Protein Composites: Biominerals
Part 8. Polyamides and Complex Proteinaceous Materials
Prof. Emeritus Arthur Veis,
Prof. Emeritus Arthur Veis
- [email protected]
- +1-312-503-1355 | Fax: +1-312-503-2544
Feinberg School of Medicine, Department of Cell and Molecular Biology, Northwestern University, 303 E. Chicago Avenue, Chicago, IL, USA, 60611
Search for more papers by this authorProf. Emeritus Arthur Veis,
Prof. Emeritus Arthur Veis
- [email protected]
- +1-312-503-1355 | Fax: +1-312-503-2544
Feinberg School of Medicine, Department of Cell and Molecular Biology, Northwestern University, 303 E. Chicago Avenue, Chicago, IL, USA, 60611
Search for more papers by this authorFirst published: 15 January 2005
Abstract
- Introduction
- Historical Outline
- Type I Collagen Synthesis and Secretion
- Molecular Structure and Fibril Assembly
- Chemistry of Collagen Crosslinking
- Matrix Mineralization and Organization
- Tooth Enamel
- Invertebrate Mineralization and Organization
- Outlook and Perspectives
- Acknowledgments
References
- Amis, E. J., Carriere, C. J., Ferry, J. D., Veis, A. (1985) Effect of pH on collagen flexibility determined from dilute solution viscosity measurements, Int. J. Biol. Macromol. 7, 130–134.
- Bachinger, H. P., Bruckner, P., Timpl, R., Prockop, D. J., Engel, J. (1980) Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. Role of disulfide bridges and peptide bond isomerization, Eur. J. Biochem. 106, 619–632.
- Bachinger, H. P., Fessler, L. I., Timpl, R., Fessler, J. H. (1981) Chain assembly intermediate in the biosynthesis of type III procollagen in chick embryo blood vessels, J. Biol. Chem. 256, 13193–13199.
- Bank, R. A., Robins, S. P., Wijmenga, C., Breslau-Siderius, L. J., Bardoel, A. F., Van der Sluijs, H. A., Pruijs, H. E., TeKoppele, J. M. (1999) Defective collagen crosslinking in bone, but not in ligament or cartilage, in Bruck syndrome: indications for a bone-specific telopeptide lysylhydroxylase on chromosome 17, Proc. Natl. Acad. Sci. USA 96, 1054–1058.
- Banse, X., Devogelaer, J. P., LaFosse, A., Sims, T. J., Grynpas, M., Bailey, A. J. (2002) Cross-link profile of bone collagen correlates with structural organization of trabeculae, Bone 31, 70–76.
- Beck, K., Boswell, B. A., Ridgway, C. C., Bachinger, H. P. (1996) Triple helix formation of procollagen type I can occur at the rough endoplasmic reticulum membrane, J. Biol. Chem. 271, 21566–21573.
- Beniash, E., Traub, W., Veis, A., Weiner, S. (2000) A transmission electron microscope study using vitrified ice sections of predentin: structural changes in the dentin collagenous matrix prior to mineralization, J. Struct. Biol. 132, 212–225.
- Bernengo, J. C., Ronziere, M. C., Bezot, P., Bezot, C., Herbage, D., Veis, A. (1983) A hydrodynamic study of collagen fibrillogenesis by electric birefringence and quasielastic light scattering, J. Biol. Chem. 258, 1001–1006.
-
Birk, D. E.,
Linsenmeyer, T. F.
(1994)
Collagen fibril assembly, deposition, and organization into tissue specific matrices, in: Extracellular Matrix Assembly and Structure ( P. D. Yurchenko, D. E. Birk, R. P. Mecham, Eds.), New York: Academic Press,
91–128.
10.1016/B978-0-12-775170-2.50009-3 Google Scholar
- Bornstein, P. (1967) The incomplete hydroxylation of individual prolyl residues in collagen, J. Biol. Chem. 242, 2572–2574.
