FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2025669021> ?p ?o ?g. }

• W2025669021 endingPage "145" @default.
• W2025669021 startingPage "131" @default.
• W2025669021 abstract "Annals of the New York Academy of SciencesVolume 408, Issue 1 p. 131-145 ELECTRON MICROSCOPIC STUDIES OF FIBRINOGEN STRUCTURE: HISTORICAL PERSPECTIVES AND RECENT EXPERIMENTS* Henry S. Slayter, Henry S. Slayter Sidney Farber Cancer Institute and Department of Physiology and Biophysics Harvard Medical School Boston, Massachusetts 02115Search for more papers by this author Henry S. Slayter, Henry S. Slayter Sidney Farber Cancer Institute and Department of Physiology and Biophysics Harvard Medical School Boston, Massachusetts 02115Search for more papers by this author First published: June 1983 https://doi.org/10.1111/j.1749-6632.1983.tb23241.xCitations: 35 * This work was supported by Research Grants GM 14237 from the National Institute of General Medical Sciences and FR 05526 from the Division of Research Facilities and Resources, National Institutes of Health. AboutPDF 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 Bachman, L., W. W. Schmitt-Fumian, R. Hammel & K. Lederer. 1975. Die Makromol. Chem. 176: 2603– 2618. 2 Blakely, P. R., M. J. Groom & R. L. Turner. 1977. Br. J. Haematol. 35: 437– 440. 3 Budzynski, A. Z., M. Stahl, M. Kopec, Z. S. Latatto, Z. Wegrzynowicz & E. Kowalski. 1967. Biochim. Biophys. Acta 147: 313– 323. 4 Cohen, C., H. S. Slayter, L. G. Goldstein, J. Kucera & C. E. Hall. 1966. J. Mol. Biol. 22: 385– 388. 5 Conio, G., G. Dondero, C. Troglia, V. Trefletti & E. Patrone. 1975. Biopolymers 14: 2363– 2372. 6 Donovan, J. W. & E. Mihalyi. 1974. Proc. Natl. Acad. Sci. USA 71: 4125– 4128. 7 Doolittle, R. F. 1973. In Advances in Protein Chemistry. C. B. Anfinsen, Ed. 27: 1– 109. Academic Press. New York . 8 Doolittle, R. F. 1975. In The Plasma Proteins. F. W. Putnam, Ed. 2: 109– 161. Academic Press. New York . 9 Doolittle, R. F., D. M. Goldbaum & L. R. Doolittle. 1978. J. Mol. Biol. 120: 311– 325. 10 Fowler, W. E. & H. P. Erickson. 1979. J. Mol. Biol. 134: 241– 249. 11 Gaffney, P. J. 1977. In Hemostasis: Biochemistry, Physiology and Pathology. D. Ogsten & B. Bennett, Eds.: 105– 169. John Wiley. New York . 12 Gorman, R. R., G. E. Stoner & A. Catlin. 1971. J. Phys. Chem. 75: 2103– 2107. 13 Hall, C. E. & H. S. Slayter. 1959b. J. Biophys. Biochem. Cytol. 5: 11– 17. 14 Hall, C. E. & H. S. Slayter. 1962. In Fifth Int. Cong. for Electron Microscopy. S. S. Breese, Ed. 1: 31– 32. Academic Press. New York . 15 Koppel, G. 1966. Nature (London) 212: 1608– 1609. 16 Krakow, W., G. F. Endres, B. M. Siegel & H. A. Sheraga. 1972. J. Mol. Biol. 71: 95– 103. 17 Lake, J. A. 1979. In Methods in Enzymology. C. H. Hirs & S. N. Timasheff, Eds. 61: 250– 257. Academic Press. New York . 18 Marder, V. J., N. R. Shulman, W. R. Carroll. 1969. J. Biol. Chem. 244: 2111– 2119. 19 Mills, D. A. & D. C. Triantophyllopoulos. 1969. Arch. Biochem. Biophys. 135: 28– 35. 20 Mosesson, M. W. 1976. Thromb. Res. 8: 737– 744. 21 Mosesson, M. W., N. Alkjaersig, B. Sweet & S. Sherry. 1967. Biochemistry 6: 3279– 3287. 22 Norton, P. & H. S. Slayter. 1981. Proc. Natl. Acad. Sci. USA 78(3): 1661– 1665. 23 Nussenzweig, V., M. Seligmann & P. Grabar. 1961. Ann. Inst. Past. 100: 490– 508. 