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Relevant bibliographies by topics / N-terminal domains

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Academic literature on the topic 'N-terminal domains'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "N-terminal domains"

1

Zouharova, Monika, Petr Herman, Kateřina Hofbauerová, Jiri Vondrasek, and Kristyna Bousova. "TRPM6 N-Terminal CaM- and S100A1-Binding Domains." International Journal of Molecular Sciences 20, no. 18 (2019): 4430. http://dx.doi.org/10.3390/ijms20184430.

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Transient receptor potential (TRPs) channels are crucial downstream targets of calcium signalling cascades. They can be modulated either by calcium itself and/or by calcium-binding proteins (CBPs). Intracellular messengers usually interact with binding domains present at the most variable TRP regions—N- and C-cytoplasmic termini. Calmodulin (CaM) is a calcium-dependent cytosolic protein serving as a modulator of most transmembrane receptors. Although CaM-binding domains are widespread within intracellular parts of TRPs, no such binding domain has been characterised at the TRP melastatin member

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Nieuwesteeg, M. A., L. A. Walsh, M. A. Fox, and S. Damjanovski. "Domain specific overexpression of TIMP-2 and TIMP-3 reveals MMP-independent functions of TIMPs during Xenopus laevis development." Biochemistry and Cell Biology 90, no. 4 (2012): 585–95. http://dx.doi.org/10.1139/o2012-014.

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Extracellular matrix remodelling mediates many processes including cell migration and differentiation and is regulated through the enzymatic action of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). TIMPs are secreted proteins, consisting of structurally and functionally distinct N- and C-terminal domains. TIMP N-terminal domains inhibit MMP activity, whereas their C-terminal domains may have cell signalling activity. The in vivo role of TIMP N- and C-terminal domains in regulating developmental events has not previously been demonstrated. Here we investig

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van den Ent, Fusinita M. I., Arnold Vos, and Ronald H. A. Plasterk. "Dissecting the Role of the N-Terminal Domain of Human Immunodeficiency Virus Integrase bytrans-Complementation Analysis." Journal of Virology 73, no. 4 (1999): 3176–83. http://dx.doi.org/10.1128/jvi.73.4.3176-3183.1999.

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ABSTRACT The human immunodeficiency virus (HIV) integrase protein (IN) catalyzes two reactions required to integrate HIV DNA into the human genome: 3′ processing of the viral DNA ends and integration. IN has three domains, the N-terminal zinc-binding domain, the catalytic core, and the C-terminal SH3 domain. Previously, it was shown that IN proteins mutated in different domains could complement each other. We now report that this does not require any overlap between the two complementing proteins; an N-terminal domain, provided intrans, can restore IN activity of a mutant lacking this domain.

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Wickström, Claes, and Ingemar Carlstedt. "N-terminal Cleavage of the Salivary MUC5B Mucin." Journal of Biological Chemistry 276, no. 50 (2001): 47116–21. http://dx.doi.org/10.1074/jbc.m106593200.

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Sequence similarities between the oligomeric mucins (MUC2, MUC5AC, MUC5B) and the von Willebrand factor suggest that they may be assembled in a similar way. After oligomerization, a fragment corresponding to the D1 and D2 domains is released from the von Willebrand factor. This cleavage does not appear to occur in pig submaxillary mucin, the only mammalian mucin in which this cleavage has been examined thus far, but whether other oligomeric mucins undergo N terminus proteolysis is not known. Antibodies recognizing the D1, D2, D3, and the first Cys domains in MUC5B were established and used to

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Tikhonova, I. G., I. I. Baskin, V. A. Palyulin, and N. S. Zefirov. "Molecular Modeling of N-Terminal Domains of NMDA-Receptor. Study of Ligand Binding to N-Terminal Domains." Doklady Biochemistry and Biophysics 397, no. 1-6 (2004): 242–50. http://dx.doi.org/10.1023/b:dobi.0000039474.86331.7a.

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Tanaka, M., W. M. Clouston, and W. Herr. "The Oct-2 glutamine-rich and proline-rich activation domains can synergize with each other or duplicates of themselves to activate transcription." Molecular and Cellular Biology 14, no. 9 (1994): 6046–55. http://dx.doi.org/10.1128/mcb.14.9.6046.