- Boskey, A. L., Boyan, B. (1996) (Eds.), Proceedings, 5th International Conference on the Chemistry and Biology of Mineralized Tissues, Connect. Tissue Res 35.
- Bourne, G. H., (1956) (Ed.) The Biochemistry and Physiology of Bone, New York: Academic Press.
- Brady, J. D., Robins, S. P. (2001) Structural characterization of pyrrolic cross-links in collagen using a biotinylated Ehrlich's reagent, J. Biol. Chem. 276, 18812–18818.
- Brenner, R. E., Vetter, U., Stoss, H., Muller, P. K., Teller, W. M. (1993) Defective collagen fibril formation and mineralization in osteogenesis imperfecta with congenital joint contractures (Bruck syndrome), Eur. J. Pediatr. 152, 505–508.
- Brownell, A. G., Veis, A. (1975) Intracellular location of the glycosylation of hydrosylysine of collagen, Biochem. Biophys. Res. Commun. 63, 371–377.
- Brownell, A. G., Veis, A. (1976) The intracellular location of triple-helix formation of collagen. Enzyme probe studies, J. Biol. Chem. 251, 7137–7143.
- Bruckner, P., Eikenberry, E. F., Prockop, D. J. (1981) Formation of the triple helix of type I procollagen in cellulo. A kinetic model based on cis-trans isomerization of peptide bonds, Eur. J. Biochem. 118, 607–613.
- Bruns, R. R., Hulmes, D. J., Therrien, S. F., Gross, J. (1979) Procollagen segment-long-spacing crystallites: their role in collagen fibrillogenesis, Proc. Natl. Acad. Sci. USA 76, 313–317.
- Burjanadze, T. V. (1979) Hydroxyproline content and location in relation to collagen thermal stability, Biopolymers 18, 931–938.
- Burjanadze, T. V., Bezhitadze, M. O. (1992) Presence of a thermostable domain in the helical part of the type I collagen molecule and its role in the mechanism of triple helix folding, Biopolymers 32, 951–956.
- Burjanadze, T. V., Veis, A. (1997) A thermodynamic analysis of the contribution of hydroxyproline to the structural stability of the collagen triple helix, Connect. Tissue Res. 36, 347–365.
- Burr, D. B. (2002) The contribution of the organic matrix to bones material properties, Bone 31, 8–11.
- Butler, W. T., Cunningham, L. W. (1966) Evidence for the linkage of a disaccharide to hydroxylysine in tropocollagen, J. Biol. Chem. 241, 3882–3888.
- Butler, W. T. (1985) (Ed.), The Chemistry and Biology of Mineralized Tissues, Birmingham, Ala: Ebsco Media, Inc.
- Dahl, T., Sabsay, B., Veis, A. (1998) Type I collagen-phosphophoryn interactions: specificity of the monomer-monomer binding, J. Struct. Biol. 123, 162–168.
- Diekwisch, T. G. H., Berman, B. J., Gentner, S., Slavkin, H. C. (1995) Initial enamel crystals are not spatially associated with mineralized dentine, Cell Tissue Res. 279, 149–167.
- Farquharson, C., Duncan, A., Seawright, E., Whitehead, C. C., Robins, S. P. (1996) Distribution and quantification of pyridinium cross-links of collagen within the different maturational zones of the chick growth plate, Biochim. Biophys. Acta 1290, 250–256.
- Fisher, L. W., Torchia, D. A., Fohr, B., Young, M. F., Fedarko, N. S. (2001) Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin, Biochem. Biophys. Res. Commun. 280, 460–465.
- Fraser, R. D. B., MacRae, T. P., Miller, A., Suzuki, E. (1983) Molecular conformation and packing in collagen fibrils, J. Mol. Biol. 167, 495–521.
