So I was at Wikpedia reading about Goliath (because who in hell was Goliath? nobody knows) when I read: “According to the Jerusalem Talmud, Goliath was born by polyspermy, and had about one hundred fathers.” I had to read more because that sounds a little strange. The Polyspermy page took me to the Cortical reaction and Acrosome reaction pages along with several others, some of which are still open and waiting to be read. The H word keeps showing up…a couple of H words keep showing up. I decided to work on “from Transylvania to Woods Hole” guy’s page because WPKOI has new templates I want to try and I also need more information on a few things from that page. One of his things was Vitamin C which was formerly called hexuronic acid. And that got me reading about uronic acid (which is ‘not to be confused with uric acid’):
Uronic acids or alduronic acids are a class of sugar acids with both carbonyl and carboxylic acid functional groups. They are sugars in which the hydroxyl group furthest from the carbonyl group has been oxidized to a carboxylic acid. Usually the sugar is an aldose, but fructuronic acid also occurs. Oxidation of the terminal aldehyde instead yields an aldonic acid, while oxidation of both the terminal hydroxyl group and the aldehyde yields an aldaric acid. The names of uronic acids are generally based on their parent sugars, for example, the uronic acid analog of glucose is glucuronic acid. Uronic acids derived from hexoses are known as hexuronic acids and uronic acids derived from pentoses are known as penturonic acids.[ “Hexuronic acid”. encyclopedia.com.] Some of these compounds have important biochemical functions; for example, many wastes in the human body are excreted in the urine as their glucuronate salts, and iduronic acid is a component of some structural complexes such as proteoglycans.
https://en.wikipedia.org/wiki/Uronic_acid
It was the Iduronic acid which mentioned the study:
l-Iduronic acid (IUPAC abbr.: IdoA) is the major uronic acid component of the glycosaminoglycans (GAGs) dermatan sulfate, and heparin. It is also present in heparan sulfate, although here in a minor amount relative to its carbon-5 epimer glucuronic acid. IdoA is a hexapyranose sugar. Most hexapyranoses are stable in one of two chair conformations 1C4 or 4C1. l-iduronate is different and adopts more than one solution conformation, with an equilibrium existing between three low-energy conformers. These are the 1C4 and 4C1 chair forms and an additional 2S0 skew-boat conformation. IdoA may be modified by the addition of an O-sulfate group at carbon position 2 to form 2-O-sulfo-l-iduronic acid (IdoA2S). In 2000, LK Hallak described the importance of this sugar in respiratory syncytial virus (RSV) infection. Dermatan sulfate and heparan sulfate were the only GAGs containing IdoA, and they were the only ones that inhibited RSV infection in cell culture. When internally positioned within an oligosaccharide, the 1C4 and 2S0 conformations (shown at Wikipedia) predominate. Proton NMR spectroscopy can be used to track changes in the balance of this equilibrium.
https://en.wikipedia.org/wiki/Iduronic_acid
That’s all very interesting. I also just read that something called Protamine sulfate “is a medication that is used to reverse the effects of heparin” and “Protamine has been reported to cause allergic reactions in patients who are allergic to fish, diabetics using insulin preparations containing protamine, and vasectomized or infertile men.“ What on earth? I don’t have time to visit the rabbit hole anytime soon so I want to make a note of it.
Here is the abstract for the title study and I’m including the references because I’ve been seeing some of this stuff way too many times. I guess we’re going to figure out why that is…and what, if anything, this has to do with Goliath. So weird.