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The B-cell POU homeodomain protein Oct-2 contains two transcriptional activation domains, one N terminal and the other C terminal of the central DNA-binding POU domain. The synergistic action of these two activation domains makes Oct-2 a more potent activator of mRNA promoters than the related broadly expressed octamer motif-binding protein Oct-1, which contains an N-terminal but not a C-terminal Oct-2-like activation domain. Both Oct-2 mRNA promoter activation domains were delineated by truncation analysis: the N-terminal Q domain is a 66-amino-acid region rich in glutamines, and the C-termin

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Tanaka, M., W. M. Clouston, and W. Herr. "The Oct-2 glutamine-rich and proline-rich activation domains can synergize with each other or duplicates of themselves to activate transcription." Molecular and Cellular Biology 14, no. 9 (1994): 6046–55. http://dx.doi.org/10.1128/mcb.14.9.6046-6055.1994.

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The B-cell POU homeodomain protein Oct-2 contains two transcriptional activation domains, one N terminal and the other C terminal of the central DNA-binding POU domain. The synergistic action of these two activation domains makes Oct-2 a more potent activator of mRNA promoters than the related broadly expressed octamer motif-binding protein Oct-1, which contains an N-terminal but not a C-terminal Oct-2-like activation domain. Both Oct-2 mRNA promoter activation domains were delineated by truncation analysis: the N-terminal Q domain is a 66-amino-acid region rich in glutamines, and the C-termin

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8

Surtees, Jennifer A., and Barbara E. Funnell. "P1 ParB Domain Structure Includes Two Independent Multimerization Domains." Journal of Bacteriology 181, no. 19 (1999): 5898–908. http://dx.doi.org/10.1128/jb.181.19.5898-5908.1999.

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ABSTRACT ParB is one of two P1-encoded proteins that are required for active partition of the P1 prophage in Escherichia coli. To probe the native domain structure of ParB, we performed limited proteolytic digestions of full-length ParB, as well as of several N-terminal and C-terminal deletion fragments of ParB. The C-terminal 140 amino acids of ParB form a very trypsin-resistant domain. In contrast, the N terminus is more susceptible to proteolysis, suggesting that it forms a less stably folded domain or domains. Because native ParB is a dimer in solution, we analyzed the ability of ParB frag

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Miller, Gregory J., Stanley D. Dunn, and Eric H. Ball. "Interaction of the N- and C-terminal Domains of Vinculin." Journal of Biological Chemistry 276, no. 15 (2000): 11729–34. http://dx.doi.org/10.1074/jbc.m008646200.

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The vinculin head to tail intramolecular self-association controls its binding sites for other components of focal adhesions. To study this interaction, the head and tail domains were expressed, purified, and assayed for various characteristics of complex formation. Analytical centrifugation demonstrated a strong interaction in solution and formation of a complex more asymmetric than either of the individual domains. A survey of binding conditions using a solid-phase binding assay revealed characteristics of both electrostatic and hydrophobic forces involved in the binding. In addition, circul

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Rubenstein, Eric M., Rhonda R. McCartney, and Martin C. Schmidt. "Regulatory Domains of Snf1-Activating Kinases Determine Pathway Specificity." Eukaryotic Cell 5, no. 4 (2006): 620–27. http://dx.doi.org/10.1128/ec.5.4.620-627.2006.

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ABSTRACT In Saccharomyces cerevisiae, the Snf1 kinase can be activated by any one of three upstream kinases, Sak1, Tos3, or Elm1. All three Snf1-activating kinases contain serine/threonine kinase domains near their N termini and large C-terminal domains with little sequence conservation and previously unknown function. Deletion of the C-terminal domains of Sak1 and Tos3 greatly reduces their ability to activate the Snf1 pathway. In contrast, deletion of the Elm1 C-terminal domain has no effect on Snf1 signaling but abrogates the ability of Elm1 to participate in the morphogenetic-checkpoint si

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Dissertations / Theses on the topic "N-terminal domains"

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Chavda, Alap Pravin. "Analysis of N-terminal domains of inositol 1,4,5-trisphosphate receptors." Thesis, University of Cambridge, 2013. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.648299.