24 Potuit, L., G. Marcille, H. Suscillon & D. Hollard. 1972. Thromb. Diath. Haemorrhag. 27: 559– 572. 25 Shrager, R. I., E. Mihalyi & D. W. Towne. 1976. Biochemistry 15: 5382– 5386. 26 Slayter, H. S. 1971. In Proceedings, Electron Microscopy Society of America, 29th Annual Meeting. C. J. Arcenaux, Ed. 424– 425. Claitor's. Baton Rouge , LA . 27 Slayter, H. S. 1976. Ultramicroscopy 1: 341– 357. 28 Stewart, G. 1971. Scand. J. Hematol. 13: 63– 67. 29 Tooney, N. M. & C. Cohen. 1977. J. Mol. Biol. 110: 363– 385. 30 Weisel, J. W., G. N. Phillips & C. Cohen. 1981. Nature (London) 289: 263– 267. 31 Price, T. M., D. D. Strong, M. L. Rudee & R. F. Doolittle. 1981. Proc. Natl. Acad. Sci. USA 78: 200– 204. 32 Fowler, W. E., L. J. Fretto, H. P. Erickson & P. A. Mc Kee. 1980. J. Clin. Invest. 66: 50– 56. 33 Estis, L. F. & R. M. Haschemeyer. 1980. Proc. Natl. Acad. Sci. USA 77: 3139– 3143. 34 Mosesson, M. W., J. Hainfeld, J. Wall & R. M. Haschemeyer. 1981. J. Mol. Biol. 153: 695– 718. 35 Rudee, M. L. & T. M. Price. 1981. Ultramicroscopy 7: 193– 196. 36 Williams, R. C. 1981. J. Mol. Biol. 150: 399– 408. 37 Tooney, N. M. & C. Cohen. 1972. Nature (London) 237: 23– 25. 38 Weisel, J. W., S. G. Warren & C. Cohen. 1978. J. Mol. Biol. 126: 159– 183. 39 Weisel, J. W., N. M. Tooney, I. Kaplan, D. Amrani & C. Cohen. 1980. J. Mol. Biol. 143: 329– 334. 40 Scheraga, H. A. & M. Laskowski, Jr.. 1957. Adv. Prot. Chem. 12: 1– 131. 41 Hall, C. E. 1949. J. Am. Chem. Soc. 71: 1138– 1139. 42 Hall, C. E. 1949. J. Biol. Chem. 179: 857– 864. 43 Porter, K. F. & C. V. Z. Hawn. 1949. J. Exp. Med. 90: 225– 232. 44 Mitchel, R. F. 1952. Biochim. Biophys. Acta 9: 430– 442. 45 Siegel, B. M., J. P. Mernan & H. A. Scheraga. 1953. Biochim. Biophys. Acta 11: 329– 336. 46 Hall, C. E. 1956. Proc. Natl. Acad. Sci. USA 42: 801– 806. 47 Mosesson, M. W., J. Escaig & G. Feldman. 1979. Thromb. Hemostasis. 42: 88. 48 Koppel, G. 1967. Z. Zellforsch. Microsk. Anat. 77: 443– 517. 49 Slayter, H. S. 1978. In Principles and Techniques of Electron Microscopy: Biological Applications. M. A. Hayat, Ed. 9: 175– 245. 50 Slayter, H. S. 1962. Ph.D. Thesis, Mass. Inst. of Tech. 1– 267. 51 Williams, R. & R. W. G. Wykoff. 1944. J. Appl. Phys. 15: 712– 716. 52 Muller, H. O. 1942. Kolloid-Z. 99: 6– 28. 53 Doolittle, R. F. 1981. Scientific American 245(6): 126– 135. 54 Hall, C. E. 1955. J. Biophys. Biochem. Cytol. 1: 1– 12. 55 Slayter, H. S. 1981. In Enzymes and Soluble Proteins. J. R. Harris, Ed. 1: 197– 254. Academic Press. London , England . 56 Slayter, H. S. & C. E. Hall. 1964. J. Mol. Biol. 8: 593– 601. 57 Slayter, H. S. 1980. In SEM Inc. O. Johari, Ed. 1: 171– 182. 58 Plow, E. F. & T. S. Edgington. 1982. Seminars in Thrombosis and Hemostasis 8: 36– 56. Citing Literature Volume408, Issue1Molecular Biology of Fibrinogen and FibrinJune 1983Pages 131-145 ReferencesRelatedInformation" @default.
• W2025669021 created "2016-06-24" @default.
• W2025669021 creator A5009454215 @default.
• W2025669021 date "1983-06-01" @default.
• W2025669021 modified "2023-09-25" @default.
• W2025669021 title "ELECTRON MICROSCOPIC STUDIES OF FIBRINOGEN STRUCTURE: HISTORICAL PERSPECTIVES AND RECENT EXPERIMENTS" @default.
• W2025669021 cites W1410342483 @default.
• W2025669021 cites W1507424043 @default.
• W2025669021 cites W1588733323 @default.
• W2025669021 cites W1969089776 @default.