- Fratzl, P., Groschner, M., Vogl, G., Plenk, H., Jr., Eschberger, J., Fratzl-Zelman, N., Koller, K., Klaushofer, K. (1992) Mineral crystals in calcified tissues: a comparative study by SAXS, J. Bone Min. Res. 7, 329–334.
- Fratzl, P., Paris, O., Klaushofer, K., Landis, W. J. (1996) Bone mineralization in an osteogenesis imperfecta mouse model studied by small-angle x-ray scattering, J. Clin. Invest. 97, 396–402.
- George, A., Sabsay, B., Simonian, P. A. L., Veis, A. (1993) Characterization of a novel dentin matrix acidic protein. Implications for biomineralization, J. Biol. Chem. 268, 12624–12630.
- George, A., Bannon, L., Sabsay, B., Dillon, J. W., Malone, J., Veis, A., Jenkins, N. A., Gilbert, D. J., Copeland, N. G. (1996) The carboxyl terminal domain of phosphophoryn contains unique extended triplet amino acid repeat sequences forming ordered carboxyl-phosphate interaction edges which may be essential in the biomineralization process, J. Biol. Chem. 271, 32869–32873.
- Glimcher, M. J. (1976) Composition, structure and organization of bone and other mineralized tissues and the mechanism of calcification, in: Handbook of Physiology-Endocrinology VII, American Physiological Society, Baltimore, MD: Williams & Wilkins Co.
- Glimcher, M. J. (Ed.) (1989) Proceedings, 3rd International Conference on the Chemistry and Biology of Mineralized Tissues, Connect. Tissue Res. 22.
- Glimcher, M. J., Hodge, A. J., Schmitt, F. O. (1957) Macromolecular aggregation states in relation to mineralization: the collagen hydroxyapatite system as studied in vitro, Proc. Natl. Acad. Sci. USA 43, 860–967.
- Goldberg, M., Robinson, C., Boskey, A. L. (2000) (Eds.), Proceedings, 6th International Conference on the Chemistry and Biology of Mineralized Tissues, Vittel France, Rosemont, IL: Orthopaedic Research Soc.
-
Gura, T.,
Hu, G.,
Veis, A.
(1996)
Posttranscriptional aspects of the biosynthesis of type I collagen pro-alpha chains. The effects of posttranslational modifications on synthesis pauses during the elongation of the pro α1(I) chain,
J. Cell. Biochem. 61,
194–215.
10.1002/(SICI)1097-4644(19960501)61:2<194::AID-JCB4>3.0.CO;2-P CAS PubMed Web of Science® Google Scholar
- Hanson, D. A., Eyre, D. R. (1996) Molecular site specificity of pyridinoline and pyrrole cross-links in type I collagen of human bone, J. Biol. Chem. 271, 26508–26516.
- Herring, G. M., Kent, P. W. (1963) Some studies on the muco-substances of bovine cortical bone, Biochem. J. 89, 405–414.
- Hodge, A. J. (1989) Molecular models illustrating the possible distributions of ‘holes' in simple systematically staggered arrays of type I collagen molecules in native-type fibrils, Connect. Tissue Res. 21, 137–147.
- Hofmann, H., Voss, T., Kuhn, K., Engel, J. (1984) Localization of flexible sites in thread-like molecules from electron micrographs. Comparison of interstitial, basement membrane and intima collagens, J. Mol. Biol. 172, 325–343.
- Hu, G., Gura, R., Sabsay, B., Sauk, J., Dixit, S. N., Veis, A. (1995) Endoplasmic reticulum protein hsp47 binds specifically to the n-terminal globular domain of the amino-propeptide of the procollagen I α1(I)-chain, J. Cell. Biochem. 59, 350–367.
- Hulmes, D. J. S., Miller, A. (1979) Quasi-hexagonal packing in collagen fibrils, Nature 282, 878–880.
- Hulmes, D. J., Jesior, J. C., Miller, A., Berthet-Colominas, C., Wolff, C. (1981) Electron microscopy shows periodic structure in collagen fibril cross sections, Proc. Natl. Acad. Sci. USA 78, 3567–3571.