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Zhu, Shujia. "Allosteric signaling in NMDA receptors via the N-terminal domains." Paris 6, 2013. http://www.theses.fr/2013PA066432.

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Les récepteurs au N-méthyl-D-aspartate (RNMDAs) constituent dans le cerveau une classe majeure de récepteurs activés par le neurotransmetteur excitateur glutamate. Ils forment des canaux ioniques perméables au calcium, au rôle essentiel dans la plasticité synaptique. Les RNMDAs s’assemblent en hétérotétramères, usuellement composés des sous-unités GluN1 et GluN2 (A-D). Des travaux ont révélé le rôle essentiel joué par le domaine N-terminal (NTD) des sous-unités GluN2, dans les fonctions spécifiques des sous-unités des RNMDAs. En revanche, on en sait peu concernant la contribution de GluN1, pou

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Nowak, Scott J. "Covalent modifications of histone N-terminal domains during transcription in Drosophila melanogaster." Available to US Hopkins community, 2003. http://wwwlib.umi.com/dissertations/dlnow/308073.

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Winzen, Uwe. "Functional analysis of the N-terminal domains of agrin by recombinant eucaryotic expression." [S.l. : s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=968092020.

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Sanchez, Perez Maria Concepcion. "Study of the N-terminal domains of MDM2 and MDM4, and their potential for targeting by small-molecule drugs." Thesis, University of Edinburgh, 2011. http://hdl.handle.net/1842/8763.

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The MDM2 and MDM4 oncoproteins are both involved in regulating the tumour suppressor, p53. While the MDM2–p53 interface is structurally and biophysically well characterised, the MDM4-p53 interaction has only recently attracted researchers’ attentions. The goal of this project was to establish structural and chemical ground rules for the disruption of the interactions between the N-terminal domains of MDM2/4 and p53, which is an attractive anticancer strategy. In the current work, successful recombinant production and purification protocols for both the N-terminal domains of MDM2 (i.e. MDM2-N,

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King, Katie. "The Roles and Interactions of the N-terminal Domains of Cardiac Myosin Binding Protein-C." Thesis, University of Oxford, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.490093.

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Myosin Binding Protein-C (MyBP-C) is a multi-domain protein located on the thick filaments of striated muscle. Mutations in the gene encoding the cardiac isoform of the protein, cMyBP-C, are known to cause hypertrophic cardiomyopathy (HCM). cMyBP-C is composed of 11 globular domains, eight of which have homology to Igl, the other three to fibronectin III. The N-terminal region of the protein has been assigned a role in the regulation of muscle contraction through its interaction with the Subfragment-2 (S2) portion of myosin.

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Liu, Sheng. "NMR studies of RNA binding domains of human lysyl aminoacyl tRNA synthetase." University of Cincinnati / OhioLINK, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1353343207.

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Learmont, Jessica. "Prion-like properties of the N-terminal domains of the rat and human FoxG1 transcription factors." Master's thesis, University of Cape Town, 2006. http://hdl.handle.net/11427/4285.

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Word processed copy.<br>Includes bibliographical references (leaves 82-90).<br>The purpose of this study was to investigate the possible prion-like properties of the N-terminal domains of the winged-helix transcription factor FoxG1.

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Khan, Samir Ali. "Structure-function relationships between N-terminal domains of inositol 1, 4, 5-trisphosphate receptors and ryanodine receptors." Thesis, University of Cambridge, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.609991.

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Moriarty, Tara J. "Regulation of telomerase-specific catalytic functions by nucleic acid interactions and human telomerase reverse transcriptase N-terminal domains." Thesis, McGill University, 2005. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=85628.

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Telomerase is an unusual reverse transcriptase (RT) that catalyzes the de novo addition of telomeric DNA repeats to telomeres. Telomerase activity counteracts the progressive loss of telomeric DNA over successive rounds of DNA replication, and is important for the immortality of most eukaryotic cells. Telomerase is distinct from other RTs in that its catalytic subunit (TERT: telomerase reverse transcriptase) stably associates with a telomerase RNA (TR) component that contains a short template used to direct synthesis of telomeric repeats. Telomerase also exhibits a unique, repeat additi

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Books on the topic "N-terminal domains"

1

Wojtyra, Urszula A. Characterization of the N-terminal domain of the molecular chaperone Clpx. National Library of Canada, 2003.

