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Relevant bibliographies by topics / Proteine serine

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Academic literature on the topic 'Proteine serine'

Author: Grafiati

Published: 4 June 2021

Last updated: 17 February 2022

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Journal articles on the topic "Proteine serine"

1

Maroncle, Nathalie M., Kelsey E. Sivick, Rebecca Brady, Faye-Ellen Stokes, and Harry L. T. Mobley. "Protease Activity, Secretion, Cell Entry, Cytotoxicity, and Cellular Targets of Secreted Autotransporter Toxin of Uropathogenic Escherichia coli." Infection and Immunity 74, no. 11 (2006): 6124–34. http://dx.doi.org/10.1128/iai.01086-06.

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ABSTRACT The secreted autotransporter toxin (Sat), found predominantly in uropathogenic Escherichia coli, is a member of the SPATE (serine protease autotransporters of Enterobacteriaceae) family and, as such, has serine protease activity and causes cytopathic effects on various cell types. To assess the contribution of the serine protease active site to the mechanism of action of Sat, mutations were made in the first (S256I), in the second (S258A), or in both (S256I/S258A) serine residues within the active site motif. Mutations in the first or both serines reduced protease activity to backgrou

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2

Barrasa, M. Inmaculada, Noam Y. Harel, and James C. Alwine. "The Phosphorylation Status of the Serine-Rich Region of the Human Cytomegalovirus 86-Kilodalton Major Immediate-Early Protein IE2/IEP86 Affects Temporal Viral Gene Expression." Journal of Virology 79, no. 3 (2005): 1428–37. http://dx.doi.org/10.1128/jvi.79.3.1428-1437.2005.

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ABSTRACT The 86-kDa major immediate-early protein (IE2/IEP86) of human cytomegalovirus (HCMV) contains a serine-rich region (amino acids 258 to 275) with several consensus casein kinase II (CKII) sites. We performed extensive mutational analysis of this region, changing serines to alternating alanines and glycines. Mutation of the serines between amino acids 266 and 275 eliminated in vitro phosphorylation by CKII. In vitro CKII phosphorylation of the serines between amino acids 266 and 269 or between amino acids 271 and 275 inhibited the ability of IE2/IEP86 to bind to TATA-binding protein. Co

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Calvo, E., D. Escors, J. A. López, et al. "Phosphorylation and subcellular localization of transmissible gastroenteritis virus nucleocapsid protein in infected cells." Journal of General Virology 86, no. 8 (2005): 2255–67. http://dx.doi.org/10.1099/vir.0.80975-0.

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The nucleocapsid (N) protein is the only phosphorylated structural protein of the coronavirus Transmissible gastroenteritis virus (TGEV). The phosphorylation state and intracellular distribution of TGEV N protein in infected cells were characterized by a combination of techniques including: (i) subcellular fractionation and analysis of tryptic peptides by two-dimensional nano-liquid chromatography, coupled to ion-trap mass spectrometry; (ii) tandem mass-spectrometry analysis of N protein resolved by SDS-PAGE; (iii) Western blotting using two specific antisera for phosphoserine-containing motif

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Lees-Miller, S. P., K. Sakaguchi, S. J. Ullrich, E. Appella, and C. W. Anderson. "Human DNA-activated protein kinase phosphorylates serines 15 and 37 in the amino-terminal transactivation domain of human p53." Molecular and Cellular Biology 12, no. 11 (1992): 5041–49. http://dx.doi.org/10.1128/mcb.12.11.5041.

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Human DNA-PK is a nuclear, serine/threonine protein kinase that, when activated by DNA, phosphorylates several DNA-binding substrates, including the tumor suppressor protein p53. To identify which p53 residues are phosphorylated, we examined DNA-PK's ability to phosphorylate synthetic peptides corresponding to human p53 sequences. Serines 15 and 37 in the amino-terminal transactivation domain of human p53, and serines 7 and 18 of mouse p53, were phosphorylated by DNA-PK in the context of synthetic peptides. Other serines in these p53 peptides, and serines in other p53 peptides, including pepti

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Lees-Miller, S. P., K. Sakaguchi, S. J. Ullrich, E. Appella, and C. W. Anderson. "Human DNA-activated protein kinase phosphorylates serines 15 and 37 in the amino-terminal transactivation domain of human p53." Molecular and Cellular Biology 12, no. 11 (1992): 5041–49. http://dx.doi.org/10.1128/mcb.12.11.5041-5049.1992.