- Hulmes, D. J., Bruns, R. R., Gross, J. (1983) On the state of aggregation of newly secreted procollagen, Proc. Natl. Acad. Sci. USA 80, 388–392.
- Hulmes, D. J., Kadler, K. E., Mould, A. P., Hojima, Y., Holmes, D. F., Cummings, C., Chapman, J. A., Prockop, D. J. (1989) Pleomorphism in type I collagen fibrils produced by persistence of the procollagen N-propeptide, J. Mol. Biol. 210, 337–345.
- Hulmes, D. J. S., Wess, T. J., Prockop, D. J., Fratzl, P. (1995) Radial packing, order, and disorder in collagen fibrils, Biophys. J. 68, 1661–1670.
- Inoue, H., Ozaki, N., Nagasawa, H. (2001) Purification and structural determination of a phosphorylated peptide with anti-calcification and chitin binding activities in the exoskeleton of the crayfish, Procambarus clarkii, Biosci. Biotechnol. Biochem., 65, 1840–1848.
- Jelinski, L. W., Sullivan, C. E., Torchia, D. A. (1980) 2H NMR study of molecular motion in collagen fibrils, Nature 282, 878–880.
- Kadler, K. E., Hojima, Y., Prockop, D. J. (1987) Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical example of an entropy-driven process, J Biol. Chem. 262, 15696–15701.
- Kadler, K. E., Hojima, Y., Prockop, D. J. (1990) Collagen fibrils in vitro grow from pointed tips in the C- to N-terminal direction, Biochem. J. 268, 339–343.
- Katz, E. P., Li, S. T. (1973a) The intermolecular space of reconstituted collagen fibrils, J. Mol. Biol. 73, 351–369.
- Katz, E. P., Li, S. T. (1973b) Structure and function of bone collagen fibrils, J. Mol. Biol. 80, 1–15.
- Katz, E. P., Wachtel, E., Yamauchi, M., Mechanic, G. L. (1989) The structure of mineralized collagen fibrils, Connect. Tissue Res. 21, 149–158.
- Katz, E. P., Billings, E., Yamauchi, M., David, C. (1992) Computer simulations of bone collagen cross-linking patterns, in: Chemistry and Biology of Mineralized Tissues ( H. Slavkin, P. Price, Eds.), Amsterdam: Elsevier Science Publishers, 61–67.
- Kinney, J. H., Oliveira, J., Haupt, D. L., Marshall, G. W., Marshall, S. J. (2002) The spatial arrangement of tubules in human dentin, J. Materials Sci.: Materials Med. 12, 743–751.
- Kivirikko, K. I., Ryhanen, L., Anttinen, H., Bornstein, P., Prockop, D. J. (1973) Further hydroxylation of lysyl residues in collagen by protocollagen lysyl hydroxylase in vitro, Biochemistry 12, 4966–4971.
- Kuypers, R., Tyler, M., Kurth, L. B., Jenkins, I. D., Horgan, D. J. (1992) Identification of the loci of the collagen-associated Ehrlich chromogen in type I collagen confirms its role as a trivalent cross-link, Biochem. J. 283, 129–136.
- Kuznetsova, N., Leikin, S. (1999) Does the triple helical domain of type I collagen encode molecular recognition and fiber assembly while telopeptides serve as catalytic domains? Effect of proteolytic cleavage on fibrillogenesis and on collagen–collagen interaction in fibers, J. Biol. Chem. 274, 36083–36088.
- Lees, S. (1981) A mixed packing model for bone collagen, Calcif. Tissue Int. 33, 591–602.
- Lees, S., Prostak, K. (1988) The locus of mineral crystallites in bone, Connect. Tissue Res. 18, 41–54.
- Landis, W. J. (1995a) Tomographic imaging of collagen–mineral interaction: implications for osteogenesis imperfecta, Connect. Tissue Res. 31, 287–290.