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2

Tsay, Mike J. Expression, purification and characterization of the LEC-rat n-terminal metal binding domain from Atp7b, an orthologue to ATP7B, a copper transporting P-type ATPase implicated in Wilson disease. National Library of Canada, 2001.

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3

Nagar, Bhushan. X=ray crystallographic analysis of 1) the two N-terminal domains of epithelial cadherin and 2) C3d, a fragment of the complement protein C3. 2001.

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Wetzel, Ronald, and Rakesh Mishra. Structural Biology. Oxford University Press, 2014. http://dx.doi.org/10.1093/med/9780199929146.003.0012.

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The 3,144–amino acid huntingtin protein (HTT) folds in water into a structure consisting of compact, organized domains interspersed with intrinsically disordered protein (IDP) elements. The IDPs function as sites of post-translational modifications and proteolysis as well as in targeting, binding, and aggregation. Although the dominant structural motif of HTT is the α‎-helix–rich HEAT repeat, the expanded polyglutamine (polyQ) toxicity responsible for Huntington’s disease is most likely played out within intrinsically disordered HTT exon 1–like fragments consisting of the 16– to 17–amino acid

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Book chapters on the topic "N-terminal domains"

1

Takatori, Sho, and Taisuke Tomita. "AP180 N-Terminal Homology (ANTH) and Epsin N-Terminal Homology (ENTH) Domains: Physiological Functions and Involvement in Disease." In Protein Reviews – Purinergic Receptors. Springer International Publishing, 2018. http://dx.doi.org/10.1007/5584_2018_218.

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Sciotti, Michel-Angelo, Christian Chatenay-Rivauday, Innocent Yamodo, and Joëlle Ogier. "The N-Terminal Half Part of the Oral Streptococcal Antigen I/IIf Contains Two Distinct Functional Domains." In Streptococci and the Host. Springer US, 1997. http://dx.doi.org/10.1007/978-1-4899-1825-3_163.

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Makarov, Valentin V., Michael E. Taliansky, Eugeny N. Dobrov, and Natalia O. Kalinina. "N-Terminal Extension Region of Hordeivirus Movement TGB1 Protein Consists of Two Domains with Different Content of Disordered Structure." In Flexible Viruses. John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9781118135570.ch17.

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4

Raguse, Tami L., Steven C. Pomerantz, Jennifer F. Nemeth, et al. "Chemical Synthesis of the N-Terminal Cysteine-Rich Domain of Human OX40." In Advances in Experimental Medicine and Biology. Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-73657-0_66.

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Mayo, K. H. "Segmental Motion at the N-Terminal Structural Domain in Epidermal Growth Factor." In Proceedings in Life Sciences. Springer New York, 1987. http://dx.doi.org/10.1007/978-1-4612-4796-8_44.

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Trapman, Jan. "Interaction of the Androgen Receptor Ligand-Binding Domain with the N-Terminal Domain and with Coactivators." In Androgen Action in Prostate Cancer. Springer US, 2009. http://dx.doi.org/10.1007/978-0-387-69179-4_16.

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Sakuraba, Yasuhito, Akihiro Yamasato, Ryouichi Tanaka, and Ayumi Tanaka. "Analysis of the N-Terminal Domain of Chlorophyllide a Oxygenase by Random Mutagenesis." In Photosynthesis. Energy from the Sun. Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6709-9_228.

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Ruvo, Menotti, Sandro De Falco, Antonio Verdoliva, Angela Scarallo, and Giorgio Fassina. "N-terminal myristoylation of HBV Pre-S1 domain affects folding and receptor recognition." In Peptides Frontiers of Peptide Science. Springer Netherlands, 2002. http://dx.doi.org/10.1007/0-306-46862-x_231.

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Luo, Jing-chu, Paul P. Bates, and Michael J. E. Sternberg. "Knowledge-based computer modelling for the N-terminal domain of carcinoembryonic antigen(CEA)." In Peptides. Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-010-9066-7_34.

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Cooper, Christopher D. O., and Brian D. Marsden. "N- and C-Terminal Truncations to Enhance Protein Solubility and Crystallization: Predicting Protein Domain Boundaries with Bioinformatics Tools." In Methods in Molecular Biology. Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6887-9_2.