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Human DNA-PK is a nuclear, serine/threonine protein kinase that, when activated by DNA, phosphorylates several DNA-binding substrates, including the tumor suppressor protein p53. To identify which p53 residues are phosphorylated, we examined DNA-PK's ability to phosphorylate synthetic peptides corresponding to human p53 sequences. Serines 15 and 37 in the amino-terminal transactivation domain of human p53, and serines 7 and 18 of mouse p53, were phosphorylated by DNA-PK in the context of synthetic peptides. Other serines in these p53 peptides, and serines in other p53 peptides, including pepti

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6

Navarro-García, Fernando, Adrián Canizalez-Roman, Bao Quan Sui, James P. Nataro, and Yenia Azamar. "The Serine Protease Motif of EspC from Enteropathogenic Escherichia coli Produces Epithelial Damage by a Mechanism Different from That of Pet Toxin from Enteroaggregative E. coli." Infection and Immunity 72, no. 6 (2004): 3609–21. http://dx.doi.org/10.1128/iai.72.6.3609-3621.2004.

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ABSTRACT EspC (Escherichia coli secreted protein C) of enteropathogenic E. coli (EPEC) shows the three classical domains of the autotransporter proteins and has a conserved serine protease motif belonging to the SPATE (serine protease autotransporters of Enterobacteriaceae) subfamily. EspC and its homolog Pet in enteroaggregative E. coli (EAEC) bear the same sequence within the serine protease motif, and both proteins produce enterotoxic effects, suggesting that like Pet, EspC could be internalized to reach and cleave the calmodulin-binding domain of fodrin, causing actin cytoskeleton disrupti

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7

Melegari, Margherita, Sarah K. Wolf, and Robert J. Schneider. "Hepatitis B Virus DNA Replication Is Coordinated by Core Protein Serine Phosphorylation and HBx Expression." Journal of Virology 79, no. 15 (2005): 9810–20. http://dx.doi.org/10.1128/jvi.79.15.9810-9820.2005.

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ABSTRACT The hepatitis B virus (HBV) core protein forms the capsid of viral particles and is essential for viral genome DNA replication and maturation. The C terminus of core protein contains three serines at positions 155, 162, and 170, phosphorylation of which is important for viral DNA replication. We demonstrate that the phosphorylation of these serines is stimulated by the viral HBx protein, a regulatory protein that activates signal transduction pathways and viral replication. HBx is therefore shown to stimulate HBV replication by increasing core serine phosphorylation. Mutational, bioch

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Koehler, Christian J., and Bernd Thiede. "Predominant cleavage of proteins N-terminal to serines and threonines using scandium(III) triflate." JBIC Journal of Biological Inorganic Chemistry 25, no. 1 (2019): 61–66. http://dx.doi.org/10.1007/s00775-019-01733-7.

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Abstract Proteolytic digestion prior to LC–MS analysis is a key step for the identification of proteins. Digestion of proteins is typically performed with trypsin, but certain proteins or important protein sequence regions might be missed using this endoproteinase. Only few alternative endoproteinases are available and chemical cleavage of proteins is rarely used. Recently, it has been reported that some metal complexes can act as artificial proteases. In particular, the Lewis acid scandium(III) triflate has been shown to catalyze the cleavage of peptide bonds to serine and threonine residues.

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Yi, Xian Ping, Jibin Zhou, Lu Huber, et al. "Nuclear compartmentalization of FAK and FRNK in cardiac myocytes." American Journal of Physiology-Heart and Circulatory Physiology 290, no. 6 (2006): H2509—H2515. http://dx.doi.org/10.1152/ajpheart.00659.2005.

