) towards human blood." Biomeditsinskaya Khimiya 58, no. 2 (2012): 176–88. http://dx.doi.org/10.18097/pbmc20125802176.

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Serpins (SERine Protease INhibitors) - is large and diverse group of proteins with similar structures, which can inhibit both serine and cysteine proteases by an irreversible suicide mechanism. A novel serpin from hepatopancreas of Red King Crab (Paralithosed camtschaticus) was obtained and was studied its effect on the process of human blood plasma clotting. The investigated serpin shows a noticeable anticoagulative activity, which increases dramatically in the combined action with heparine. Though the inhibitor has almost no effect on thrombin, it inhibits C1s (C1-esterase). We studied the a

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Varkoly, Kyle, Roxana Beladi, Mostafa Hamada, Grant McFadden, James Irving, and Alexandra R. Lucas. "Viral SERPINS—A Family of Highly Potent Immune-Modulating Therapeutic Proteins." Biomolecules 13, no. 9 (2023): 1393. http://dx.doi.org/10.3390/biom13091393.

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Serine protease inhibitors, SERPINS, are a highly conserved family of proteins that regulate serine proteases in the central coagulation and immune pathways, representing 2–10% of circulating proteins in the blood. Serine proteases form cascades of sequentially activated enzymes that direct thrombosis (clot formation) and thrombolysis (clot dissolution), complement activation in immune responses and also programmed cell death (apoptosis). Virus-derived serpins have co-evolved with mammalian proteases and serpins, developing into highly effective inhibitors of mammalian proteolytic pathways. Th

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Wells, Michael, William Sheffield, and Morris Blajchman. "The Clearance of Thrombin-antithrombin and Related Serpin-enzyme Complexes from the Circulation: Role of Various Hepatocyte Receptors." Thrombosis and Haemostasis 81, no. 03 (1999): 325–37. http://dx.doi.org/10.1055/s-0037-1614472.

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IntroductionPeptide bond cleavage can herald the end of a protein’s active life, or its transformation from an inactive precursor to an active enzyme. If the newly activated protein is a proteinase, even a highly specific proteinase, then its activity must be regulated in order that unbridled cleavage and damage to the host organism do not ensue. Such regulation for many of the key serine proteinases of the coagulation, fibrinolytic, complement, and inflammatory pathways is provided by the inhibitory proteins of the serpin family.The serpins are a large family of over 100 proteins (1). Many ar

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Guerin, Jean-Luc, Jacqueline Gelfi, Christelle Camus, et al. "Characterization and functional analysis of Serp3: a novel myxoma virus-encoded serpin involved in virulence." Journal of General Virology 82, no. 6 (2001): 1407–17. http://dx.doi.org/10.1099/0022-1317-82-6-1407.

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Myxoma virus (MV), a member of the family Poxviridae, is the causative agent of myxomatosis, a fatal disease of the European rabbit. The MV genome is a linear, double-stranded DNA molecule that encodes several factors important for evasion of the host immune system. Sequencing the right-end region of the MV genome identified an 801 bp open reading frame (ORF) encoding a polypeptide that belongs to the serpin superfamily. To date, two MV-encoded serpins have been characterized: SERP-1 binds to several targets and is an anti-inflammatory molecule, whereas Serp2 is essential for virus virulence a

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Irving, James A., Robert N. Pike, Arthur M. Lesk, and James C. Whisstock. "Phylogeny of the Serpin Superfamily: Implications of Patterns of Amino Acid Conservation for Structure and Function." Genome Research 10, no. 12 (2000): 1845–64. http://dx.doi.org/10.1101/gr.147800.