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Conference papers on the topic "N-terminal domains"

1

Brown, David W., and Enoch W. Small. "Rotational diffusion of nucleosomes: role of the N-terminal histone domains in structural transitions." In OE/LASE '92, edited by Joseph R. Lakowicz. SPIE, 1992. http://dx.doi.org/10.1117/12.58276.

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Beneckv, M. J., C. G. Kolvenbach, D. L. Amrani, and M. W. Mosesson. "EVIDENCE THAT THE C-TERMINAL HEPARIN BINDING DOMAIN ("HEP II") DOMINATES HEPARIN-FIBRONECTIN INTERACTIONS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643631.

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The interaction of glycosaminoglycans with plasma fibronectin (PFn) may play a role in the conversion of PFn from an “inert” dimeric circulating form to an “activated” multimeric form deposited on the cell surface or in the extracellular matrix. We carried out a quantitative comparison of heparin affinity for PFn and its proteolytic fragments in order to assess the relative importance of heparin interactions with PFn’s various reported heparin-binding domains. We employed affinity chromatography on PFn-sepharose to prepare a subset of fluorescein-labelled heparin molecules with high affinity f

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3

Takahashi, Y., J. P. Girma, M. Kalafatis, K. Sewerin, L. O. Andersson, and D. Meyer. "LOCALIZATION OF A FACTOR VIII BINDING DOMAIN ON THE N-TERMINAL PORTION (FRAGMENT SpIII) OF VON WILLEBRAND FACTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642876.

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A new domain has been identified on the von Willebrand Factor (vWF) subunit. vWF binds to platelet glycoproteins GPIb and GPIIb/IIIa as well as to collagen and corresponding domains have been isolated. vWF also binds to Factor VIII (F.VIII). We show here that the corresponding domain is located on the N-terminal portion of the vWF subunit (residues 1 to 1,365). For this purpose, F.VIII was tested for its ability to bind to purified vWF degradation fragments obtained by digestion with S.aureus V-8 protease, ie a dimeric N-terminal fragment of 320 kd (SpIII) and a dimeric C-terminal fragment of

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Butler-Zimrin, A. E., J. S. Bennett, M. Poncz, et al. "ISOLATION AND CHARACTERIZATION OF cDNA CLONES FOR THE PLATELET MEMBRANE GLYCOPROTEINS IIb and IIIa." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643961.

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The platelet membrane GPIIb/GPIIIa complex on activated platelets contains receptors for fibrinogen, von Willebrand factor, and fibronectin. GPIIb and GPIlia also appear to be members of a family of membrane receptors involved in cell-cell and cell-matrix interactions. To study the structure of GPIIb and GPIIIa, we have constructed an expression library in the vector lambda gtll using mRNA from the HEL cell line and screened it with polyclonal antibody against each platelet protein. HEL cells constitutively express proteins similar to platelet GPIIb and GPIIIa. A 3.2kb GPIIb cDNA clone was ide

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Hantgan, R. R. "LOCALIZATION OF THE DOMAINS OF FIBRIN INVOLVED IN BINDING TO PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643773.

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The molecular basis of platelet-fibrin interactions has been investigated by using synthetic peptides as potential inhibitors of binding fibrin protofibrils and fibrinogen to ADP-stimulated platelets, adhesion of fibrin fibers to the platelet surface, and platelet-mediated clot retraction. Synthetic peptides RGDS and HHLGGAKQAGDV, corresponding to regions of the fibrinogen α and γ chains previously identified as platelet recognition sites, inhibited the binding of radiolabelled soluble fibrin oligomers to ADP-stimulated platelets with IC50 values of 12 and 40 μM, respectively. The IC50 values

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Günzler, W. A., B. Wolf, and L. Flohé. "CHARACTERIZATION OF RECOMBINANT HUMAN SINGLE-CHAIN LOW MOLECULAR WEIGHT UROKINASE (RE-SC-LUK)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643602.