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Focal adhesion kinase (FAK) and FAK-related non-kinase (FRNK) accumulate in the nucleus of cardiac myocytes during hypertensive hypertrophy. Nuclear FAK and FRNK are phosphorylated on different serines and form distinct bright spots. The subnuclear distribution of serine-phosphorylated FAK and FRNK was examined in this study by double labeling with fibrillarin, a component of nucleoli, and Sam68, a constituent of Sam68 nuclear bodies. We also investigated the role of protein kinase C (PKC)-mediated phosphorylation of FAK and FRNK on nuclear translocation. PKC activation by 12- O-tetradecanoylp

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DaSilva, John, Lizhong Xu, Hong Joo Kim, W. Todd Miller, and Dafna Bar-Sagi. "Regulation of Sprouty Stability by Mnk1-Dependent Phosphorylation." Molecular and Cellular Biology 26, no. 5 (2006): 1898–907. http://dx.doi.org/10.1128/mcb.26.5.1898-1907.2006.

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ABSTRACT Sprouty (Spry) proteins are negative feedback modulators of receptor tyrosine kinase pathways in Drosophila melanogaster and mammals. Mammalian Spry proteins have been shown to undergo tyrosine and serine phosphorylation in response to growth factor stimulation. While several studies have addressed the function of tyrosine phosphorylation of Spry, little is known about the significance of Spry serine phosphorylation. Here we identify mitogen-activated protein kinase-interacting kinase 1 (Mnk1) as the kinase that phosphorylates human Spry2 (hSpry2) on serines 112 and 121. Mutation of t

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Dissertations / Theses on the topic "Proteine serine"

1

Pomerance, Martine. "Etapes précoces de la transmission du signal des facteurs de croissance : phosphatidylinositol-3 kinase et protéines serine/threonine kinases." Paris 11, 1994. http://www.theses.fr/1994PA11T008.

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Peyron, Jean-Francois. "Etude du role des reactions de phosphorylation au cours de l'activation du lymphocyte t : stimulation precoce d'une activite serine kinase et d'une activite tyrosine kinase." Nice, 1987. http://www.theses.fr/1987NICE4162.

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L'activation des lymphocytes t par le recepteur de l'antigene cd3-ti entraine la stimulation de deux activites kinase independantes: une activite serine kinase qui conduit a la phosphorylation de 2 proteines cytosoliques (pp21 et pp23); une activite tyrosine kinase qui a pour substrats au moins huit proteines cellulaires, cette activite est regulee negativement par l'activation de la proteine kinase c et par le taux amp cyclique intracellulaire

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Lallemand, François. "Modulation de l'expression de proteines regulatrices de l'activite de proteines kinases a serine/threonine dependantes des cyclines par le butyrate de sodium." Paris 11, 1998. http://www.theses.fr/1998PA11T009.

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Donzeau, Michel. "La famille multigénique SRP (Sérine Rich-Protéin) chez saccharomyces cerevisiae : caractérisation du gène SRP2, contrôle de l'expression génique par le froid et l'anaérobiose." Bordeaux 2, 1993. http://www.theses.fr/1993BOR28275.

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Hilmi, Souad. "Myélinogénèse du système nerveux periphérique de la souris - étude de la phosphorylation de la glycoproteine majeure PO de la myeline - identification des sites phosphorylés in vitro et in vivo." Bordeaux 2, 1993. http://www.theses.fr/1993BOR28273.

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Lazaro, Jean-Bernard. "Implication et régulation de la kinase dépendante des cyclines 5 (cdk5) dans la neurogénèse, la myogénèse et le cycle cellulaire." Montpellier 1, 1996. http://www.theses.fr/1996MON1T012.

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Illy, Chantal. "Structures et mécanismes impliqués dans l'assemblage et l'activation du complexe C1 de la voie classique du complément humain." Grenoble 1, 1992. http://www.theses.fr/1992GRE10152.