- Landis, W. J. (1995b) The strength of a calcified tissue depends in part on the molecular structure and organization of its constituent mineral crystals in their organic matrix, Bone 16, 533–544.
- Leikina, E., Mertts, M. V., Kuznetsova, N., Leikin, S. (2002) Type I collagen is thermally unstable at body temperature, Proc. Natl. Acad. Sci. USA 99, 1314–1318.
- Lenaers, A., Ansay, M., Nusgens, B. V., Lapiere, C. M. (1971) Collagen made of extended α-chains, procollagen, in genetically-defective dermatosparaxic calves, Eur. J. Biochem. 23, 533–543.
- Levene, C. I. (1966) Plant toxins and human disease. Collagen and lathyrism, Proc. Roy. Soc. Med. 59, 757–758.
- Linde, A., Robins, S. P. (1988) Quantitative assessment of collagen crosslinks in dissected predentin and dentin, Coll. Relat. Res. 8, 443–450.
- Linde, A., Lussi, A., Crenshaw, M. A. (1989) Mineral induction by immobilized polyanionic proteins, Calcif. Tissue Int. 44, 286–295.
- Long, G. C., Thomas, M., Brodsky, B. (1995) Atypical G-X-Y sequences surround the interruptions in the repeating tripeptide pattern of basement membrane collagen, Biopolymers 35, 621–628.
-
Lowenstam, H. A.,
Weiner, S.
(1989)
On Biomineralization, New York: Oxford University Press.
10.1093/oso/9780195049770.001.0001 Google Scholar
- Lussi, A., Crenshaw, M. A., Linde, A. (1988) Induction and inhibition of hydroxyapatite formation by rat dentine phosphoprotein in vitro, Arch. Oral Biol. 33, 685–691.
- Malone, J. P. (2002) Molecular modeling of the conformation of type I collagen amino-telopeptide as docked and cross-linked to its collagen helix receptor domain: implications of telopeptides interactions in fibrillogenesis and biomineralization. Dissertation submitted to the Graduate School, Northwestern University, Evanston, IL in partial fulfillment of the requirements for the PhD degree.
- Miller, A. (1976) Molecular packing in collagen, in: Biochemistry of Collagen ( G. N. Ramachandran, A. H. Reddi, Eds.), New York: Plenum Publishing Corp., 85–136.
- Morgan, P. H., Jacobs, H. G., Segrest, J. P., Cunningham, L. W. (1970) A comparative study of glycopeptides derived from selected vertebrate collagens. A possible role of the carbohydrate in fibril formation, J. Biol. Chem. 245, 5042–5048.
-
Nakahara, H.
(1983)
Calcification of gastropod nacre, in: Biomineralization and Biological Metal Accumulation ( P. Westbroek, E. de Jong, Eds.), Dordrecht, Holland: D. Riedel Publishing Co.,
225–230.
10.1007/978-94-009-7944-4_19 Google Scholar
- Nestler, H., Hvidt, S., Ferry, J., Veis, A. (1983) Flexibility of collagen determined from dilute solution viscoelastic measurements, Biopolymers 22, 1747–1758.
- Otsubo, K., Katz, E. P., Mechanic, G. L., Yamauchi, M. (1992) Cross-linking connectivity in bone collagen fibrils: the COOH-terminal locus of free aldehyde, Biochemistry 31, 396–402.
- Petruska, J. A., Hodge, A. J. (1964) A subunit model for the tropocollagen macromolecule, Proc. Natl. Acad. Sci. USA 51, 871–876.
- Pierard, G. E., Le, T., Hermanns, J. F., Nusgens, B. V., Lapiere, C. M. (1987) Morphometric study of cauliflower collagen fibrils in dermatosparaxis of the calves, Coll. Relat. Res. 6, 481–492.
-
Prockop, D. J.,
Hulmes, D. J. S.
