Matches in SemOpenAlex for { <https://semopenalex.org/work/W2077126871> ?p ?o ?g. }
Showing items 1 to 70 of
70
with 100 items per page.
- W2077126871 endingPage "620" @default.
- W2077126871 startingPage "610" @default.
- W2077126871 abstract "Annals of the New York Academy of SciencesVolume 408, Issue 1 p. 610-620 BINDING OF SOLUBLE FIBRIN TO MACROPHAGES Laurence A. Sherman, Laurence A. Sherman Division of Laboratory Medicine Departments of Pathology and Medicine Washington University School of Medicine St. Louis, MissouriSearch for more papers by this author Laurence A. Sherman, Laurence A. Sherman Division of Laboratory Medicine Departments of Pathology and Medicine Washington University School of Medicine St. Louis, MissouriSearch for more papers by this author First published: June 1983 https://doi.org/10.1111/j.1749-6632.1983.tb23278.xCitations: 6AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL REFERENCES 1 Lewis, J. R. & I. L. F. Szeto. 1965. Clearance of infused fibrin transport. Fed. Proc. 24: 840. 2 Gans, H. & J. R. Lowman. 1967. The uptake of fibrin and fibrin-degradation products by the isolated perfused rat liver. Blood 29: 526. 3 Glueck, H. I. & L. G. Herrmann. 1964. Cold-precipitable fibrinogen, cryofibrinogen. Arch. Intern. Med. 113: 748– 757. 4 Mc Kee, P. A., J. M. Kalbfleisch & R. M. Bird. 1963. Incidence and significance of cryofibrinogenemia. J. Lab. Clin. Med. 61: 203. 5 Smith, R. T. & R. W. von Korff. 1957. Heparin precipitable fraction of human plasma. I. Isolation and characterization of fraction. J. Clin. Invest. 36: 596. 6 Kierulf, P. 1973. Studies on soluble fibrin in plasma. II. N-terminal analysis of a modified fraction I (Cohn) from patient plasmas. Scand. J. Clin. Lab. Invest. 31: 37. 7 Lipinska, B. & K. Worowski. 1968. Detection of soluble fibrin monomer complexes in blood by means of protamine sulfate test. Thromb. Diath. Haemostas. 20: 44. 8 Shainoff, J. R. & I. H. Page. 1962. Significance of cryoprofibrin in fibrinogenfibrin conversion. J. Exp. Med. 116: 687. 9 Sherman, L. A. 1972. Fibrinogen turnover: Demonstration of multiple pathways of catabolism. J. Lab. Clin. Med. 79: 710. 10 Wegrzynowicz, A., M. Kopec & Z. S. Latallo. 1971. Formation of soluble fibrin complexes and some factors affecting their solubility. Scand. J. Haematol. 13: 49. 11 Fletcher, A. P., H. Alkjaersig, J. O'Brien, et al. 1970. Blood hypercoagulability and thrombosis. Trans. Assoc. Am. Physicians 83: 159. 12 Bang, N. U., M. S. Hansen, G. F. Smith, et al. 1973. Properties of soluble fibrin polymers encountered in thrombotic states. In Present Status of Thrombosis. R. Losito, Ed.: 75. F. K. Schattauer Verlag. New York . 13 Sherman, L. A., S. Harwig & J. Lee. 1975. In vitro formation and biological fate of fibrinogen:fibrin complexes. J. Lab. Clin. Med. 86: 100. 14 Muller-Berghaus, G., I. Mahn, G. Koveker & F.-D. Maul. 1976. In vivo behavior of homologous urea-soluble 131I-fibrinogen in rabbits: The effect of fibrinolysis inhibition. Brit. J. Haematol. 33: 61. 15 Chang, M. L. & N. U. Bang. 1977. Biological behavior of higher molecular weight products of fibrinolysis. J. Lab. Clin. Med. 90: 216. 16 von Hugo, R., R. Hafer, B. Stein, et al. 1977. Incorporation of 125I-fibrinogen in circulating soluble fibrin monomer complexes during hypercoagulability. Thrombos. Res. 10: 703. 