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We present a comprehensive alignment and phylogenetic analysis of the serpins, a superfamily of proteins with known members in higher animals, nematodes, insects, plants, and viruses. We analyze, compare, and classify 219 proteins representative of eight major and eight minor subfamilies, using a novel technique of consensus analysis. Patterns of sequence conservation characterize the family as a whole, with a clear relationship to the mechanism of function. Variations of these patterns within phylogenetically distinct groups can be correlated with the divergence of structure and function. The

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Turner, Stephen J., John Silke, Bronwyn Kenshole, and Janet Ruby. "Characterization of the ectromelia virus serpin, SPI-2." Journal of General Virology 81, no. 10 (2000): 2425–30. http://dx.doi.org/10.1099/0022-1317-81-10-2425.

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Poxviruses encode multiple proteins that enable them to evade host responses. Among these are serine protease inhibitors (serpins). One of the earliest serpins described, cowpox virus crmA, acts to inhibit inflammation and apoptosis. crmA homologous serpins, known as SPI-2, are conserved in rabbitpox, vaccinia and variola viruses. Here, we describe the characterization of ectromelia virus (EV) SPI-2. EV SPI-2 encodes a protein of approximately 38 kDa showing >94% identity with other poxviral homologues. Conservative changes in amino acid sequence were found within the reactive site loop and

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Fonseca, Roberto, Stephan-Nicollas Oliveira, Vitor Pomin, André Mecawi, Iracema Araujo, and Paulo Mourão. "Effects of oversulfated and fucosylated chondroitin sulfates on coagulation." Thrombosis and Haemostasis 103, no. 05 (2010): 994–1004. http://dx.doi.org/10.1160/th09-10-0734.

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SummaryWe report the effects of a chemically oversulfated chondroitin sulfate and a naturally fucosylated chondroitin sulfate on the coagulation system. The former has been recently identified as a contaminant of heparin preparations and the latter has been proposed as an alternative anticoagulant. The mechanism of action of these polymers on coagulation is complex and target different components of the coagulation system. They have serpin-independent anticoagulant activity, which preponderates in plasma. They also have serpin-dependent anticoagulant activity but differ significantly in the ta

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Roudnický, Pavel, Jiří Vorel, Jana Ilgová, et al. "Identification and partial characterization of a novel serpin from Eudiplozoon nipponicum (Monogenea, Polyopisthocotylea)." Parasite 25 (2018): 61. http://dx.doi.org/10.1051/parasite/2018062.

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Background: Serpins are a superfamily of serine peptidase inhibitors that participate in the regulation of many physiological and cell peptidase-mediated processes in all organisms (e.g. in blood clotting, complement activation, fibrinolysis, inflammation, and programmed cell death). It was postulated that in the blood-feeding members of the monogenean family Diplozoidae, serpins could play an important role in the prevention of thrombus formation, activation of complement, inflammation in the host, and/or in the endogenous regulation of protein degradation. Results: In silico analysis showed

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Meekins, David A., Xin Zhang, Kevin P. Battaile, Scott Lovell, and Kristin Michel. "1.45 Å resolution structure of SRPN18 from the malaria vectorAnopheles gambiae." Acta Crystallographica Section F Structural Biology Communications 72, no. 12 (2016): 853–62. http://dx.doi.org/10.1107/s2053230x16017854.

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Serine protease inhibitors (serpins) in insects function within development, wound healing and immunity. The genome of the African malaria vector,Anopheles gambiae, encodes 23 distinct serpin proteins, several of which are implicated in disease-relevant physiological responses.A. gambiaeserpin 18 (SRPN18) was previously categorized as non-inhibitory based on the sequence of its reactive-center loop (RCL), a region responsible for targeting and initiating protease inhibition. The crystal structure ofA. gambiaeSRPN18 was determined to a resolution of 1.45 Å, including nearly the entire RCL in on

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Patston, PA, RL Medcalf, Y. Kourteva, and M. Schapira. "C1-inhibitor-serine proteinase complexes and the biosynthesis of C1- inhibitor by Hep G2 and U 937 cells." Blood 82, no. 11 (1993): 3371–79. http://dx.doi.org/10.1182/blood.v82.11.3371.3371.

