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Journal articles on the topic 'Serpico'

Author: Grafiati

Published: 4 June 2021

Last updated: 3 March 2023

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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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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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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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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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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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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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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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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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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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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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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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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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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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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.v94.4.1418.416k03_1418_1428.

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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-lived blood-d

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Ciaccia, Angelina V., and Frank C. Church. "Determinants of heparin cofactor ii specificity for thrombin." Protein & Peptide Letters 4, no. 4 (1997): 215–24. http://dx.doi.org/10.2174/092986650404221017120326.

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Abstract: Hemostasis is a critical element of the host defense system. The "balance" in hemostasis is achieved by the tight regulation of both procoagulant and anticoagulant proteins. The focus of this short review is on one particular anticoagulant protein, heparin cofactor II (HCII), a member of the serine proteinase (serpin) superfarnily of proteins. A brief overview of serpins and the mechanism by which HCII specifically regulates the activity of the most critical procoagulant proteinase thrombin are addressed.

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Taboada, Carlos, Andrés E. Brunetti, Mariana L. Lyra, et al. "Multiple origins of green coloration in frogs mediated by a novel biliverdin-binding serpin." Proceedings of the National Academy of Sciences 117, no. 31 (2020): 18574–81. http://dx.doi.org/10.1073/pnas.2006771117.

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Many vertebrates have distinctive blue-green bones and other tissues due to unusually high biliverdin concentrations—a phenomenon called chlorosis. Despite its prevalence, the biochemical basis, biology, and evolution of chlorosis are poorly understood. In this study, we show that the occurrence of high biliverdin in anurans (frogs and toads) has evolved multiple times during their evolutionary history, and relies on the same mechanism—the presence of a class of serpin family proteins that bind biliverdin. Using a diverse combination of techniques, we purified these serpins from several specie

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Bird, Catherina H., Elizabeth J. Blink, Claire E. Hirst, et al. "Nucleocytoplasmic Distribution of the Ovalbumin Serpin PI-9 Requires a Nonconventional Nuclear Import Pathway and the Export Factor Crm1." Molecular and Cellular Biology 21, no. 16 (2001): 5396–407. http://dx.doi.org/10.1128/mcb.21.16.5396-5407.2001.

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ABSTRACT Proteinase inhibitor 9 (PI-9) is a human serpin present in the cytoplasm of cytotoxic lymphocytes and epithelial cells. It inhibits the cytotoxic lymphocyte granule proteinase granzyme B (graB) and is thought to protect cytotoxic lymphocytes and bystander cells from graB-mediated apoptosis. Following uptake into cells, graB promotes DNA degradation, rapidly translocating to the nucleus, where it binds a nuclear component. PI-9 should therefore be found in cytotoxic lymphocyte and bystander cell nuclei to ensure complete protection against graB. Here we demonstrate by microscopy and su

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MOLEHIN, ADEBAYO J., GEOFFREY N. GOBERT, PATRICK DRIGUEZ, and DONALD P. MCMANUS. "Functional characterization ofSjB10, an intracellular serpin fromSchistosoma japonicum." Parasitology 141, no. 13 (2014): 1746–60. http://dx.doi.org/10.1017/s0031182014001061.

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SUMMARYSerine protease inhibitors (serpin) play essential roles in many organisms. Mammalian serpins regulate the blood coagulation, fibrinolysis, inflammation and complement activation pathways. In parasitic helminths, serpins are less well characterized, but may also be involved in evasion of the host immune response. In this study, aSchistosoma japonicumserpin (SjB10), containing a 1212 bp open reading frame (ORF), was cloned, expressed and functionally characterized. Sequence analysis, comparative modelling and structural-based alignment revealed thatSjB10contains the essential structural

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Turroni, Francesca, Elena Foroni, Mary O'Connell Motherway, et al. "Characterization of the Serpin-Encoding Gene of Bifidobacterium breve 210B." Applied and Environmental Microbiology 76, no. 10 (2010): 3206–19. http://dx.doi.org/10.1128/aem.02938-09.