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Le complexe c1 du systeme complementaire humain est une protease multimoleculaire (comprenant 2 sous-unites, c1q et c1s-c1r-c1r-c1s), dont l'activation declenche la cascade proteolytique de la voie classique du complement. Le travail presente dans cette these a pour objet la caracterisation des sites responsables des interactions ca#2#+-dependantes c1s/c1s, c1r/c1s et c1q/c1s-c1r-c1r-c1s, et des mecanismes d'activation de c1. L'iodation catalysee par la lactoperoxydase de c1s sous ses formes monomere et dimere a permis de definir plus precisement les portions de c1s impliquees dans sa dimerisa

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ZACHAYUS, JEAN-LUC. "Mecanismes de phosphorylation sur les residus serine du recepteur insulinique dans l'hepatocyte foetal de rat en culture. Role de la proteine kinase c et relation avec la reponse glycogenique a l'hormone." Paris 7, 1994. http://www.theses.fr/1994PA077109.

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La phosphorylation du recepteur insulinique resultant de l'activation de la tyrosine kinase intrinseque du recepteur et d'une serine kinase associee est essentielle pour la transduction du signal hormonal. L'objet de notre etude a ete de caracteriser les mecanismes de phosphorylation sur les serines du recepteur insulinique et leur relation avec la reponse glycogenique a l'hormone dans l'hepatocyte ftal en culture. La sous-unite beta du recepteur insulinique a ete revelee comme la phosphoproteine membranaire majeure de l'hepatocyte ftal permeabilise par la digitonine, du fait de sa phosphoryla

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singh, supriya. "NOVEL PROTEIN-PROTEIN INTERACTIONS REGULATE THE PROTEOLYTIC ACTIVITY OF THE PRO- APOPTOTIC SERINE PROTEASE, OMI/HTRA2." Master's thesis, University of Central Florida, 2005. http://digital.library.ucf.edu/cdm/ref/collection/ETD/id/4091.

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Omi/HtrA2 is a mitochondrial serine protease with high homology to the bacterial HtrA proteins. Omi promotes caspase-dependent apoptosis by binding and degrading IAPs-inhibitor of apoptosis proteins. Omi can also induce caspase-independent apoptosis but the actual mechanism is still unknown. IAP's are not the only substrates cleaved by Omi. There are at least two more known substrates of Omi, the HAX-1 and the ped/pea-15 proteins. HS1-associated protein X-1 (HAX-1) is a mitochondrial protein, degraded by Omi after induction of caspase-dependent apoptosis. Ped/pea-15 is also an anti-apoptotic p

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Shakir, Salika Mehreen. "Characterization of a serine/threonine phosphatase-kinase pair in Bacillus anthracis." Oklahoma City : [s.n.], 2010.

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Books on the topic "Proteine serine"

1

Georgiev, Bojidor. Serpins and protein kinase inhibitors: Novel functions, structural features and molecular mechanisms. Nova Science Publishers, 2010.

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2

Carthy, Barry Mc. Ovalbumin, gene Y and serpin inhibitory function. University College Dublin, 1998.

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Barnes, Ruth C. Identification and characterisation of a novel human serpin gene: Leupin. University College Dublin, 1998.

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Pekkarinen, Anja. The serine proteinases of Fusarium grown on cereal proteins and in barley grain and their inhibition by barley proteins. VTT Technical Research Centre of Finland, 2003.

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5

Raouf, Ramin K. Functional regulation of N-methyl-D-aspartate receptors by serine/threonine protein kinases. National Library of Canada = Bibliothèque nationale du Canada, 1999.

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6

Toivola, Diana. Microcystins: Potent tools to study serine/threonine protein phosphatases and their role in cytoskeletal regulation. Åbo Akademi University Press, 1998.

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7

Hodge, Sarah Anne. The study of protein serine/threonine kinase mediated phosphorylation in the cyanobacterium anabaena sp. strain PCC7120. typescript, 1994.

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8

Craig, Gavin Michael. The identification and characterisation of centrosome associated kinase (Cenk), a novel serine/threonine protein kinase expressed in gastrulating mouse embryos. typescript, 1999.

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9

El Servicio Secreto de EE.UU: Protegen a nuestros líderes. Capstone Press, 2014.