17 Sherman, L. A. & J. Lee. 1982. Fibronectin: Blood turnovers in normal animals and during intravascular coagulation. Blood 80: 558. 18 Colvin, R. B. & H. F. Dvorak. 1975. Fibrinogen/fibrin on the surface of macrophages: Detection, distribution, binding requirements, and possible role in macrophage adherence phenomena. J. Exp. Med. 142: 1377. 19 Sherman, L. A. & J. Lee. 1977. Specific binding of soluble fibrin to macrophages. J. Exp. Med. 145: 76. 20 Bang, N. U., M. L. Chang, L. E. Mattler et al. 1981. Monocyte/macrophage-mediated catabolism of fibrinogen and fibrin. Ann. N.Y. Acad. Sci. 370: 568. 21 Gonda, S. R. & J. R. Shainoff. 1982. Absorptive endocytosis of fibrin monomer by macrophages; Evidence of a receptor for the amino terminus of the fibrin α-chain. Proc. Natl. Acad. Sci. USA 79: 4565. 22 Esnouf, M. P. & R. Marshall. 1968. The effect of blockade of the reticuloendothelial system and of hypotension on the response of dogs to Ancitrodon rhodostoma venom. Clin. Sci. 35: 261. 23 Jilik, F. & H. Hormann. 1978. Fibronectin (cold-insoluble globulin), V[1] mediation of fibrin-monomer binding to macrophages. In Hoppe-Seyler's Physiol. Chem. 358: 1603. 24 Sherman, L. A., J. Lee & A. Jacobson. 1977. Quantitation of the reticuloendothelial system clearance of soluble fibrin. Brit. J. Haematol. 37: 231. 25 Muller-Berghaus, G., T. Eckhardt & W. Kramer. 1974. The role of leukocytes and platelets in the precipitation of fibrin in vivo: Mechanisms of the generation of microclots from soluble fibrin. Thrombos. Res. 4: 895. 26 Lipinski, B., A. Nowak & V. Gurewich. 1974. The organ distribution of 125I-fibrin in the generalized Shwartzman reaction and its relation to leucocytes. Brit. J. Haematol. 28: 221. 27 Unkeless, J. C., S. Gordon & E. Reich. 1974. Secretion of plasminogen activator by stimulated macrophages. J. Exp. Med. 139: 834. 28 Sherman, L. A., J. Lee & C. Stewart. 1981. Release of fibrinolytic enzymes from macrophages in response to soluble fibrin. J. Reticuloend. Soc. 30: 317. 29 Banda, M. J. & Z. Werb. 1980. The role of macrophage elastase in the proteolysis of fibrinogen, plasminogen, and fibronectin. Fed. Proc. 39: 1756. (abstract). 30 Plow, E. F. & T. S. Edgington. 1975. An alternative pathway for fibrinolysis. I. The cleavage of fibrinogen by leukocyte proteases at physiologic pH. J. Clin. Invest. 56: 30. 31 Plow, E. F. 1982. Leukocyte elastase release during blood coagulation. A potential mechanism for activation of the alternative fibrinolytic pathway. J. Clin. Invest. 59: 564. 32 Kopec, M., K. Bykowska, K. Lopaciuk, et al. 1980. Effects of neutral proteases from human leukocytes on structure and biological properties of human Factor VIII. Thromb. Haemostas. 43: 211. 33 Morland, B. & J. Morland. 1978. Selective induction of lysosomal enzyme activities in mouse peritoneal macrophages. J. Reticuloendothel. Soc. 23: 469. 34 Snedeker, P. W., J. E. Kaplan & T. M. Saba. 1978. Effect of traumatic shock and alteration of reticuloendothelial function on the vascular clearance of soluble fibrin. Physiologist 21: 113. Citing Literature Volume408, Issue1Molecular Biology of Fibrinogen and FibrinJune 1983Pages 610-620 ReferencesRelatedInformation" @default.