Abstract
Respiratory syncytial virus (RSV) is an important human respiratory pathogen, particularly in infants. Glycosaminoglycans (GAGs) have been implicated in the initiation of RSV infection of cultured cells, but it is not clear what type of GAGs and GAG components are involved, whether the important GAGs are on the virus or the cell, or what the magnitude is of their contribution to infection. We constructed and rescued a recombinant green fluorescent protein (GFP)-expressing RSV (rgRSV) and used this virus to develop a sensitive system to assess and quantify infection by flow cytometry. Evaluation of a panel of mutant Chinese hamster ovary cell lines that are genetically deficient in various aspects of GAG synthesis showed that infection was reduced up to 80% depending on the type of GAG deficiency. Enzymatic removal of heparan sulfate and/or chondroitin sulfate from the surface of HEp-2 cells also reduced infection, and the removal of both reduced infection even further. Blocking experiments in which RSV was preincubated with various soluble GAGs revealed the relative blocking order of: heparin > heparan sulfate > chondroitin sulfate B. Iduronic acid is a component common to these GAGs. GAGs that do not contain iduronic acid, namely, chondroitin sulfate A and C and hyaluronic acid, did not inhibit infection. A role for iduronic acid-containing GAGs in RSV infection was confirmed by the ability of basic fibroblast growth factor to block infection, because basic fibroblast growth factor binds to GAGs containing iduronic acid. Pretreatment of cells with protamine sulfate, which binds and blocks GAGs, also reduced infection. In these examples, infection was reduced by pretreatment of the virus with soluble GAGs, pretreatment of the cells with GAG-binding molecules, pretreatment of the cells with GAG-destroying enzymes or in cells genetically deficient in GAGs. These results establish that the GAGs involved in RSV infection are present on the cell rather than on the virus particle. Thus, the presence of cell surface GAGs containing iduronic acid, like heparan sulfate and chondroitin sulfate B, is required for efficient RSV infection in cell culture.
Hallak LK, Collins PL, Knudson W, Peeples ME. Iduronic acid-containing glycosaminoglycans on target cells are required for efficient respiratory syncytial virus infection. Virology. 2000 Jun 5;271(2):264-75. doi: 10.1006/viro.2000.0293. PMID: 10860881
REFERENCES
- G. Backstrom, M. Hook, U. Lindahl, D.S. Feingold, A. Malmstrom, L. Roden, I. JacobssonBiosynthesis of heparin: Assay and properties of the microsomal uronosyl C-5 epimeraseJ. Biol. Chem., 254 (1979), pp. 2975-2982 View PDF View article Google Scholar
- D.C. Baulcombe, S. Chapman, C.S. SantaJellyfish green fluorescent protein as a reporter for virus infectionsPlant J., 7 (1995), pp. 1045-1053 View PDF This article is free to access.View in Scopus Google Scholar
- C.L. Borders Jr., M.A. RafteryPurification and partial characterization of testicular hyaluronidaseJ. Biol. Chem., 243 (1968), pp. 3756-3762View PDFView articleView in ScopusGoogle Scholar
- V. Bossennec, M. Petitou, B. Perly1H-n.m.r. investigation of naturally occurring and chemically oversulphated dermatan sulphates. Identification of minor monosaccharide residuesBiochem. J., 267 (1990), pp. 625-630View article CrossRefView in ScopusGoogle Scholar
- M.A. Bourdon, T. Krusius, S. Campbell, N.B. Schwartz, E. RuoslahtiIdentification and synthesis of a recognition signal for the attachment of glycosaminoglycans to proteinsProc. Natl. Acad. Sci. USA, 84 (1987), pp. 3194-3198View article CrossRefView in ScopusGoogle Scholar