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10

West, A. Investigations by mass spectrometry of the interactions of novel serine protease inhibitors with Herpes Simplex Virus type 2 and Human Cytomegalovirus proteases. typescript, 1999.

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Book chapters on the topic "Proteine serine"

1

Barra, Donatella, Filippo Martini, Sebastiana Angelaccio, Stefano Pascarella, Francesco Bossa, and LaVerne Schirch. "Primary Structure Studies on Serine Hydroxymethyltransferase." In Proteins. Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1787-6_78.

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2

Cohen, Patricia T. W. "Overview of protein serine/threonine phosphatases." In Protein Phosphatases. Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-540-40035-6_1.

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3

Kennelly, Peter J. "Prokaryotic Protein-Serine/Threonine Phosphatases." In Protein Phosphatase Protocols. Humana Press, 1998. http://dx.doi.org/10.1385/0-89603-468-2:1.

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Heierhorst, Jörg, Richard Pearson, James Horne, Steven Bozinovski, Bostjan Kobe, and Bruce E. Kemp. "Protein Serine/Threonine Kinases." In Principles of Molecular Regulation. Humana Press, 2000. http://dx.doi.org/10.1007/978-1-59259-032-2_17.

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Shenolikar, Shirish. "Protein Serine/Threonine Phosphatases." In Principles of Molecular Regulation. Humana Press, 2000. http://dx.doi.org/10.1007/978-1-59259-032-2_18.

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Horstkorte, Rüdiger, Bettina Büttner, Kaya Bork, et al. "NSP, Novel Serine Protease." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100942.

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Warkentin, Peter H., Ingemar Lundström, and Pentti Tengvall. "Protein—Protein Interactions Affecting Proteins at Surfaces." In ACS Symposium Series. American Chemical Society, 1995. http://dx.doi.org/10.1021/bk-1995-0602.ch012.

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Donato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, et al. "Protein Serine/Threonine-Phosphatase 2C." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101104.

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Yamashita, Akio. "Serine/Threonine-Protein Kinase SMG1." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101805.

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Janssens, Veerle. "Serine/Threonine-Protein Phosphatase 2A." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101865.

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Conference papers on the topic "Proteine serine"

1

Heckel, A., and K. M. Hasselbach. "PREDICTION OF THE THREE-DIMENSIONAL STRUCTURE OF THE ENZYMATIC PART OF T-PA." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644407.

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Up to now the three-dimensional structure of t-PA or parts of this enzyme is unknown. Using computer graphical methods the spatial structure of the enzymatic part of t-PA is predicted on the hypothesis, the three-dimensional backbone structure of t-PA being similar to that of other serine proteases. The t-PA model was built up in three steps:1) Alignment of the t-PA sequence with other serine proteases. Comparison of enzyme structures available from Brookhaven Protein Data Bank proved elastase as a basis for modeling.2) Exchange of amino acids of elastase differing from the t-PA sequence. The

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2

Strandberg, L., D. Lawrence, and T. Ny. "ISOLATION OF THE GENOMIC REGION CODING FOR TYPE-1 PLASMINOGEN ACTIVATOR INHIBITOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644439.

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The type-1 Plasminogen Activator Inhibitor (PAI-1) has recently been identified as a member of the Serine Protease Inhibitor family (SERPINS). This family of proteins contain many serine protease inhibitors but also functionally unrelated proteins like ovalbumin and anginotensinogen. PAI-1 inhibits both u-PA and t-PA and might therefore be an important regulator of the fibrinolytic system.In order to study the evolution of the Serpin family as well as PAI-1 gene expression we have isolated the genomic region carrying the PAI-1 gene. A cDNA sequence for PAI-1 was used as probe to screen a human

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3

Ny, T., L. Hansson, and B. Åstedt. "ISOLATION OF cDNA FOR TYPE-2 PLASMINOGEN ACTIVATOR INHIBITOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642855.