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RE-SC-LUK obtained from recomoinant b. con Bacteria showed a molecular mass similar to that of recombinant two-chain LUK (RE-TC-LUK) as judged from SDS-PAGE. By “Western“ blot analysis immunoreactivity of RE-SC-LUK was observed with monoclonal antibodies directed against the B chain but not with those against the A1 chain of urokinase. N-terminal sequence analysis c RE-SC-LUK showed identity to the A, chain of RE-TC_LUK and provided evidence for its single-chain nature, i.e. integrity of the Lys-Ile bond which is split in TC-UK. In all other respects structural identity of RE-SC-LUK and RE-TC-

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Kalyan, N. K., S. G. Lee, W.-T. Hum, R. Hartzell, M. Levner, and P. P. Hung. "IN VITRO STUDIES ON THE BINDING OF TISSUE-TYPE PLASMINOGEN ACTIVATOR (t-PA) AND UROKINASE (u-PA) TO LIVER MEMBRANES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643603.

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The plasminogen activators, t-PA and u-PA, are glycoproteins known to be involved in homeostasis of the blood clotting system, and thus are of potential clinical use in the treatment of thrombosis. Several in vivo studies have shown that both t-PA and u-PA are quickly removed from the blood circulation, predominantly by the liver. The mechanism by which the liver removes these proteins is not understood. To delineate this, we conducted in vitro studies of binding of PAs or their derivatives to isolated mouse liver membranes utilizing a functional assay developed in our laboratory. The assay co

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Cambier, P., F. van de werf, and D. collen. "CORONARY THROMBOLYSIS IN DOGS WITH A NONGLYCOSYLATED VARIANT OF HUMAN TISSUE-TYPE PLASMINOGEN ACTIVATOR LACKING THE FINGER AND GROWTH FACTOR DOMAINS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643794.

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A variant of human tissue-type plasminogen activator (t-PA-AΔFE3X), with deletion of the NH2-terminal fibronectin-like finger (F) and epidermal growth factor (E) domains, and with amino acid substitution of Gin for Asn at all known N-linked glycosylation sites was expressed in Chinese Hamster Ovary Cells and purified to homogeneity. The thrombolytic and pharmacokinetic properties of this variant were studied in a canine model with copper coil induced thrombosis of the left anterior descending coronary artery. Infusion of t PAΔFE3X at a rate of 5 pg/kg/min for 30 min in 3 dogs resulted in a pla

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Dahiback, Bjorn, Ake Lundwall, Andreas Hillarp, Johan Malm, and Johan Stenflo. "STRUCTURE AND FUNCTION OF VITAMIN K-DEPENDENT PROTEIN S, a cofactor to activated protein C which also interacts with the complement protein C4b-binding protein." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642960.

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Protein S is a single chain (Mr 75.000) plasma protein. It is a cofactor to activated protein C (APC) in the regulation of coagulation factors Va and Villa. It has high affinity for negatively charged phospolipids and it forms a 1:1 complex with APC on phospholipid surfaces, platelets and on endothelial cells. Patients with heterozygous protein S deficiency have a high incidence of thrombosis. Protein S is cleaved by thrombin, which leads to a loss of calcium binding sites and of APC cofactor activity. Protein S has two to three high affinity (KD 20uM) calcium binding sites - unrelated to the

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Grau, E., and L. A. Moroz. "FIBRINOLYTIC ACTIVITY (FA) OF NORMAL HUMAN PERIPHERAL BLOOD MONOCYTES (MC)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644383.

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FA of blood encompasses a large cellular phase in addition to a fluid (plasma) phase. Polymorphonuclear neutrophils (PMN) have been implicated in this cellular activity, and MC have demonstrated fibrinolytic potential. Using a solid phase radiofibrin assay, we have examined FA of normal blood and plasma, and of purified PMN and MC alone, and with purified plasminogen (PLG), mini-plasminogen (mPLG) produced by gMN elastase digestion, or autologous plasma. PMN alone (0.5 x 106/mL) had striking activity (292 ± 25 SEM ng fibrin lysed/h), (n=10 normal subjects) while MC alone (0.5 x 106/ml) had mea

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Reports on the topic "N-terminal domains"

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Rogers, Aaron. Translational Fidelity of a Eukaryotic Glutaminyl-tRNA Synthetase with an N-terminal Domain Appendage. Portland State University Library, 2000. http://dx.doi.org/10.15760/etd.2005.

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