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ABSTRACT Members of the serpin (serine protease inhibitor) superfamily have been identified in higher multicellular eukaryotes, as well as in bacteria, although examination of available genome sequences has indicated that homologs of the bacterial serpin-encoding gene (ser) are not widely distributed. In members of the genus Bifidobacterium this gene appears to be present in at least 5, and perhaps up to 9, of the 30 species tested. Moreover, phylogenetic analysis using available bacterial and eukaryotic serpin sequences revealed that bifidobacteria produce serpins that form a separate clade.

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Nallagangula, Krishna. "Cirrhosis of liver: Comparative cross reactivity for quantification of SERPINA4/Kallistatin." Journal of Clinical and Laboratory Research 2, no. 1 (2021): 01–05. http://dx.doi.org/10.31579/2768-0487/005.

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Cirrhosis of liver is an end stage of chronic liver insults from varied etiologies which leads to impaired liver functions. Proteins expressed from liver and enters into circulation reflects degree of liver dysfunction. Serpins (Serine protease inhibitors) are class of plasma proteins expressed from liver; SERPINA4/Kallistatin is a multifunctional serpin clade A protein expressed from liver and concentration in serum is the reflection of extent of liver dysfunction. The present study aimed to compare cross reactivity of serpins for polyclonal and monospecific antibodies in both cirrhotic liver

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Yusova, Olena, Natalia Makarova, and Serhij Verevka. "SERPINS’ REACTIVE SITES LOOPS MOBILITY AND ITS FUNCTIONAL VALUE." Grail of Science, no. 20 (October 6, 2022): 56–65. http://dx.doi.org/10.36074/grail-of-science.30.09.2022.009.

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Protein inhibitors from the serpin family are important regulators of various metabolic processes. They differ significantly from most protein inhibitors of proteinases both in structure and in the mechanism of interaction with proteolytic enzymes. The loop of their reactive site is mobile, and the formed complex with enzymes is a covalent acyl-enzyme. Comparison of the properties of serpins both among themselves and with protein inhibitors of other families indicates the key role of the mobility of the loop of the reactive center in ensuring the selectivity of the inhibitors.

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Green, Clare, Elena Levashina, Carol McKimmie, Tim Dafforn, Jean-Marc Reichhart, and David Gubb. "The necrotic Gene in Drosophila Corresponds to One of a Cluster of Three Serpin Transcripts Mapping at 43A1.2." Genetics 156, no. 3 (2000): 1117–27. http://dx.doi.org/10.1093/genetics/156.3.1117.

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Abstract Mutants of the necrotic (nec) gene in Drosophila melanogaster die in the late pupal stage as pharate adults, or hatch as weak, but relatively normal-looking, flies. Adults develop black melanized spots on the body and leg joints, the abdomen swells with hemolymph, and flies die within 3 or 4 days of eclosion. The TOLL-mediated immune response to fungal infections is constitutively activated in nec mutants and pleiotropic phenotypes include melanization and cellular necrosis. These changes are consistent with activation of one or more proteolytic cascades. The nec gene corresponds to S

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Kryvalap, Yury, та Jan Czyzyk. "The Role of Proteases and Serpin Protease Inhibitors in β-Cell Biology and Diabetes". Biomolecules 12, № 1 (2022): 67. http://dx.doi.org/10.3390/biom12010067.

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Regulation of the equilibrium between proteases and their inhibitors is fundamental to health maintenance. Consequently, developing a means of targeting protease activity to promote tissue regeneration and inhibit inflammation may offer a new strategy in therapy development for diabetes and other diseases. Specifically, recent efforts have focused on serine protease inhibitors, known as serpins, as potential therapeutic targets. The serpin protein family comprises a broad range of protease inhibitors, which are categorized into 16 clades that are all extracellular, with the exception of Clade

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