- C. Bourgeois, J.B. Bour, K. Lidholt, C. Gauthray, P. PothierHeparin-like structures on respiratory syncytial virus are involved in its infectivity in vitroJ. Virol., 72 (1998), pp. 7221-7227 View PDF This article is free to access.CrossRefView in ScopusGoogle Scholar
- A.P. Byrnes, D.E. GriffinBinding of Sindbis virus to cell surface heparan sulfateJ. Virol., 72 (1998), pp. 7349-7356 View PDF This article is free to access.CrossRefView in ScopusGoogle Scholar
- Y. Byun, V.K. Singh, V.C. YangLow molecular weight protamine: A potential nontoxic heparin antagonistThromb. Res., 94 (1999), pp. 53-61View PDFView articleView in ScopusGoogle Scholar
- B. Casu, M. Petitou, M. Provasoli, P. SinayConformational flexibility: A new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycansTrends Biochem. Sci., 13 (1988), pp. 221-225View PDFView articleView in ScopusGoogle Scholar
- P.C. Champe, R.A. HarveyGlycosaminoglycansD. Barnes, S. Robinson, L.E. Hoeltzel (Eds.), Biochemistry, J. B. Lippincott Company, Philadelphia (1987), pp. 81-89Google Scholar
- Y. Chen, T. Maguire, R.E. Hileman, J.R. Fromm, J.D. Esko, R.J. Linhardt, R.M. MarksDengue virus infectivity depends on envelope protein binding to target cell heparan sulfate [see comments]Nat. Med., 3 (1997), pp. 866-871View in ScopusGoogle Scholar
- S.K. Chintala, R.R. Miller, C.A. McDevittBasic fibroblast growth factor binds to heparan sulfate in the extracellular matrix of rat growth plate chondrocytesArch. Biochem. Biophys., 310 (1994), pp. 180-186View PDFView articleView in ScopusGoogle Scholar
- R.K. Chopra, C.H. Pearson, G.A. Pringle, D.S. Fackre, P.G. ScottDermatan sulphate is located on serine-4 of bovine skin proteodermatan sulphate: Demonstration that most molecules possess only one glycosaminoglycan chain and comparison of amino acid sequences around glycosylation sites in different proteoglycansBiochem. J., 232 (1985), pp. 277-279View article CrossRefView in ScopusGoogle Scholar
- P.L. Collins, M.G. Hill, E. Camargo, H. Grosfeld, R.M. Chanock, B.R. MurphyProduction of infectious human respiratory syncytial virus from cloned cDNA confirms an essential role for the transcription elongation factor from the 5′ proximal open reading frame of the M2 mRNA in gene expression and provides a capability for vaccine developmentProc. Natl. Acad. Sci. USA, 92 (1995), pp. 11563-11567 View article CrossRefView in ScopusGoogle Scholar
- J.D. Esko, C.R. RaetzReplica plating and in situ enzymatic assay of animal cell colonies established on filter paperProc. Natl. Acad. Sci. USA, 75 (1978), pp. 1190-1193 View article CrossRefView in ScopusGoogle Scholar
- J.D. Esko, L. ZhangInfluence of core protein sequence on glycosaminoglycan assemblyCurr. Opin. Struct. Biol., 6 (1996), pp. 663-670 View PDFView articleView in ScopusGoogle Scholar
- J.D. Esko, K.S. Rostand, J.L. WeinkeTumor formation dependent on proteoglycan biosynthesisScience, 241 (1988), pp. 1092-1096 View article CrossRefView in ScopusGoogle Scholar
- J.D. Esko, T.E. Stewart, W.H. TaylorAnimal cell mutants defective in glycosaminoglycan biosynthesisProc. Natl. Acad. Sci. USA, 82 (1985), pp. 3197-3201 View article CrossRef View in Scopus Google Scholar
- J.D. Esko, J.L. Weinke, W.H. Taylor, G. Ekborg, L. Roden, G. Anantharamaiah, A. GawishInhibition of chondroitin and heparan sulfate biosynthesis in Chinese hamster ovary cell mutants defective in galactosyltransferase IJ. Biol. Chem., 262 (1987), pp. 12189-12195 View PDFView articleView in ScopusGoogle Scholar
- S.A. Feldman, R.M. Hendry, J.A. BeelerIdentification of a linear heparin binding domain for human respiratory syncytial virus attachment glycoprotein GJ. Virol., 73 (1999), pp. 6610-6617 View PDF This article is free to access.CrossRef View in Scopus Google Scholar