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The placental type plasminogen activator inhibitor (PAI-2) has been purified from extracts of human placenta and from a histiocytic lymphoma cell line. It is mainly an uPA inhibitor but it also inhibits the two-chain form of tPA.In order to determine the factors regulating PAI-2 gene expression and thereby clarify the physiological role of PAI-2 we have undertaken the molecular cloning of PAI-2 cDNA. A λgt11 expression library prepared from placental mRNA, was screened, immunologically using a monoclonal antibody probe developed against PAI-2 purified from human placenta. When 1.7×105 recombin

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Berkner, K. L., S. J. Busby, J. Gambee, and A. Kumar. "EXPRESSION IN MAMMALIAN CELLS OF FUSION PROTEINS BETWEEN HUMAN FACTORS IX AND VII." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643568.

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The vitamin K-dependent plasma proteins demonstrate remarkable similarities in their structures: all have multiple domains in common and extensive homology is observed within many of these domains. In order to investigate the structure-function relationship of these proteins, we have interchanged domains of one protein (factor IX) with that of another (factor VII) and have compared the expression of these fusion proteins with recombinant and native factors IX and VII. Oligonucleotide-directed mutagenesis was used to generate four fusion proteins: factor IX/VII-1, which contains the factor IX l

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Stenflo, J., A.-K. öhlin, Å. Lundvall та B. Dahlback. "β-HYDROXY ASPARTIC ACID AND ft-HYDROXYASPARAGINE IN THEEGF-HOMOLOGY REGIONS OF PROTEIN C AND PROTEINS". У XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643995.

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The amino acid sequence has been determined for all of the vitamin K-dependent proteins and the gene structure is known for some of them. These findings have shown the proteins to consist of four clearly discernible domains, except protein S which has six domains. The protein domains seem to be coded on separate exons (Foster, D. C. et. al. 1985 Proc. Natl. Acad. Sci. USA 82,4673). The vitamin K-dependent γ-carboxyglutamic acid (Gla) containing domain isthe common structural denominator of the members of this protein family. In addition, all of these proteins except prothrombin contain domains

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Foster, D., B. Schach, M. Rudinsky, et al. "The Effect of Changes in the Leader Sequence of Human Protein C on Biosynthetic Processing and Gamma-Carboxylation." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643648.

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Protein C is the precursor to a serine protease in plasma which contains gamma-carboxy glutamic acid and functions as a potent anticoagulant. Protein C shows considerable structural homology with the other vitamin K-dependent coagulation factors including prothrombin, factor VII, factor IX and factor X. This homology includes the putative pro-peptide region of the prepro leader sequences for these proteins, as well as the leader sequences for gamma-carboxylated proteins from bone. Deletion mutants have been constructed in the cDNA for human protein C in order to test the possibility that the p

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Varela, D., R. O’Hara, and A. C. Neves. "BY-PRODUCTS OF THE WHELK PROCESSING INDUSTRY AS VALUABLE SOURCE OF ANTIOXIDANT PEPTIDES." In World Conference on Waste Management. The International Institute of Knowledge Management, 2021. http://dx.doi.org/10.17501/26510251.2021.1103.

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The fish and shellfish industry processes 851,984 tonnes of fish per year worldwide. However, only 43% of that is consumed, and valuable proteins are processed as waste. Protein hydrolysates are widely used in food technology for their nutritional and functional properties. The goal of this project is to extract protein from whelk by-products derived from the shellfish processing industry and create protein hydrolysates that have marketable value. The by-products were divided into two types: raw (R) and cooked byproduct (C). The proteins were extracted using the pH shift method and quantified

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Tokunaga, F., T. Miyata, T. Nakamura, T. Morita, and S. Iwanaga. "LIPOPOLYSACCHARIDE-SENSITIVE SERINE-PROTEASE ZYMOGEN (FACTOR C) OF LIMULUS HEMOCYTES: IDENTIFICATION AND ALIGNMENT OF PROTEOLYTIC FRAGMENTS PRODUCED DURING THE ACTIVATION SHOW THAT IT IS A NOVEL TYPE OF SERINE-PROTEASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644609.