- W2077126871 created "2016-06-24" @default.
- W2077126871 creator A5080774353 @default.
- W2077126871 date "1983-06-01" @default.
- W2077126871 modified "2023-09-26" @default.
- W2077126871 title "BINDING OF SOLUBLE FIBRIN TO MACROPHAGES" @default.
- W2077126871 cites W1529214549 @default.
- W2077126871 cites W1970577919 @default.
- W2077126871 cites W1995632373 @default.
- W2077126871 cites W2022723958 @default.
- W2077126871 cites W2028381044 @default.
- W2077126871 cites W2052457763 @default.
- W2077126871 cites W2067349895 @default.
- W2077126871 cites W2087409367 @default.
- W2077126871 cites W2089011674 @default.
- W2077126871 cites W2100898244 @default.
- W2077126871 cites W2109095941 @default.
- W2077126871 cites W2123708308 @default.
- W2077126871 cites W2128680871 @default.
- W2077126871 cites W2130190460 @default.
- W2077126871 cites W2143979495 @default.
- W2077126871 cites W2145780410 @default.
- W2077126871 cites W2394741803 @default.
- W2077126871 cites W2416585194 @default.
- W2077126871 cites W29667720 @default.
- W2077126871 cites W92489547 @default.
- W2077126871 doi "https://doi.org/10.1111/j.1749-6632.1983.tb23278.x" @default.
- W2077126871 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/6575704" @default.
- W2077126871 hasPublicationYear "1983" @default.
- W2077126871 type Work @default.
- W2077126871 sameAs 2077126871 @default.
- W2077126871 citedByCount "7" @default.
- W2077126871 crossrefType "journal-article" @default.
- W2077126871 hasAuthorship W2077126871A5080774353 @default.
- W2077126871 hasConcept C12554922 @default.
- W2077126871 hasConcept C185592680 @default.
- W2077126871 hasConcept C203014093 @default.
- W2077126871 hasConcept C54173615 @default.
- W2077126871 hasConcept C55493867 @default.
- W2077126871 hasConcept C71924100 @default.
- W2077126871 hasConcept C86803240 @default.
- W2077126871 hasConceptScore W2077126871C12554922 @default.
- W2077126871 hasConceptScore W2077126871C185592680 @default.
- W2077126871 hasConceptScore W2077126871C203014093 @default.
- W2077126871 hasConceptScore W2077126871C54173615 @default.
- W2077126871 hasConceptScore W2077126871C55493867 @default.
- W2077126871 hasConceptScore W2077126871C71924100 @default.
- W2077126871 hasConceptScore W2077126871C86803240 @default.
- W2077126871 hasIssue "1 Molecular Bio" @default.
- W2077126871 hasLocation W20771268711 @default.
- W2077126871 hasLocation W20771268712 @default.
- W2077126871 hasOpenAccess W2077126871 @default.
- W2077126871 hasPrimaryLocation W20771268711 @default.
- W2077126871 hasRelatedWork W1543804368 @default.
- W2077126871 hasRelatedWork W1711208506 @default.
- W2077126871 hasRelatedWork W1970454941 @default.
- W2077126871 hasRelatedWork W1976401919 @default.
- W2077126871 hasRelatedWork W2033799196 @default.
- W2077126871 hasRelatedWork W2049718692 @default.
- W2077126871 hasRelatedWork W2076058780 @default.
- W2077126871 hasRelatedWork W2884004647 @default.
- W2077126871 hasRelatedWork W2895997225 @default.
- W2077126871 hasRelatedWork W4243317180 @default.
- W2077126871 hasVolume "408" @default.
- W2077126871 isParatext "false" @default.
- W2077126871 isRetracted "false" @default.
- W2077126871 magId "2077126871" @default.
- W2077126871 workType "article" @default.