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Abstract The biosynthesis of the serpin alpha 1-proteinase inhibitor is regulated by a feedback mechanism whereby complexes between alpha 1- proteinase inhibitor and serine proteinases bind to liver cells and monocytes, a reaction that activates alpha 1-proteinase-inhibitor gene transcription. Such a mechanism may form the basis for the development of new therapeutic strategies for serpin deficiency states with reduced levels of otherwise normally functioning serpins. This issue was addressed for C1-inhibitor, the missing serpin in hereditary angioedema. C1-inhibitor biosynthesis by Hep G2 hep

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Patston, PA, RL Medcalf, Y. Kourteva, and M. Schapira. "C1-inhibitor-serine proteinase complexes and the biosynthesis of C1- inhibitor by Hep G2 and U 937 cells." Blood 82, no. 11 (1993): 3371–79. http://dx.doi.org/10.1182/blood.v82.11.3371.bloodjournal82113371.

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The biosynthesis of the serpin alpha 1-proteinase inhibitor is regulated by a feedback mechanism whereby complexes between alpha 1- proteinase inhibitor and serine proteinases bind to liver cells and monocytes, a reaction that activates alpha 1-proteinase-inhibitor gene transcription. Such a mechanism may form the basis for the development of new therapeutic strategies for serpin deficiency states with reduced levels of otherwise normally functioning serpins. This issue was addressed for C1-inhibitor, the missing serpin in hereditary angioedema. C1-inhibitor biosynthesis by Hep G2 hepatoma cel

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MORRIS, Emma C., Timothy R. DAFFORN, Sharon L. FORSYTH, et al. "Murine serpin 2A is a redox-sensitive intracellular protein." Biochemical Journal 371, no. 1 (2003): 165–73. http://dx.doi.org/10.1042/bj20021567.

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Murine serpin 2A is expressed at high levels in haemopoietic progenitors and down-regulated on differentiation. When it is constitutively expressed in the multipotent haemopoietic cell line, FDCP-Mix, it causes a delay in differentiation and increased clonogenic potential. The serpin is also dramatically up-regulated on T-cell activation. It has an unusual reactive site Cys-Cys sequence, a unique C-terminal extension and lacks a typical cleavable N-terminal signal sequence. In spite of these features, the protein is not a member of the ovalbumin—serpin family, but is instead most closely relat

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Yan, Zhichao, Qi Fang, Jiqiang Song, et al. "A serpin gene from a parasitoid wasp disrupts host immunity and exhibits adaptive alternative splicing." PLOS Pathogens 19, no. 9 (2023): e1011649. http://dx.doi.org/10.1371/journal.ppat.1011649.

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Alternative splicing (AS) is a major source of protein diversity in eukaryotes, but less is known about its evolution compared to gene duplication (GD). How AS and GD interact is also largely understudied. By constructing the evolutionary trajectory of the serpin gene PpSerpin-1 (Pteromalus puparum serpin 1) in parasitoids and other insects, we found that both AS and GD jointly contribute to serpin protein diversity. These two processes are negatively correlated and show divergent features in both protein and regulatory sequences. Parasitoid wasps exhibit higher numbers of serpin protein/domai

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Zang, Xingxing, Maria Yazdanbakhsh, Haobo Jiang, Michael R. Kanost, and Rick M. Maizels. "A Novel Serpin Expressed by Blood-Borne Microfilariae of the Parasitic Nematode Brugia malayi Inhibits Human Neutrophil Serine Proteinases." Blood 94, no. 4 (1999): 1418–28. http://dx.doi.org/10.1182/blood.v94.4.1418.

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Abstract Serine proteinase inhibitors (serpins) play a vital regulatory role in a wide range of biological processes, and serpins from viruses have been implicated in pathogen evasion of the host defence system. For the first time, we report a functional serpin gene from nematodes that may function in this manner. This gene, named Bm-spn-2, has been isolated from the filarial nematode Brugia malayi, a causative agent of human lymphatic filariasis. Polymerase chain reaction (PCR) and Western blot experiments indicate that Bm-spn-2 is expressed only by microfilariae (Mf), which are the long-live

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