(1994)
Assembly of collagen fibrils de novo from soluble precursors: Polymerization and copolymerization of procollagen, pN-collagen and mutated collagens, in: Extracellular Matrix Assembly and Structure ( P. D. Yurchenko, D. E. Birk, R. P. Mecham, Eds.), New York: Academic Press,
47–90.
10.1016/B978-0-12-775170-2.50008-1 Google Scholar
- Rabie, A. M., Veis, A. (1995) An immunocytochemical study of the routes of secretion of collagen and phosphophoryn from odontoblasts, Connect. Tissue Res. 31, 197–209.
- Rebers, J. E., Riddiford, L. M. (1988) Structure and expression of a Manduca sexta larval cuticle gene homologous to Drosophila cuticle genes, J. Mol. Biol. 203, 411–423.
- Robins, S. P., Duncan, A. (1987) Pyridinium crosslinks of bone collagen and their location in peptides isolated from rat femur, Biochim. Biophys. Acta 914, 233–239.
- Robinson, R. A., Watson, M. L. (1952) Collagen–crystal relationships in bone as seen in the electron microscope, Anat. Rec. 114, 383–409.
- Saito, T., Yamauchi, M., Crenshaw, M. A. (1988) Apatite induction by insoluble dentin collagen, J. Bone Mineral Res. 13, 265–270.
- Saito, T., Arsenault, A. L., Yamauchi, M., Kuboki, Y., Crenshaw, M. A. (1997) Mineral induction by immobilized phosphoproteins, Bone 21, 305–311.
- Saito, T., Yamauchi, M., Abiko, Y., Matsuda, K., Crenshaw, M. A. (2000) In vitro apatite induction by phosphophoryn immobilized on modified collagen fibrils, J. Bone Mineral Res. 15, 1615–1619.
- Sarashina, I., Endo, K. (2001) The complete primary structure of molluscan shell protein 1 (MSP-1), an acidic glycoprotein in the shell matrix of the scallop Patinopecten yessoensis, Mar. Biotechnol. 3, 362–369.
- Sauk, J. J., Smith, T., Norris, K., Ferreira, L. (1994) Hsp47 and the translation-translocation machinery cooperate in the production of alpha 1(I) chains of type I procollagen, J. Biol. Chem. 269, 3941–3946.
- Sfeir, C., Veis, A. (1996) The membrane associated kinases which phosphorylate bone and dentin matrix phosphoproteins are isoforms of cytosolic CKII, Connect. Tissue Res. 35, 215–222.
- Sipilä, L., Szatanik, M., Vainionpaa, H., Ruotsalainen, H., Myllyla, R., Guenet, J. L. (2000) The genes encoding mouse lysyl hydroxylase isoforms map to chromosomes 4,5, and 9, Mammalian Genome 11, 1132–1134.
- Slavkin, H., Price, P. (1992) (Eds.), Chemistry and Biology of Mineralized Tissues, New York: Elsevier Science Publishers.
- Smith, J. W. (1968) Molecular pattern in native collagen, Nature 219, 157–158.
- Somerman, M., Gibson, C. (2003) (Eds.), Proceedings, 7th International Conference on the Chemistry and Biology of Mineralized Tissues, Connect. Tissue Res. (in press).
- Stetler-Stevenson, W. G., Veis, A. (1986) Type I collagen shows a specific binding affinity for bovine dentin phosphophoryn, Calcif. Tissue Int. 38, 135–141.
- Stetler-Stevenson, W. G., Veis, A. (1987) Bovine dentin phosphophoryn: calcium ion binding properties of a high molecular weight preparation, Calcif. Tissue Int. 40, 97–102.
- Stock, S. R., Barss, J., Dahl, T., Veis, A., Almer, J. D. (2002) X-ray absorption microtomography (microCT) and small beam diffraction mapping of sea urchin teeth, J. Struct. Biol. 39, 1–12.