• W2025669021 cites W1969454710 @default.
• W2025669021 cites W1977769473 @default.
• W2025669021 cites W1980900878 @default.
• W2025669021 cites W1988813238 @default.
• W2025669021 cites W1993869344 @default.
• W2025669021 cites W1999981955 @default.
• W2025669021 cites W1999987649 @default.
• W2025669021 cites W2003994921 @default.
• W2025669021 cites W2004903846 @default.
• W2025669021 cites W2006344385 @default.
• W2025669021 cites W200730172 @default.
• W2025669021 cites W2009881077 @default.
• W2025669021 cites W2010730285 @default.
• W2025669021 cites W2011292034 @default.
• W2025669021 cites W2015969025 @default.
• W2025669021 cites W2017214116 @default.
• W2025669021 cites W2030759953 @default.
• W2025669021 cites W2033474964 @default.
• W2025669021 cites W2035353298 @default.
• W2025669021 cites W2051727131 @default.
• W2025669021 cites W2057617747 @default.
• W2025669021 cites W2059407964 @default.
• W2025669021 cites W2070403021 @default.
• W2025669021 cites W2071144173 @default.
• W2025669021 cites W2073233247 @default.
• W2025669021 cites W2077344832 @default.
• W2025669021 cites W2078673427 @default.
• W2025669021 cites W2080874316 @default.
• W2025669021 cites W2082814490 @default.
• W2025669021 cites W2082857339 @default.
• W2025669021 cites W2086632608 @default.
• W2025669021 cites W2088538995 @default.
• W2025669021 cites W2088712842 @default.
• W2025669021 cites W2089175575 @default.
• W2025669021 cites W2091809838 @default.
• W2025669021 cites W2120670813 @default.
• W2025669021 cites W2134080134 @default.
• W2025669021 cites W2160124075 @default.
• W2025669021 cites W2416105133 @default.
• W2025669021 cites W3031737188 @default.
• W2025669021 cites W3036471829 @default.
• W2025669021 cites W4300052337 @default.
• W2025669021 doi "https://doi.org/10.1111/j.1749-6632.1983.tb23241.x" @default.
• W2025669021 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/6223556" @default.
• W2025669021 hasPublicationYear "1983" @default.
• W2025669021 type Work @default.
• W2025669021 sameAs 2025669021 @default.
• W2025669021 citedByCount "43" @default.
• W2025669021 countsByYear W20256690212012 @default.
• W2025669021 countsByYear W20256690212015 @default.
• W2025669021 countsByYear W20256690212017 @default.
• W2025669021 countsByYear W20256690212021 @default.
• W2025669021 crossrefType "journal-article" @default.
• W2025669021 hasAuthorship W2025669021A5009454215 @default.
• W2025669021 hasConcept C121332964 @default.
• W2025669021 hasConcept C147120987 @default.
• W2025669021 hasConcept C185544564 @default.
• W2025669021 hasConcept C185592680 @default.
• W2025669021 hasConcept C192562407 @default.
• W2025669021 hasConcept C2779036427 @default.
• W2025669021 hasConcept C55493867 @default.
• W2025669021 hasConceptScore W2025669021C121332964 @default.
• W2025669021 hasConceptScore W2025669021C147120987 @default.
• W2025669021 hasConceptScore W2025669021C185544564 @default.
• W2025669021 hasConceptScore W2025669021C185592680 @default.
• W2025669021 hasConceptScore W2025669021C192562407 @default.
• W2025669021 hasConceptScore W2025669021C2779036427 @default.
• W2025669021 hasConceptScore W2025669021C55493867 @default.
• W2025669021 hasIssue "1 Molecular Bio" @default.
• W2025669021 hasLocation W20256690211 @default.
• W2025669021 hasLocation W20256690212 @default.
• W2025669021 hasOpenAccess W2025669021 @default.
• W2025669021 hasPrimaryLocation W20256690211 @default.
• W2025669021 hasRelatedWork W1673008620 @default.
• W2025669021 hasRelatedWork W2036427972 @default.
• W2025669021 hasRelatedWork W2069315014 @default.
• W2025669021 hasRelatedWork W2082591874 @default.
• W2025669021 hasRelatedWork W2084289794 @default.
• W2025669021 hasRelatedWork W2086395407 @default.
• W2025669021 hasRelatedWork W2092198327 @default.
• W2025669021 hasRelatedWork W2889997997 @default.
• W2025669021 hasRelatedWork W2899084033 @default.
• W2025669021 hasRelatedWork W69032430 @default.
• W2025669021 hasVolume "408" @default.
• W2025669021 isParatext "false" @default.
• W2025669021 isRetracted "false" @default.
• W2025669021 magId "2025669021" @default.
• W2025669021 workType "article" @default.