- E. Forsberg, G. Pejler, M. Ringvall, C. Lunderius, B. Tomasini-Johansson, M. Kusche-Gullberg, I. Eriksson, J. Ledin, L. Hellman, L. KjellenAbnormal mast cells in mice deficient in a heparin-synthesizing enzyme [In Process Citation]Nature, 400 (1999), pp. 773-776 View in ScopusGoogle Scholar
- R. Godavarti, R. SasisekharanHeparinase I from Flavobacterium heparinum: Role of positive charge in enzymatic activityJ. Biol. Chem., 273 (1998), pp. 248-255View PDFView articleView in ScopusGoogle Scholar
- H. Greve, Z. Cully, P. Blumberg, H. KresseInfluence of chlorate on proteoglycan biosynthesis by cultured human fibroblastsJ. Biol. Chem., 263 (1988), pp. 12886-12892View PDFView articleView in ScopusGoogle Scholar
- B.R. Heminway, Y. Yu, Y. Tanaka, K.G. Perrine, E. Gustafson, J.M. Bernstein, M.S. GalinskiAnalysis of respiratory syncytial virus F, G, and SH proteins in cell fusionVirology, 200 (1994), pp. 801-805View PDFView articleView in ScopusGoogle Scholar
- J.C. Hsiao, C.S. Chung, W. ChangCell surface proteoglycans are necessary for A27L protein-mediated cell fusion: Identification of the N-terminal region of A27L protein as the glycosaminoglycan-binding domainJ. Virol., 72 (1998), pp. 8374-8379 View PDF This article is free to access.CrossRefView in ScopusGoogle Scholar
- J.C. Hsiao, C.S. Chung, W. ChangVaccinia virus envelope D8L protein binds to cell surface chondroitin sulfate and mediates the adsorption of intracellular mature virions to cellsJ. Virol., 73 (1999), pp. 8750-8761 View PDF This article is free to access.CrossRefView in ScopusGoogle Scholar
- A.R. Hubbard, C.A. JenningsNeutralisation of heparan sulphate and low molecular weight heparin by protamineThromb. Haemost., 53 (1985), pp. 86-89View in ScopusGoogle Scholar
- T. Jackson, F.M. Ellard, R.A. Ghazaleh, S.M. Brookes, W.E. Blakemore, A.H. Corteyn, D.I. Stuart, J.W. Newman, A.M. King Efficient infection of cells in culture by type O foot-and-mouth disease virus requires binding to cell surface heparan sulfate J. Virol., 70 (1996), pp. 5282-5287 View PDF This article is free to access.CrossRef View in Scopus Google Scholar
- K.G. Jacobsson, U. Lindahl, A.A. HornerLocation of antithrombin-binding regions in rat skin heparin proteoglycansBiochem. J., 240 (1986), pp. 625-632View article CrossRefView in ScopusGoogle Scholar
- P.R. Johnson, M.K. Spriggs, R.A. Olmsted, P.L. CollinsThe G glycoprotein of human respiratory syncytial viruses of subgroups A and B: Extensive sequence divergence between antigenically related proteinsProc. Natl. Acad. Sci. USA, 84 (1987), pp. 5625-5629View article CrossRefView in ScopusGoogle Scholar
- N.K. Karamanos, P. Vanky, A. Syrokou, A. HjerpeIdentity of dermatan and chondroitin sequences in dermatan sulfate chains determined by using fragmentation with chondroitinases and ion- pair high-performance liquid chromatographyAnal. Biochem., 225 (1995), pp. 220-230View PDFView articleView in ScopusGoogle Scholar
- R.A. Karron, D.A. Buonagurio, A.F. Georgiu, S.S. Whitehead, J.E. Adamus, M.L. Clements-Mann, D.O. Harris, V.B. Randolph, S.A. Udem, B.R. Murphy, M.S. SidhuRespiratory syncytial virus (RSV) SH and G proteins are not essential for viral replication in vitro: Clinical evaluation and molecular characterization of a cold-passaged, attenuated RSV subgroup B mutantProc. Natl. Acad. Sci. USA, 94 (1997), pp. 13961-13966View in ScopusGoogle Scholar
- W.B. Klimstra, K.D. Ryman, R.E. JohnstonAdaptation of Sindbis virus to BHK cells selects for use of heparan sulfate as an attachment receptorJ. Virol., 72 (1998), pp. 7357-7366 View PDF This article is free to access.CrossRefView in ScopusGoogle Scholar