- Torchia, D. A. (1982) Solid-state NMR studies of molecular motion in collagen fibrils, Methods Enzymol. 82, 174–186.
- Traub, W., Arad, T., Weiner, S. (1989) Three-dimensional ordered distribution of crystals in turkey tendon collagen fibers, Proc. Natl. Acad. Sci. USA 86, 9822–9826.
- Traub, W., Jodaikin, A., Arad, T., Veis, A., Sabsay, B. (1992a) Dentin phosphophoryn binding to collagen fibrils, Matrix 12, 197–201.
- Traub, W., Arad, T., Weiner, S. (1992b) Growth of mineral crystals in turkey tendon collagen fibers, Connect. Tissue Res. 28, 99–111.
- Trus, B. L., Piez, K. A. (1980) Compressed microfibril models of the native collagen fibril, Nature 286, 300–301.
- Uzawa, K., Grzesik, W. J., Nishiura, T., Kuznetsov, S. A., Robey, P. G., Brenner, D. A., Yamauchi, M. (1999) Differential expression of human lysyl hydroxylase genes, lysine hydroxylation, and cross-linking of type I collagen during osteoblastic differentiation in vitro, J. Bone Mineral Res. 14, 1272–1280.
- Veis, A. (1981) (Ed.), Chemistry and Biology of Mineralized Connective Tissues, New York: Elsevier North Holland.
- Veis, A. (1982) Collagen fibrillogenesis, Connect. Tissue Res. 1, 11–24
- Veis, A., Brownell, A. G. (1977) Triple-helix formation on ribosome bound nascent chains of procollagen. Deuterium- hydrogen exchange studies, Proc. Natl. Acad. Sci. USA 74, 902–905.
-
Veis, A.,
George, A.
(1994)
Fundamentals of interstitial collagen self-assembly, in: Extracellular Matrix Assembly and Structure ( P. D. Yurchenko, D. E. Birk, R. P. Mecham, Eds.), New York: Academic Press,
15–45.
10.1016/B978-0-12-775170-2.50007-X Google Scholar
- Veis, A., Kirk, T. Z. (1989) The coordinate synthesis and cotranslational assembly of type I procollagen, J. Biol. Chem. 264, 3884–3889.
- Veis, A., Payne, K. (1988) Collagen fibrillogenesis, in: Collagen: Chemistry, Biology and Biotechnology ( M. Nimni, Ed.), Boca Raton, FL: CRC Press, 113–137.
- Veis, A., Schlueter, R. (1963) Presence of phosphate-mediated cross-linkages in hard tissue collagens, Nature 197, 1204.
- Veis, A., Yuan, L. (1975) Structure of the collagen micro-fibril. A four-strand overlap model, Biopolymers 14, 895–900.
- Veis, A., Anesey, J., Mussell, S. (1967) A limiting microfibril model for the three-dimensional arrangement within collagen fibers, Nature 215, 931–934.
- Veis, A., Leibovich, S. J., Evans, J., Kirk, T. Z. (1985) Supramolecular assemblies of mRNA direct the coordinated synthesis of type I procollagen chains, Proc. Natl. Acad. Sci. USA 82, 3693–3697.
- Veis, D. J., Albinger, T. M., Clohisy, J., Rahima, M., Sabsay, B., Veis, A. (1986) Matrix proteins of the teeth of the sea urchin: Lytechinus variegatus, J. Exp. Zool. 240, 35–46.
- Veis, A., Wei, K., Sfeir, C., George, A., Malone, J. (1998) The properties of the (DSS)n triplet repeat domain of rat dentin phosphophoryn, Eur. J. Oral Sci. 106 (Suppl. 1), 234–238.
- Veis, A., Dahl, T., Sabsay, B. (2000) The specificity of phosphophoryn-collagen I interactions, in: Proceedings, 6th International Conference on the Chemistry and Biology of Mineralized Tissues, Vittel, France (Goldberg, M., Robinson, C., Boskey, A., Eds.). Rosemont, IL: Orthopaedic Research Society, 169–173.