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Limulus clotting factor, factor C, is a lipopolysaccharide (LPS)-sensitive serine-protease zymogen present in the hemocytes. It is a two-chain glycoprotein (M.W. = 123,000) composed of a heavy chain (M.W. = 80,000) and a light chain (M.W. = 43,000) T. Nakamura et al. (1986) Eur. J. Biochem. 154, 511-521 .On further studies of this zymogen, a single-chain factor C (M.W. = 123,000) was identified by Western blotting technique. The heavy chain had an NH2-terminal sequence of Ser-Gly-Val-Asp-, which was consistent with the NH2-terminal sequence of the single-chain factor C, indicating that the hea

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O'hara, Patrick J., Frank A. Grant, A. Betty, J. Haldmen, and Mark J. Murray. "Structure of the Human Factor VII Gene." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643786.

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Factor VII is a member of a family of vitamin K-dependent, gamma-carboxylated plasma protein which includes factor IX, factor X, protein C, protein S and prothrombin. Activated factor VII (factor Vila) is a plasma serine protease which participates in a cascade of reactions leading to the coagulation of blood. Two overlapping genomic clones containing sequences encoding human factor VII were isolated and characterized. The complete sequence of the gene was determined and found to span 12.8 kilobases. The mRNA for factor VII as demonstrated by cDNA cloning is polyadenylated at multiple sites bu

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de Vries, C. J. M., N. K. Veerman, and H. Pannekoek. "ARTIFICIAL EXON SHUFFLING: CONSTRUCTION OF HYBRID cDNAS CONTAINING DOMAINS OF TISSUE-TYPE PLASMINOGEN ACTIVATOR (T-PA) AND UROKINASE (u-PA)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643940.

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The intriguing finding that functions of t-PA coincide with structural domains and that these domains occur in related proteins, has been the basis to construct hybrid proteins by artificial exon shuffling to prove the conservation of functions in the shuffled domains. The heavy chain (Hch) of t-PA mediates both binding to fibrin and stimulation of plasminogen activator activity via its Finger- and Kringle-2 domain, whereas the light chain (Lch) contains the serine protease moiety of the protein. The Hch of u-PA is very homologous to the Lch of t-PA, but exhibits a higher plasminogen activator

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Reports on the topic "Proteine serine"

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Kelly, Jr, Simms Thomas J., Huang Avis E., Mazur Yan, and Anna. Fibroblast Activation Protein-Alpha, a Serine Protease that Facilitates Metastasis by Modification of Diverse Microenvironments. Defense Technical Information Center, 2011. http://dx.doi.org/10.21236/ada588423.

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

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

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van Harn, J., M. A. Dijkslag, and M. M. van Krimpen. Glycine plus serine requirement of broilers fed low-protein diets : a dose response study. Wageningen Livestock Research, 2018. http://dx.doi.org/10.18174/454645.

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Lin, Chen-Yong. An Epithelial-Derived, Integral Membrane, Kunitz-Type Serine Protease Inhibitor in Breast Cancer. Defense Technical Information Center, 2005. http://dx.doi.org/10.21236/ada442974.

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Lin, Chen-Yong. An Epithelial-Derived, Integral Membrane, Kunitz-Type Serine Protease Inhibitor in Breast Cancer. Defense Technical Information Center, 2002. http://dx.doi.org/10.21236/ada410178.

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Lin, Chen-Yong. An Epithelial-Derived, Integral Membrane, Kunitz-Type serine Protease Inhibitor in Breast Cancer. Defense Technical Information Center, 2004. http://dx.doi.org/10.21236/ada435266.

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Lin, Chen-Yong. An Epithelial-Derived Integral Membrane Kunitz-Type Serine Protease Inhibitor in Breast Cancer. Defense Technical Information Center, 2003. http://dx.doi.org/10.21236/ada420072.

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Chai, Karl X., Li-Mei Chen, and Ying Zhang. Prostasin Serine Protease as a Breast Cancer Invasion Marker and a Metastasis Suppressor. Defense Technical Information Center, 2006. http://dx.doi.org/10.21236/ada460801.

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Dickson, Robert B. A Novel Serine Protease Target for Prevention of Breast Cancer by a Soy Bean-Derived Inhibitor. Defense Technical Information Center, 2001. http://dx.doi.org/10.21236/ada396285.

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