- C.B. Knudson, W. KnudsonHyaluronan-binding proteins in development, tissue homeostasis, and diseaseFASEB J., 7 (1993), pp. 1233-1241View article CrossRefView in ScopusGoogle Scholar
- R. Kokenyesi, M. BernfieldCore protein structure and sequence determine the site and presence of heparan sulfate and chondroitin sulfate on syndecan-1J. Biol. Chem., 269 (1994), pp. 12304-12309View PDFView articleView in ScopusGoogle Scholar
- J. Kovensky, P. Duchaussoy, F. Bono, M. Salmivirta, P. Sizun, J.M. Herbert, M. Petitou, P. SinayA synthetic heparan sulfate pentasaccharide, exclusively containing L-iduronic acid, displays higher affinity for FGF-2 than its D-glucuronic acid-containing isomersBioorg. Med. Chem., 7 (1999), pp. 1567-1580View PDFView articleView in ScopusGoogle Scholar
- T. Krusat, H.J. StreckertHeparin-dependent attachment of respiratory syncytial virus (RSV) to host cellsArch. Virol., 142 (1997), pp. 1247-1254View in ScopusGoogle Scholar
- J.P. Langedijk, W.M. Schaaper, R.H. Meloen, J.T. van OirschotProposed three-dimensional model for the attachment protein G of respiratory syncytial virusJ. Gen. Virol., 77 (1996), pp. 1249-1257View article CrossRefView in ScopusGoogle Scholar
- S. Levine, R. Klaiber-Franco, P.R. ParadisoDemonstration that glycoprotein G is the attachment protein of respiratory syncytial virusJ. Gen. Virol., 68 (1987), pp. 2521-2524View article CrossRefView in ScopusGoogle Scholar
- K. Lidholt, J.L. Weinke, C.S. Kiser, F.N. Lugemwa, K.J. Bame, S. Cheifetz, J. Massague, U. Lindahl, J.D. EskoA single mutation affects both N-acetylglucosaminyltransferase and glucuronosyltransferase activities in a Chinese hamster ovary cell mutant defective in heparan sulfate biosynthesisProc. Natl. Acad. Sci. USA, 89 (1992), pp. 2267-2271View article CrossRefView in ScopusGoogle Scholar
- U. LindahlApproaches to the synthesis of heparinHaemostasis, 20 (1990), pp. 146-153View article CrossRefView in ScopusGoogle Scholar
- U. LindahlBiosynthesis of heparinBiochem. Soc. Trans., 18 (1990), pp. 803-805View article CrossRefView in ScopusGoogle Scholar
- U. Lindahl, D.S. Feingold, L. RodenBiosynthesis of heparinTrends Biochem. Sci., 11 (1986), pp. 221-225View PDFView articleView in ScopusGoogle Scholar
- U. Lindahl, M. Kusche, K. Lidholt, L.G. OscarssonBiosynthesis of heparin and heparan sulfateAnn. NY Acad. Sci., 556 (1989), pp. 36-50View article CrossRefView in ScopusGoogle Scholar
- R.J. Linhardt, A. al Hakim, J.A. Liu, D. Hoppensteadt, G. Mascellani, P. Bianchini, J. FareedStructural features of dermatan sulfates and their relationship to anticoagulant and antithrombotic activitiesBiochem. Pharmacol., 42 (1991), pp. 1609-1619View PDFView articleView in ScopusGoogle Scholar
- D.L. Lohse, R.J. LinhardtPurification and characterization of heparin lyases from Flavobacterium heparinumJ. Biol. Chem., 267 (1992), pp. 24347-24355View PDFView articleView in ScopusGoogle Scholar
- V. Lories, H. de Boeck, G. David, J.J. Cassiman, B.H. Van DenHeparan sulfate proteoglycans of human lung fibroblasts: Structural heterogeneity of the core proteins of the hydrophobic cell-associated formsJ. Biol. Chem., 262 (1987), pp. 854-859View PDFView articleView in ScopusGoogle Scholar
- M. Maccarana, Y. Sakura, A. Tawada, K. Yoshida, U. LindahlDomain structure of heparan sulfates from bovine organsJ. Biol. Chem., 271 (1996), pp. 17804-17810View PDFView articleView in ScopusGoogle Scholar
- Y.M. Michelacci, C.P. DietrichA comparative study between a chondroitinase B and a chondroitinase AC from Flavobacterium heparinum: Isolation of a chondroitinase AC- susceptible dodecasaccharide from chondroitin sulphate BBiochem. J., 151 (1975), pp. 121-129View article CrossRefView in ScopusGoogle Scholar
- I. Mondor, S. Ugolini, Q.J. SattentauHuman immunodeficiency virus type 1 attachment to HeLa CD4 cells is CD4 independent and gp120 dependent and requires cell surface heparansJ. Virol., 72 (1998), pp. 3623-3634 View PDF This article is free to access.CrossRefView in ScopusGoogle Scholar
- K. Nackaerts, E. Verbeken, G. Deneffe, B. Vanderschueren, M. Demedts, G. DavidHeparan sulfate proteoglycan expression in human lung-cancer cellsInt. J. Cancer, 74 (1997), pp. 335-345 View PDF This article is free to access.View in ScopusGoogle Scholar
- A.J. Nahmias, S. KibrickInhibitory effect of heparin on herpes simplex virusJ. Bacteriol., 87 (1964), pp. 1060-1066 View PDF This article is free to access.CrossRefView in ScopusGoogle Scholar
- T. Ohya, Y. KanekoNovel hyaluronidase from streptomycesBiochim. Biophys. Acta, 198 (1970), pp. 607-609View PDFView articleView in ScopusGoogle Scholar
- M.K. Pastey, S.K. SamalAnalysis of bovine respiratory syncytial virus envelope glycoproteins in cell fusionJ. Gen. Virol., 78 (1997), pp. 1885-1889View article CrossRefView in ScopusGoogle Scholar
- A.S. PerlinRecent Structural Studies on HeparinN.M. McDuffie (Ed.), Heparin: Structure, Cellular Functions, and Clinical Applications, Academic Press, San Diego (1979), pp. 25-37View PDFView articleGoogle Scholar
- M.W. Piepkorn, D. Lagunoff, G. SchmerHeparin binding to antithrombin III: Variation in binding sites and affinityBiochem. Biophys. Res. Commun., 85 (1978), pp. 851-856View PDFView articleView in ScopusGoogle Scholar
- J. Portelli, A. Gordon, J.T. MayEffect of compounds with antibacterial activities in human milk on respiratory syncytial virus and cytomegalovirus in vitroJ. Med. Microbiol., 47 (1998), pp. 1015-1018View article CrossRefView in ScopusGoogle Scholar
- K. Schmid, J. Grundboeck-Jusco, A. Kimura, F.A. Tschopp, R. Zollinger, J.P. Binette, W. Lewis, S. HayashiThe distribution of the glycosaminoglycans in the anatomic components of the lung and the changes in concentration of these macromolecules during development and agingBiochim. Biophys. Acta, 716 (1982), pp. 178-187View PDFView articleView in ScopusGoogle Scholar
- M.T. Shieh, D. WuDunn, R.I. Montgomery, J.D. Esko, P.G. SpearCell surface receptors for herpes simplex virus are heparan sulfate proteoglycansJ. Cell Biol., 116 (1992), pp. 1273-1281 View PDF This article is free to access.View in ScopusGoogle Scholar
- D. Shukla, J. Liu, P. Blaiklock, N.W. Shworak, X. Bai, J.D. Esko, G.H. Cohen, R.J. Eisenberg, R.D. Rosenberg, P.G. SpearA novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entryCell, 99 (1999), pp. 13-22View PDFView articleView in ScopusGoogle Scholar
- P. Sie, B. Cremers, D. Dupouy, C. Caranobe, F. Dol, B. BoneuNeutralization of dermatan sulfate in vitro and in vivo by protamine sulfate and polybreneThromb. Res., 54 (1989), pp. 63-74View PDFView articleView in ScopusGoogle Scholar
- C.K. Silbert, D.E. Humphries, M.E. Palmer, J.E. SilbertEffects of sulfate deprivation on the production of chondroitin/dermatan sulfate by cultures of skin fibroblasts from normal and diabetic individualsArch. Biochem. Biophys., 285 (1991), pp. 137-141View PDFView articleView in ScopusGoogle Scholar
- P.G. Spear, M.T. Shieh, B.C. Herold, D. WuDunn, T.I. KoshyHeparan sulfate glycosaminoglycans as primary cell surface receptors for herpes simplex virusAdv. Exp. Med. Biol., 313 (1992), pp. 341-353View article CrossRefView in ScopusGoogle Scholar
- S. Suzuki, H. Saito, T. Yamagata, K. Anno, N. Seno, Y. Kawai, T. FuruhashiFormation of three types of disulfated disaccharides from chondroitin sulfates by chondroitinase digestionJ. Biol. Chem., 243 (1968), pp. 1543-1550View PDFView articleView in ScopusGoogle Scholar
- H. Tekotte, M. Engel, R.U. Margolis, R.K. MargolisDisaccharide composition of heparan sulfates: Brain, nervous tissue storage organelles, kidney, and lungJ. Neurochem., 62 (1994), pp. 1126-1130View in ScopusGoogle Scholar
- T. Toida, H. Yoshida, H. Toyoda, I. Koshiishi, T. Imanari, R.E. Hileman, J.R. Fromm, R.J. LinhardtStructural differences and the presence of unsubstituted amino groups in heparan sulphates from different tissues and speciesBiochem. J., 322 (1997), pp. 499-506View article CrossRefView in ScopusGoogle Scholar
- J.E. Turnbull, D.G. Fernig, Y. Ke, M.C. Wilkinson, J.T. GallagherIdentification of the basic fibroblast growth factor binding sequence in fibroblast heparan sulfateJ. Biol. Chem., 267 (1992), pp. 10337-10341View PDFView articleView in ScopusGoogle Scholar
- C. UnderhillCD44: The hyaluronan receptorJ. Cell Sci., 103 (1992), pp. 293-298View article CrossRefView in ScopusGoogle Scholar
- T.H. van Kuppevelt, F.P. Cremers, J.G. Domen, C.M. KuyperStaining of proteoglycans in mouse lung alveoli. II. Characterization of the Cuprolinic blue-positive, anionic sitesHistochem. J., 16 (1984), pp. 671-686View in ScopusGoogle Scholar
- T.H. van Kuppevelt, F.P. Cremers, J.G. Domen, H.M. van Beuningen, A.J. van den Brule, C.M. KuyperUltrastructural localization and characterization of proteoglycans in human lung alveoliEur. J. Cell Biol., 36 (1985), pp. 74-80View in ScopusGoogle Scholar
- E.E. Walsh, J. HruskaMonoclonal antibodies to respiratory syncytial virus proteins: Identification of the fusion proteinJ. Virol., 47 (1983), pp. 171-177 View PDF This article is free to access.CrossRefView in ScopusGoogle Scholar
- A. Walter, L.A. DowningRespiratory syncytial virus interactions with host cell membranes: An enigma among the paramyxoviridaeJ. Bentz (Ed.), Viral Fusion Mechanisms, CRC Press, Inc, Boca Raton (1993), pp. 363-383Google Scholar
- G. Westergren-Thorsson, P.O. Onnervik, L.A. Fransson, A. MalmstromProliferation of cultured fibroblasts is inhibited by L-iduronate- containing glycosaminoglycansJ. Cell. Physiol., 147 (1991), pp. 523-530View article CrossRefView in ScopusGoogle Scholar
- G. Westergren-Thorsson, S. Persson, A. Isaksson, P.O. Onnervik, A. Malmstrom, L.A. FranssonL-iduronate-rich glycosaminoglycans inhibit growth of normal fibroblasts independently of serum or added growth factorsExp. Cell Res., 206 (1993), pp. 93-99View PDFView articleView in ScopusGoogle Scholar
- D.M. Whitfield, J. Choay, B. Sarkar Heavy metal binding to heparin disaccharides. I. Iduronic acid is the main binding site Biopolymers, 32 (1992), pp. 585-596 View article CrossRef View in Scopus Google Scholar
- D. WuDunn, P.G. SpearInitial interaction of herpes simplex virus with cells is binding to heparan sulfateJ. Virol., 63 (1989), pp. 52-58 View PDF This article is free to access.CrossRefView in ScopusGoogle Scholar
- L.S. Wyatt, B. Moss, S. RozenblattReplication-deficient vaccinia virus encoding bacteriophage T7 RNA polymerase for transient gene expression in mammalian cellsVirology, 210 (1995), pp. 202-205View PDFView articleView in ScopusGoogle Scholar
- T. Yamagata, H. Saito, O. Habuchi, S. SuzukiPurification and properties of bacterial chondroitinases and chondrosulfatasesJ. Biol. Chem., 243 (1968), pp. 1523-1535View PDFView articleView in ScopusGoogle Scholar
- L. Zhang, G. David, J.D. EskoRepetitive Ser-Gly sequences enhance heparan sulfate assembly in proteoglycansJ. Biol. Chem., 270 (1995), pp. 27127-27135View PDFView articleView in ScopusGoogle Scholar
- L. Zhang, J.D. EskoAmino acid determinants that drive heparan sulfate assembly in a proteoglycanJ. Biol. Chem., 269 (1994), pp. 19295-19299View PDFView articleView in ScopusGoogle Scholar
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