- Veis, A., Barss, J., Dahl, T., Rahima, M., Stock, S. (2002) Mineral-related proteins of the sea urchin teeth: Lytechinus variegatus, Microsc. Res. Techn. 59, 341–352.
- Venugopal, M. G., Ramshaw, J. A. M., Braswell, E., Zuh, D., Brodsky, B. (1994) Electrostatic interactions in collagen-like triple-helical peptides, Biochemistry 33, 7948–7956.
- Wang, R. Z., Addadi, L., Weiner, S. (1997) Design strategies of sea urchin teeth: structure, composition, and micromechanical relations to function, Philos. Trans. R. Soc Lond. B. 352, 469–480.
- Weiner, S., Hood, L. (1975) Soluble protein of the organic matrix of mollusk shells: a potential template for shell formation, Science 190, 987–989.
- Weiner, S., Arad, T., Traub, W. (1991) Crystal organization in rat bone lamellae, FEBS Lett. 285, 49–54.
- Weiner, S., Arad, T., Sabanay, I., Traub, W. (1997) Rotated plywood structure of primary lamellar bone in the rat: orientations of the collagen fibril arrays, Bone 20, 509–514.
- Weiner, S., Traub, W., Wagner, H. D. (1999a) Lamellar bone: structure–function relations, J Struct. Biol. 126, 241–255.
- Weiner, S., Veis, A., Beniash, E., Arad, T, Dillon, J. W., Sabsay, B., Siddiqui, F. (1999b) Peritubular dentin formation: crystal organization and the macromolecular constituents in human teeth, J. Struct. Biol. 126, 27–41.
- Weinstock, M., Leblond, C. P. (1974) Synthesis, migration, and release of precursor collagen by odontoblasts as visualized by radioautography after (3H) proline administration, J. Cell Biol. 60, 92–127.
- Wess, T. J., Hammersley, A., Wess, L., Miller, A. (1995) Type I collagen packing, conformation of the triclinic unit cell, J. Mol. Biol. 248, 487–493.
- Woodhead-Galloway, J., Machin, P. A. (1976) Modern theories of liquids and the diffuse equatorial x-ray scattering from collagen, Acta Crystallogr. 32, 368–372.
- Wu, C. B., Pelech, S. L., Veis, A. (1992) The in vitro phosphorylation of the native rat incisor dentin phosphophoryns, J. Biol. Chem. 267, 16588–16594.
- Yamauchi, M., Banes, A. J., Kuboki, Y., Mechanic, G. L. (1981) A comparative study of the distribution of the stable crosslink, pyridinoline, in bone collagens from normal, osteoblastoma, and vitamin D-deficient chicks, Biochem. Biophy. Res. Commun. 102, 59–65.
- Yamauchi, M., Young, D. R., Chandler, G. S., Mechanic, G. L. (1988) Cross-linking and new bone collagen synthesis in immobilized and recovering primate osteoporosis, Bone 9, 415–418.
- Yamauchi, M., Katz, E. P., Otsubo, K., Teraoka, K., Mechanic, G. L. (1989) Cross-linking and stereospecific structure of collagen in mineralized and nonmineralized skeletal tissues, Connect. Tissue Res. 21, 159–167.
- Yamauchi, M., Chandler, G. S., Katz, E. P. (1992) Collagen cross-linking and mineralization, in: Chemistry and Biology of Mineralized Tissues ( H. Slavkin, P. Price, Eds.), New York: Elsevier Science Publishers, 39–46.
- Zylberberg, L., Traub, W., de Buffrenil, V., Allizard, F., Arad, T., Weiner, S. (1998) Rostrum of a toothed whale: ultrastructural study of a very dense bone, Bone 23, 241–247.
Biopolymers Online: Biology • Chemistry • Biotechnology • Applications
Browse other articles of this reference work:
